ID L1CAM_HUMAN Reviewed; 1257 AA. AC P32004; A0AV65; A4ZYW4; B2RMU7; G3XAF4; Q8TA87; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 27-MAR-2024, entry version 240. DE RecName: Full=Neural cell adhesion molecule L1; DE Short=N-CAM-L1; DE Short=NCAM-L1; DE AltName: CD_antigen=CD171; DE Flags: Precursor; GN Name=L1CAM; Synonyms=CAML1, MIC5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=1932117; DOI=10.1016/0167-4781(91)90108-x; RA Kobayashi M., Miura M., Asou H., Uyemura K.; RT "Molecular cloning of cell adhesion molecule L1 from human nervous tissue: RT a comparison of the primary sequences of L1 molecules of different RT origin."; RL Biochim. Biophys. Acta 1090:238-240(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=1769655; DOI=10.1016/0888-7543(91)90150-d; RA Hlavin M.L., Lemmon V.; RT "Molecular structure and functional testing of human L1CAM: an interspecies RT comparison."; RL Genomics 11:416-423(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=1627459; DOI=10.1007/bf02919404; RA Reid R.A., Hemperly J.J.; RT "Variants of human L1 cell adhesion molecule arise through alternate RT splicing of RNA."; RL J. Mol. Neurosci. 3:127-135(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9286695; DOI=10.1006/geno.1997.4822; RA Brenner V., Nyakatura G., Rosenthal A., Platzer M.; RT "Genomic organization of two novel genes on human Xq28: compact head to RT head arrangement of IDH gamma and TRAP delta is conserved in rat and RT mouse."; RL Genomics 44:8-14(1997). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RX PubMed=9479034; DOI=10.1016/s0378-1119(97)00614-8; RA Coutelle O., Nyakatura G., Taudien S., Elgar G., Brenner S., Platzer M., RA Drescher B., Jouet M., Kenwrick S., Rosenthal A.; RT "The neural cell adhesion molecule L1: genomic organisation and RT differential splicing is conserved between man and the pufferfish Fugu."; RL Gene 208:7-15(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Son Y.S.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PROTEIN SEQUENCE OF 20-36. RX PubMed=3136168; DOI=10.1016/s0021-9258(18)37877-3; RA Wolff J.M., Frank R., Mujoo K., Spiro R.C., Reisfeld R.A., Rathjen F.G.; RT "A human brain glycoprotein related to the mouse cell adhesion molecule RT L1."; RL J. Biol. Chem. 263:11943-11947(1988). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-371. RX PubMed=2387585; DOI=10.1016/0888-7543(90)90203-7; RA Djabali M., Mattei M.-G., Nguyen C., Roux D., Demengeot J., Denizot F., RA Moos M., Schachner M., Goridis C., Jordan B.R.; RT "The gene encoding L1, a neural adhesion molecule of the immunoglobulin RT family, is located on the X chromosome in mouse and man."; RL Genomics 7:587-593(1990). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 353-1176, AND NUCLEOTIDE SEQUENCE [GENOMIC RP DNA] OF 1082-1176. RC TISSUE=Fetal brain; RX PubMed=1923824; DOI=10.1093/nar/19.19.5395; RA Rosenthal A., Mackinnon R.N., Jones D.S.C.; RT "PCR walking from microdissection clone M54 identifies three exons from the RT human gene for the neural cell adhesion molecule L1 (CAM-L1)."; RL Nucleic Acids Res. 19:5395-5401(1991). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1030-1257. RX PubMed=1993895; DOI=10.1111/j.1471-4159.1991.tb01994.x; RA Harper J.R., Prince J.T., Healy P.A., Stuart J.K., Nauman S.J., RA Stallcup W.B.; RT "Isolation and sequence of partial cDNA clones of human L1: homology of RT human and rodent L1 in the cytoplasmic region."; RL J. Neurochem. 56:797-804(1991). RN [14] RP PHOSPHORYLATION AT SER-1181. RX PubMed=8592152; DOI=10.1046/j.1471-4159.1996.66020779.x; RA Wong E.V., Schaefer A.W., Landreth G., Lemmon V.; RT "Casein kinase II phosphorylates the neural cell adhesion molecule L1."; RL J. Neurochem. 66:779-786(1996). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-671. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1163, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-671. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [19] RP INVOLVEMENT IN L1 SYNDROME, VARIANTS 26-TYR--GLU-1257 DEL; ASN-37; MET-38; RP 66-GLN--GLU-1257 DEL; 109-GLN--GLU-1257 DEL; 133-GLU--GLU-1257 DEL; RP 138-TRP--GLU-1257 DEL; ILE-172; GLY-184; 187-MET--VAL-198 DEL; ASP-254; RP ARG-276; PRO-313; 366-TRP--GLU-1257 DEL; LYS-369; 423-GLN--GLU-1257 DEL; RP ARG-480; ASN-516; TYR-516; HIS-525; MET-627; PRO-645; 662-TRP--GLU-1257 RP DEL; SER-714; ARG-754; 760-ARG--GLU-1257 DEL; 789-GLN--GLU-1257 DEL; RP 811-TYR--GLU-1257 DEL; 891-TYR--GLU-1257 DEL; 901-ARG--GLU-1257 DEL; RP 1064-SER--GLU-1257 DEL; ASN-1071 DEL AND GLN-1080, VARIANTS MASA SER-179; RP TYR-202; ARG-335 AND MET-752, AND VARIANTS HYCX SER-179; GLN-184; ARG-335; RP PRO-415 AND MET-752. RX PubMed=19846429; DOI=10.1136/jmg.2009.071688; RA Vos Y.J., de Walle H.E., Bos K.K., Stegeman J.A., Ten Berge A.M., RA Bruining M., van Maarle M.C., Elting M.W., den Hollander N.S., Hamel B., RA Fortuna A.M., Sunde L.E., Stolte-Dijkstra I., Schrander-Stumpel C.T., RA Hofstra R.M.; RT "Genotype-phenotype correlations in L1 syndrome: a guide for genetic RT counselling and mutation analysis."; RL J. Med. Genet. 47:169-175(2010). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-1177 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-1172 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177 (ISOFORM 2), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1172 (ISOFORM 3), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [23] RP INVOLVEMENT IN L1 SYNDROME, VARIANTS CYS-635 AND ILE-768, AND RP GLYCOSYLATION. RX PubMed=22222883; DOI=10.1007/s10048-011-0307-4; RA Marx M., Diestel S., Bozon M., Keglowich L., Drouot N., Bouche E., RA Frebourg T., Minz M., Saugier-Veber P., Castellani V., Schaefer M.K.; RT "Pathomechanistic characterization of two exonic L1CAM variants located in RT trans in an obligate carrier of X-linked hydrocephalus."; RL Neurogenetics 13:49-59(2012). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] RP VARIANT HYCX TYR-264. RX PubMed=8401576; DOI=10.1038/ng0893-331; RA Jouet M., Rosenthal A., Macfarlane J., Kenwrick S., Donnai D.; RT "A missense mutation confirms the L1 defect in X-linked hydrocephalus RT (HSAS)."; RL Nat. Genet. 4:331-331(1993). RN [26] RP VARIANT HYCX LEU-1194, AND VARIANT MASA LEU-1194. RX PubMed=7881431; DOI=10.1093/hmg/3.12.2255; RA Fransen E., Schrander-Stumpel C., Vits L., Coucke P., van Camp G., RA Willems P.J.; RT "X-linked hydrocephalus and MASA syndrome present in one family are due to RT a single missense mutation in exon 28 of the L1CAM gene."; RL Hum. Mol. Genet. 3:2255-2256(1994). RN [27] RP INVOLVEMENT IN MASA, INVOLVEMENT IN HYCX, VARIANTS HYCX GLN-184 AND RP ARG-452, AND VARIANT MASA GLN-210. RX PubMed=7920659; DOI=10.1038/ng0794-402; RA Jouet M., Rosenthal A., Armstrong G., Macfarlane J., Stevenson R., RA Paterson J., Metzenberg A., Ionasescu V., Temple K., Kenwrick S.; RT "X-linked spastic paraplegia (SPG1), MASA syndrome and X-linked RT hydrocephalus result from mutations in the L1 gene."; RL Nat. Genet. 7:402-407(1994). RN [28] RP VARIANTS MASA GLN-210 AND ASN-598. RX PubMed=7920660; DOI=10.1038/ng0794-408; RA Vits L., van Camp G., Coucke P., Fransen E., de Boulle K., Reyniers E., RA Korn B., Poustka A., Wilson G., Schrander-Stumpel C., Winter R.M., RA Schwartz C., Willems P.J.; RT "MASA syndrome is due to mutations in the neural cell adhesion gene RT L1CAM."; RL Nat. Genet. 7:408-413(1994). RN [29] RP VARIANTS MASA LYS-309 AND LEU-941, AND VARIANTS HYCX SER-9; SER-121; RP PHE-768; LEU-941 AND CYS-1070. RX PubMed=7762552; RA Jouet M., Moncla A., Paterson J., McKeown C., Fryer A., Carpenter N., RA Holmberg E., Wadelius C., Kenwrick S.; RT "New domains of neural cell-adhesion molecule L1 implicated in X-linked RT hydrocephalus and MASA syndrome."; RL Am. J. Hum. Genet. 56:1304-1314(1995). RN [30] RP VARIANTS HYCX GLN-184; TYR-264; ARG-452 AND LEU-1194, AND VARIANTS MASA RP GLN-210; ASN-598 AND LEU-1194. RX PubMed=8556302; DOI=10.1159/000472311; RA Fransen E., Lemmon V., van Camp G., Vits L., Coucke P., Willems P.J.; RT "CRASH syndrome: clinical spectrum of corpus callosum hypoplasia, RT retardation, adducted thumbs, spastic paraparesis and hydrocephalus due to RT mutations in one single gene, L1."; RL Eur. J. Hum. Genet. 3:273-284(1995). RN [31] RP ERRATUM OF PUBMED:8556302. RA Fransen E., Lemmon V., van Camp G., Vits L., Coucke P., Willems P.J.; RL Eur. J. Hum. Genet. 4:126-126(1996). RN [32] RP INVOLVEMENT IN MASA, INVOLVEMENT IN HYCX, VARIANTS HYCX SER-179 AND RP ARG-370, AND VARIANTS MASA SER-179 AND ARG-370. RX PubMed=7562969; DOI=10.1136/jmg.32.7.549; RA Ruiz J.C., Cuppens H., Legius E., Fryns J.-P., Glover T., Marynen P., RA Cassiman J.-J.; RT "Mutations in L1-CAM in two families with X linked complicated spastic RT paraplegia, MASA syndrome, and HSAS."; RL J. Med. Genet. 32:549-552(1995). RN [33] RP VARIANT HYCX GLU-655. RX PubMed=9118141; DOI=10.1007/bf00261591; RA Izumoto S., Yamasaki M., Arita N., Hiraga S., Ohnishi T., Fujitani K., RA Sakoda S., Hayakawa T.; RT "A new mutation of the L1CAM gene in an X-linked hydrocephalus family."; RL Childs Nerv. Syst. 12:742-747(1996). RN [34] RP VARIANTS HYCX CYS-194 AND LEU-240. RX PubMed=8929944; DOI=10.1136/jmg.33.2.103; RA Gu S.-M., Orth U., Veske A., Enders H., Kluender K., Schloesser M., RA Engel W., Schwinger E., Gal A.; RT "Five novel mutations in the L1CAM gene in families with X linked RT hydrocephalus."; RL J. Med. Genet. 33:103-106(1996). RN [35] RP VARIANT MASA PRO-482, VARIANTS HYCX SER-526 DEL; PRO-542 AND THR-741, RP VARIANT HYCX/MASA MET-752, AND VARIANT ILE-768. RX PubMed=9268105; RX DOI=10.1002/(sici)1096-8628(19970822)71:3<336::aid-ajmg15>3.0.co;2-l; RA Gu S.-M., Orth U., Zankl M., Schroeder J., Gal A.; RT "Molecular analysis of the L1CAM gene in patients with X-linked RT hydrocephalus demonstrates eight novel mutations and suggests non-allelic RT heterogeneity of the trait."; RL Am. J. Med. Genet. 71:336-340(1997). RN [36] RP VARIANTS MASA ASP-268 AND ASP-426. RX PubMed=9300653; DOI=10.1093/hmg/6.10.1625; RA Fransen E., Van Camp G., Vits L., Willems P.J.; RT "L1-associated diseases: clinical geneticists divide, molecular geneticists RT unite."; RL Hum. Mol. Genet. 6:1625-1632(1997). RN [37] RP VARIANTS HYCX GLN-184; 439-VAL--THR-443 DEL; CYS-784 AND 936-LEU--LEU-948 RP DEL. RX PubMed=9195224; RX DOI=10.1002/(sici)1098-1004(1997)9:6<512::aid-humu3>3.0.co;2-3; RA Macfarlane J.R., Du J.-S., Pepys M.E., Ramsden S., Donnai D., Charlton R., RA Garrett C., Tolmie J., Yates J.R.W., Berry C., Goudie D., Moncla A., RA Lunt P., Hodgson S., Jouet M., Kenwrick S.; RT "Nine novel L1 CAM mutations in families with X-linked hydrocephalus."; RL Hum. Mutat. 9:512-518(1997). RN [38] RP VARIANTS MASA ASP-691 AND ARG-698, AND VARIANTS HYCX ARG-698 AND PRO-935. RX PubMed=9521424; RX DOI=10.1002/(sici)1098-1004(1998)11:3<222::aid-humu7>3.0.co;2-j; RA Du Y.-Z., Srivastava A.K., Schwartz C.E.; RT "Multiple exon screening using restriction endonuclease fingerprinting RT (REF): detection of six novel mutations in the L1 cell adhesion molecule RT (L1CAM) gene."; RL Hum. Mutat. 11:222-230(1998). RN [39] RP VARIANT MASA PRO-632. RX PubMed=9452110; DOI=10.1002/humu.1380110189; RA Vits L., Chitayat D., van Camp G., Holden J.J.A., Fransen E., Willems P.J.; RT "Evidence for somatic and germline mosaicism in CRASH syndrome."; RL Hum. Mutat. Suppl. 1:S284-S287(1998). RN [40] RP VARIANTS MASA ARG-335 AND CYS-473, AND VARIANTS HYCX THR-219; ARG-335; RP CYS-386; CYS-473 AND LEU-1224. RX PubMed=9744477; RX DOI=10.1002/(sici)1098-1004(1998)12:4<259::aid-humu7>3.0.co;2-a; RA Saugier-Veber P., Martin C., le Meur N., Lyonnet S., Munnich A., David A., RA Henocq A., Heron D., Jonveaux P., Odent S., Manouvrier S., Moncla A., RA Morichon N., Philip N., Satge D., Tosi M., Frebourg T.; RT "Identification of novel L1CAM mutations using fluorescence-assisted RT mismatch analysis."; RL Hum. Mutat. 12:259-266(1998). RN [41] RP VARIANTS HYCX CYS-674; ASP-691 AND ARG-698. RX PubMed=9832035; DOI=10.1136/jmg.35.11.901; RA Michaelis R.C., Du Y.-Z., Schwartz C.E.; RT "The site of a missense mutation in the extracellular Ig or FN domains of RT L1CAM influences infant mortality and the severity of X linked RT hydrocephalus."; RL J. Med. Genet. 35:901-904(1998). RN [42] RP VARIANTS HYCX TRP-184; CYS-335; ILE-408; ASP-421; TYR-497; THR-691 AND RP PRO-751, VARIANTS ASN-30; TRP-739 AND GLU-1239, AND VARIANT HYCX/MASA RP ARG-370. RX PubMed=10797421; RX DOI=10.1002/(sici)1096-8628(20000501)92:1<40::aid-ajmg7>3.0.co;2-r; RA Finckh U., Schroeder J., Ressler B., Veske A., Gal A.; RT "Spectrum and detection rate of L1CAM mutations in isolated and familial RT cases with clinically suspected L1-disease."; RL Am. J. Med. Genet. 92:40-46(2000). RN [43] RP VARIANT MASA TYR-202. RX PubMed=10805190; DOI=10.1177/088307380001500407; RA Sztriha L., Frossard P., Hofstra R.M., Verlind E., Nork M.; RT "Novel missense mutation in the L1 gene in a child with corpus callosum RT agenesis, retardation, adducted thumbs, spastic paraparesis, and RT hydrocephalus."; RL J. Child Neurol. 15:239-243(2000). RN [44] RP VARIANT HYCX/MASA MET-752, AND POSSIBLE INVOLVEMENT IN HIRSCHSPRUNG RP DISEASE. RX PubMed=11857550; DOI=10.1002/ajmg.10185; RA Parisi M.A., Kapur R.P., Neilson I., Hofstra R.M.W., Holloway L.W., RA Michaelis R.C., Leppig K.A.; RT "Hydrocephalus and intestinal aganglionosis: is L1CAM a modifier gene in RT Hirschsprung disease?"; RL Am. J. Med. Genet. 108:51-56(2002). RN [45] RP VARIANT HYCX PRO-415. RX PubMed=12435569; DOI=10.1016/s0887-8994(02)00440-x; RA Sztriha L., Vos Y.J., Verlind E., Johansen J., Berg B.; RT "X-linked hydrocephalus: a novel missense mutation in the L1CAM gene."; RL Pediatr. Neurol. 27:293-296(2002). RN [46] RP CHARACTERIZATION OF VARIANT HYCX TYR-264, SUBCELLULAR LOCATION, AND RP GLYCOSYLATION. RX PubMed=12514225; DOI=10.1523/jneurosci.23-01-00277.2003; RA Ruenker A.E., Bartsch U., Nave K.A., Schachner M.; RT "The C264Y missense mutation in the extracellular domain of L1 impairs RT protein trafficking in vitro and in vivo."; RL J. Neurosci. 23:277-286(2003). RN [47] RP VARIANT ACCPX LEU-240. RX PubMed=16650080; DOI=10.1111/j.1399-0004.2006.00607.x; RA Basel-Vanagaite L., Straussberg R., Friez M.J., Inbar D., Korenreich L., RA Shohat M., Schwartz C.E.; RT "Expanding the phenotypic spectrum of L1CAM-associated disease."; RL Clin. Genet. 69:414-419(2006). RN [48] RP VARIANT MASA ASN-770. RX PubMed=16816908; DOI=10.1007/s10072-006-0610-2; RA Simonati A., Boaretto F., Vettori A., Dabrilli P., Criscuolo L., RA Rizzuto N., Mostacciuolo M.L.; RT "A novel missense mutation in the L1CAM gene in a boy with L1 disease."; RL Neurol. Sci. 27:114-117(2006). RN [49] RP CHARACTERIZATION OF VARIANTS HYCX GLN-184 AND LEU-1036, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=20621658; DOI=10.1016/j.nbd.2010.05.029; RA Schaefer M.K., Nam Y.C., Moumen A., Keglowich L., Bouche E., Kueffner M., RA Bock H.H., Rathjen F.G., Raoul C., Frotscher M.; RT "L1 syndrome mutations impair neuronal L1 function at different levels by RT divergent mechanisms."; RL Neurobiol. Dis. 40:222-237(2010). RN [50] RP VARIANT HYCX ARG-698. RX PubMed=22344793; DOI=10.1002/ajmg.a.35244; RA Fernandez R.M., Nunez-Torres R., Garcia-Diaz L., de Agustin J.C., RA Antinolo G., Borrego S.; RT "Association of X-linked hydrocephalus and Hirschsprung disease: Report of RT a new patient with a mutation in the L1CAM gene."; RL Am. J. Med. Genet. A 158:816-820(2012). RN [51] RP CHARACTERIZATION OF VARIANTS MASA GLN-210 AND LYS-309, CHARACTERIZATION OF RP VARIANTS HYCX THR-219 AND CYS-264, CHARACTERIZATION OF VARIANT HYCX/MASA RP LEU-941, AND SUBCELLULAR LOCATION. RX PubMed=22973895; DOI=10.1111/jnc.12015; RA Tagliavacca L., Colombo F., Racchetti G., Meldolesi J.; RT "L1CAM and its cell-surface mutants: new mechanisms and effects relevant to RT the physiology and pathology of neural cells."; RL J. Neurochem. 124:397-409(2013). RN [52] RP CHARACTERIZATION OF VARIANT VAL-120, CHARACTERIZATION OF VARIANTS MASA RP GLN-210 AND LYS-309, CHARACTERIZATION OF VARIANTS HYCX GLN-184; TYR-264 AND RP CYS-1070, AND MUTAGENESIS OF 1147-LYS--VAL-1153. RX PubMed=24155914; DOI=10.1371/journal.pone.0076974; RA Kudumala S., Freund J., Hortsch M., Godenschwege T.A.; RT "Differential effects of human L1CAM mutations on complementing guidance RT and synaptic defects in Drosophila melanogaster."; RL PLoS ONE 8:E76974-E76974(2013). RN [53] RP VARIANT 789-GLN--GLU-1257 DEL, CHARACTERIZATION OF VARIANTS ASN-37; MET-38 RP AND ILE-172, CHARACTERIZATION OF VARIANT MASA TYR-202, AND SUBCELLULAR RP LOCATION. RX PubMed=26891472; DOI=10.1111/cge.12763; RA Christaller W.A., Vos Y., Gebre-Medhin S., Hofstra R.M., Schaefer M.K.; RT "L1 syndrome diagnosis complemented with functional analysis of L1CAM RT variants located to the two N-terminal Ig-like domains."; RL Clin. Genet. 91:115-120(2017). CC -!- FUNCTION: Neural cell adhesion molecule involved in the dynamics of CC cell adhesion and in the generation of transmembrane signals at CC tyrosine kinase receptors. During brain development, critical in CC multiple processes, including neuronal migration, axonal growth and CC fasciculation, and synaptogenesis. In the mature brain, plays a role in CC the dynamics of neuronal structure and function, including synaptic CC plasticity. {ECO:0000269|PubMed:20621658, ECO:0000305}. CC -!- SUBUNIT: Interacts with SHTN1; the interaction occurs in axonal growth CC cones (By similarity). Interacts with isoform 2 of BSG (By similarity). CC {ECO:0000250|UniProtKB:P11627, ECO:0000250|UniProtKB:Q05695}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12514225, CC ECO:0000269|PubMed:20621658, ECO:0000269|PubMed:22973895, CC ECO:0000269|PubMed:26891472}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q05695}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:Q05695}. Cell projection, axon CC {ECO:0000269|PubMed:20621658}. Cell projection, dendrite. CC Note=Colocalized with SHTN1 in close apposition with actin filaments in CC filopodia and lamellipodia of axonalne growth cones of hippocampal CC neurons (By similarity). In neurons, detected predominantly in axons CC and cell body, weak localization to dendrites (PubMed:20621658). CC {ECO:0000250|UniProtKB:Q05695, ECO:0000269|PubMed:20621658}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P32004-1; Sequence=Displayed; CC Name=2; CC IsoId=P32004-2; Sequence=VSP_002591; CC Name=3; CC IsoId=P32004-3; Sequence=VSP_046317, VSP_002591; CC -!- DISEASE: Hydrocephalus, congenital, X-linked (HYCX) [MIM:307000]: An X- CC linked recessive form of congenital hydrocephalus, a disease CC characterized by in utero onset of enlarged ventricles due to CC accumulation of ventricular cerebrospinal fluid. HYCX is the most CC common inherited form and occurs in approximately 1/30000 male births. CC The primary diagnostic criteria of intellectual disability and enlarged CC cerebral ventricles are often accompanied by spastic paraparesis and CC adducted thumbs and, occasionally, visual defects or seizures. The most CC severe cases die pre- or perinatally with gross hydrocephalus and CC enlarged head circumference. Stenosis of the aqueduct of Sylvius is CC frequently associated with the disorder. {ECO:0000269|PubMed:10797421, CC ECO:0000269|PubMed:11857550, ECO:0000269|PubMed:12435569, CC ECO:0000269|PubMed:12514225, ECO:0000269|PubMed:19846429, CC ECO:0000269|PubMed:20621658, ECO:0000269|PubMed:22344793, CC ECO:0000269|PubMed:22973895, ECO:0000269|PubMed:24155914, CC ECO:0000269|PubMed:7562969, ECO:0000269|PubMed:7762552, CC ECO:0000269|PubMed:7881431, ECO:0000269|PubMed:7920659, CC ECO:0000269|PubMed:8401576, ECO:0000269|PubMed:8556302, CC ECO:0000269|PubMed:8929944, ECO:0000269|PubMed:9118141, CC ECO:0000269|PubMed:9195224, ECO:0000269|PubMed:9268105, CC ECO:0000269|PubMed:9521424, ECO:0000269|PubMed:9744477, CC ECO:0000269|PubMed:9832035}. Note=The disease is caused by variants CC affecting the gene represented in this entry. L1CAM mutations have also CC been found in few patients affected by hydrocephalus with Hirschsprung CC disease, suggesting a role of this gene acting either in a direct or CC indirect way in the pathogenesis of Hirschsprung disease CC (PubMed:22344793). {ECO:0000269|PubMed:22344793}. CC -!- DISEASE: MASA syndrome (MASA) [MIM:303350]: An X-linked recessive CC syndrome with a highly variable clinical spectrum. Main clinical CC features include spasticity and hyperreflexia of lower limbs, shuffling CC gait, intellectual disability, aphasia and adducted thumbs. The CC features of spasticity have been referred to as complicated spastic CC paraplegia type 1 (SPG1). Some patients manifest corpus callosum CC hypoplasia and hydrocephalus. Inter- and intrafamilial variability is CC very wide, such that patients with hydrocephalus, MASA, SPG1, and CC agenesis of corpus callosum can be present within the same family. CC {ECO:0000269|PubMed:10797421, ECO:0000269|PubMed:10805190, CC ECO:0000269|PubMed:11857550, ECO:0000269|PubMed:16816908, CC ECO:0000269|PubMed:19846429, ECO:0000269|PubMed:22344793, CC ECO:0000269|PubMed:22973895, ECO:0000269|PubMed:24155914, CC ECO:0000269|PubMed:26891472, ECO:0000269|PubMed:7562969, CC ECO:0000269|PubMed:7762552, ECO:0000269|PubMed:7881431, CC ECO:0000269|PubMed:7920659, ECO:0000269|PubMed:7920660, CC ECO:0000269|PubMed:8556302, ECO:0000269|PubMed:9268105, CC ECO:0000269|PubMed:9300653, ECO:0000269|PubMed:9452110, CC ECO:0000269|PubMed:9521424, ECO:0000269|PubMed:9744477, CC ECO:0000269|PubMed:9832035}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Note=Defects in L1CAM may contribute to Hirschsprung disease CC by modifying the effects of Hirschsprung disease-associated genes to CC cause intestinal aganglionosis. {ECO:0000269|PubMed:11857550}. CC -!- DISEASE: Agenesis of the corpus callosum, X-linked, partial (ACCPX) CC [MIM:304100]: A syndrome characterized by partial corpus callosum CC agenesis, hypoplasia of inferior vermis and cerebellum, intellectual CC disability, seizures and spasticity. Other features include CC microcephaly, unusual facies, and Hirschsprung disease in some CC patients. {ECO:0000269|PubMed:16650080}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Note=Defects in L1CAM are associated with a wide phenotypic CC spectrum which varies from severe hydrocephalus and prenatal death CC (HYCX) to a milder phenotype (MASA). These variations may even occur CC within the same family. Due to the overlap of phenotypes between HYCX CC and MASA, many authors use the general concept of L1 syndrome which CC covers both ends of the spectrum. {ECO:0000269|PubMed:19846429, CC ECO:0000269|PubMed:22222883, ECO:0000269|PubMed:26891472}. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CC L1/neurofascin/NgCAM family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44110/L1CAM"; CC -!- WEB RESOURCE: Name=L1CAM; Note=L1CAM mutation Web Page; CC URL="http://www.l1cammutationdatabase.info/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59847; CAA42508.1; -; mRNA. DR EMBL; M77640; AAC14352.1; -; mRNA. DR EMBL; M74387; AAA59476.1; -; mRNA. DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z29373; CAA82564.1; -; Genomic_DNA. DR EMBL; EF506611; ABP88252.1; -; mRNA. DR EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471172; EAW72787.1; -; Genomic_DNA. DR EMBL; BC025843; AAH25843.1; -; mRNA. DR EMBL; BC126229; AAI26230.1; -; mRNA. DR EMBL; BC136447; AAI36448.1; -; mRNA. DR EMBL; M55271; AAA36353.1; ALT_SEQ; mRNA. DR EMBL; X58775; CAA41576.1; -; Genomic_DNA. DR EMBL; X58776; CAB37831.1; -; mRNA. DR CCDS; CCDS14733.1; -. [P32004-1] DR CCDS; CCDS14734.1; -. [P32004-2] DR CCDS; CCDS48192.1; -. [P32004-3] DR PIR; A41060; A41060. DR RefSeq; NP_000416.1; NM_000425.4. [P32004-1] DR RefSeq; NP_001137435.1; NM_001143963.2. [P32004-3] DR RefSeq; NP_001265045.1; NM_001278116.1. [P32004-1] DR RefSeq; NP_076493.1; NM_024003.3. [P32004-2] DR PDB; 8AFO; X-ray; 1.99 A; A=712-917. DR PDB; 8AFP; X-ray; 3.00 A; A=712-917. DR PDBsum; 8AFO; -. DR PDBsum; 8AFP; -. DR AlphaFoldDB; P32004; -. DR SASBDB; P32004; -. DR SMR; P32004; -. DR BioGRID; 110094; 61. DR CORUM; P32004; -. DR ELM; P32004; -. DR IntAct; P32004; 13. DR MINT; P32004; -. DR STRING; 9606.ENSP00000359077; -. DR BindingDB; P32004; -. DR ChEMBL; CHEMBL5169129; -. DR DrugBank; DB00898; Ethanol. DR TCDB; 8.A.23.1.62; the basigin (basigin) family. DR GlyConnect; 1547; 18 N-Linked glycans (4 sites). DR GlyCosmos; P32004; 21 sites, 21 glycans. DR GlyGen; P32004; 22 sites, 20 N-linked glycans (4 sites), 1 O-linked glycan (1 site). DR iPTMnet; P32004; -. DR PhosphoSitePlus; P32004; -. DR SwissPalm; P32004; -. DR BioMuta; L1CAM; -. DR DMDM; 1705571; -. DR EPD; P32004; -. DR jPOST; P32004; -. DR MassIVE; P32004; -. DR MaxQB; P32004; -. DR PaxDb; 9606-ENSP00000359077; -. DR PeptideAtlas; P32004; -. DR ProteomicsDB; 33733; -. DR ProteomicsDB; 54830; -. [P32004-1] DR ProteomicsDB; 54831; -. [P32004-2] DR Pumba; P32004; -. DR ABCD; P32004; 16 sequenced antibodies. DR Antibodypedia; 449; 1405 antibodies from 46 providers. DR DNASU; 3897; -. DR Ensembl; ENST00000361699.8; ENSP00000355380.4; ENSG00000198910.14. [P32004-2] DR Ensembl; ENST00000361981.7; ENSP00000354712.3; ENSG00000198910.14. [P32004-3] DR Ensembl; ENST00000370055.5; ENSP00000359072.1; ENSG00000198910.14. [P32004-3] DR Ensembl; ENST00000370060.7; ENSP00000359077.1; ENSG00000198910.14. [P32004-1] DR GeneID; 3897; -. DR KEGG; hsa:3897; -. DR MANE-Select; ENST00000370060.7; ENSP00000359077.1; NM_001278116.2; NP_001265045.1. DR UCSC; uc004fjc.5; human. [P32004-1] DR AGR; HGNC:6470; -. DR CTD; 3897; -. DR DisGeNET; 3897; -. DR GeneCards; L1CAM; -. DR GeneReviews; L1CAM; -. DR HGNC; HGNC:6470; L1CAM. DR HPA; ENSG00000198910; Tissue enhanced (brain, intestine). DR MalaCards; L1CAM; -. DR MIM; 303350; phenotype. DR MIM; 304100; phenotype. DR MIM; 307000; phenotype. DR MIM; 308840; gene. DR neXtProt; NX_P32004; -. DR OpenTargets; ENSG00000198910; -. DR Orphanet; 2182; Hydrocephalus with stenosis of the aqueduct of Sylvius. DR Orphanet; 2466; MASA syndrome. DR Orphanet; 1497; X-linked complicated corpus callosum dysgenesis. DR Orphanet; 306617; X-linked complicated spastic paraplegia type 1. DR PharmGKB; PA30259; -. DR VEuPathDB; HostDB:ENSG00000198910; -. DR eggNOG; KOG3513; Eukaryota. DR GeneTree; ENSGT00940000157506; -. DR HOGENOM; CLU_005756_1_1_1; -. DR InParanoid; P32004; -. DR OMA; GARTIIQ; -. DR OrthoDB; 2912783at2759; -. DR PhylomeDB; P32004; -. DR TreeFam; TF351098; -. DR PathwayCommons; P32004; -. DR Reactome; R-HSA-210991; Basigin interactions. DR Reactome; R-HSA-373760; L1CAM interactions. DR Reactome; R-HSA-437239; Recycling pathway of L1. DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins. DR Reactome; R-HSA-445144; Signal transduction by L1. DR SignaLink; P32004; -. DR SIGNOR; P32004; -. DR BioGRID-ORCS; 3897; 8 hits in 771 CRISPR screens. DR ChiTaRS; L1CAM; human. DR GeneWiki; L1_(protein); -. DR GenomeRNAi; 3897; -. DR Pharos; P32004; Tbio. DR PRO; PR:P32004; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P32004; Protein. DR Bgee; ENSG00000198910; Expressed in cortical plate and 162 other cell types or tissues. DR ExpressionAtlas; P32004; baseline and differential. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008046; F:axon guidance receptor activity; IBA:GO_Central. DR GO; GO:0019904; F:protein domain specific binding; IDA:CAFA. DR GO; GO:0061564; P:axon development; IDA:UniProtKB. DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc. DR GO; GO:0016477; P:cell migration; IDA:UniProtKB. DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB. DR GO; GO:0006935; P:chemotaxis; TAS:BHF-UCL. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB. DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB. DR GO; GO:0050808; P:synapse organization; IDA:UniProtKB. DR CDD; cd00063; FN3; 4. DR CDD; cd05876; Ig3_L1-CAM; 1. DR CDD; cd05867; Ig4_L1-CAM_like; 1. DR CDD; cd05845; IgI_2_L1-CAM_like; 1. DR DisProt; DP00666; -. DR Gene3D; 2.60.40.10; Immunoglobulins; 10. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C. DR PANTHER; PTHR44170:SF44; L1 CELL ADHESION MOLECULE; 1. DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1. DR Pfam; PF13882; Bravo_FIGEY; 1. DR Pfam; PF00041; fn3; 4. DR Pfam; PF07679; I-set; 3. DR Pfam; PF13927; Ig_3; 2. DR SMART; SM00060; FN3; 4. DR SMART; SM00409; IG; 6. DR SMART; SM00408; IGc2; 5. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR SUPFAM; SSF48726; Immunoglobulin; 6. DR PROSITE; PS50853; FN3; 5. DR PROSITE; PS50835; IG_LIKE; 6. DR Genevisible; P32004; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Cell projection; Developmental protein; Differentiation; KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; KW Hereditary spastic paraplegia; Hirschsprung disease; Immunoglobulin domain; KW Intellectual disability; Membrane; Neurodegeneration; Neurogenesis; KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:3136168" FT CHAIN 20..1257 FT /note="Neural cell adhesion molecule L1" FT /id="PRO_0000015022" FT TOPO_DOM 20..1120 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1121..1143 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1144..1257 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 35..125 FT /note="Ig-like C2-type 1" FT DOMAIN 139..226 FT /note="Ig-like C2-type 2" FT DOMAIN 240..328 FT /note="Ig-like C2-type 3" FT DOMAIN 333..420 FT /note="Ig-like C2-type 4" FT DOMAIN 425..507 FT /note="Ig-like C2-type 5" FT DOMAIN 518..607 FT /note="Ig-like C2-type 6" FT DOMAIN 615..712 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 717..810 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 814..916 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 920..1015 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1016..1115 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 698..725 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1176..1207 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1226..1257 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 554..556 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOD_RES 1163 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 1178 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11627" FT MOD_RES 1181 FT /note="Phosphoserine; by CaMK2" FT /evidence="ECO:0000269|PubMed:8592152" FT MOD_RES 1194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1243 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1244 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11627" FT MOD_RES 1248 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT CARBOHYD 100 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 203 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 247 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 294 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 433 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 479 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 490 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 505 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 588 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 671 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 726 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 777 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 825 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 849 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 876 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 979 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1022 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1030 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1071 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1105 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 57..114 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 158..209 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 264..312 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 354..404 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 448..497 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 539..591 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 26..31 FT /note="YEGHHV -> L (in isoform 3)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_046317" FT VAR_SEQ 1177..1180 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:1627459, ECO:0000303|Ref.6" FT /id="VSP_002591" FT VARIANT 9 FT /note="W -> S (in HYCX)" FT /evidence="ECO:0000269|PubMed:7762552" FT /id="VAR_003921" FT VARIANT 26..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078350" FT VARIANT 30 FT /note="H -> N" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030403" FT VARIANT 37 FT /note="I -> N (found in L1 syndrome; likely pathogenic; FT loss of localization at the cell surface; retention in the FT endoplasmic reticulum; loss of homophilic interactions at FT the cell surface)" FT /evidence="ECO:0000269|PubMed:19846429, FT ECO:0000269|PubMed:26891472" FT /id="VAR_078351" FT VARIANT 38 FT /note="T -> M (no effect on localization at the cell FT surface; dbSNP:rs201151358)" FT /evidence="ECO:0000269|PubMed:19846429, FT ECO:0000269|PubMed:26891472" FT /id="VAR_078352" FT VARIANT 66..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078353" FT VARIANT 109..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078354" FT VARIANT 120 FT /note="L -> V (no effect on axon guidance activity, nor on FT synapse formation, when assayed in a heterologous system; FT dbSNP:rs796052697)" FT /evidence="ECO:0000269|PubMed:24155914" FT /id="VAR_078355" FT VARIANT 121 FT /note="G -> S (in HYCX)" FT /evidence="ECO:0000269|PubMed:7762552" FT /id="VAR_003922" FT VARIANT 133..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078356" FT VARIANT 138..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078357" FT VARIANT 172 FT /note="M -> I (found in a patient with L1 syndrome; likely FT pathogenic; loss of homophilic interactions at the cell FT surface; no effect on the localization at the cell FT surface)" FT /evidence="ECO:0000269|PubMed:19846429, FT ECO:0000269|PubMed:26891472" FT /id="VAR_078358" FT VARIANT 179 FT /note="I -> S (in HYCX and MASA; dbSNP:rs137852523)" FT /evidence="ECO:0000269|PubMed:19846429, FT ECO:0000269|PubMed:7562969" FT /id="VAR_003923" FT VARIANT 184 FT /note="R -> G (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078359" FT VARIANT 184 FT /note="R -> Q (in HYCX; severe; reduced axon arborization; FT partial loss of localization at the cell surface; retention FT in the endoplasmic reticulum; in neurons, restricted to FT cell bodies and proximal segments of processes; loss of FT axon guidance and of proper synapse formation, when assayed FT in a heterologous system; dbSNP:rs137852521)" FT /evidence="ECO:0000269|PubMed:19846429, FT ECO:0000269|PubMed:20621658, ECO:0000269|PubMed:24155914, FT ECO:0000269|PubMed:7920659, ECO:0000269|PubMed:8556302, FT ECO:0000269|PubMed:9195224" FT /id="VAR_003924" FT VARIANT 184 FT /note="R -> W (in HYCX)" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030404" FT VARIANT 187..198 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078360" FT VARIANT 194 FT /note="Y -> C (in HYCX)" FT /evidence="ECO:0000269|PubMed:8929944" FT /id="VAR_003925" FT VARIANT 202 FT /note="D -> Y (in MASA; loss of homophilic interactions at FT the cell surface; no effect on localization at the cell FT surface)" FT /evidence="ECO:0000269|PubMed:10805190, FT ECO:0000269|PubMed:19846429, ECO:0000269|PubMed:26891472" FT /id="VAR_030405" FT VARIANT 210 FT /note="H -> Q (in MASA; decrease in cell-matrix adhesion; FT decreased cell migration; loss of axon guidance and of FT proper synapse formation, when assayed in a heterologous FT system; no effect on the localization at the cell surface; FT no effect on cell proliferation, when transfected in FT pheochromocytoma PC12 cells; no effect on neurite FT outgrowth, when assayed in NGF-treated pheochromocytoma FT PC12 cells; dbSNP:rs28933683)" FT /evidence="ECO:0000269|PubMed:22973895, FT ECO:0000269|PubMed:24155914, ECO:0000269|PubMed:7920659, FT ECO:0000269|PubMed:7920660, ECO:0000269|PubMed:8556302" FT /id="VAR_003926" FT VARIANT 219 FT /note="I -> T (in HYCX; decrease in cell-matrix adhesion; FT decreased cell migration; no effect on the localization at FT the cell surface; no effect on cell proliferation, when FT transfected in pheochromocytoma PC12 cells; no effect on FT neurite outgrowth, when assayed in NGF-treated FT pheochromocytoma PC12 cells)" FT /evidence="ECO:0000269|PubMed:22973895, FT ECO:0000269|PubMed:9744477" FT /id="VAR_003927" FT VARIANT 240 FT /note="P -> L (in HYCX and ACCPX; dbSNP:rs137852526)" FT /evidence="ECO:0000269|PubMed:16650080, FT ECO:0000269|PubMed:8929944" FT /id="VAR_003928" FT VARIANT 254 FT /note="A -> D (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078361" FT VARIANT 264 FT /note="C -> Y (in HYCX; severe; loss of localization to the FT cell surface; retention in the endoplasmic reticulum; loss FT of axon guidance, when assayed in a heterologous system; FT dbSNP:rs137852518)" FT /evidence="ECO:0000269|PubMed:12514225, FT ECO:0000269|PubMed:22973895, ECO:0000269|PubMed:24155914, FT ECO:0000269|PubMed:8401576, ECO:0000269|PubMed:8556302" FT /id="VAR_003929" FT VARIANT 268 FT /note="G -> D (in MASA)" FT /evidence="ECO:0000269|PubMed:9300653" FT /id="VAR_030406" FT VARIANT 276 FT /note="W -> R (found in L1 syndrome; likely pathogenic; FT dbSNP:rs1131691900)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078362" FT VARIANT 309 FT /note="E -> K (in MASA; decrease in neurite outgrowth, when FT assayed in NGF-treated pheochromocytoma PC12 cells; FT decrease in cell-matrix adhesion; decreased cell migration; FT no effect on axon guidance, on subcellular location to FT synaptic terminals, nor on proper synapse formation, when FT assayed in a heterologous system; no effect on the FT localization at the cell surface; no effect on cell FT proliferation, when transfected in pheochromocytoma PC12 FT cells; dbSNP:rs367665974)" FT /evidence="ECO:0000269|PubMed:22973895, FT ECO:0000269|PubMed:24155914, ECO:0000269|PubMed:7762552" FT /id="VAR_003930" FT VARIANT 313 FT /note="L -> P (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078363" FT VARIANT 335 FT /note="W -> C (in HYCX)" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030407" FT VARIANT 335 FT /note="W -> R (in HYCX and MASA; also in a patient with FT hydrocephalus and Hirschsprung disease)" FT /evidence="ECO:0000269|PubMed:19846429, FT ECO:0000269|PubMed:9744477" FT /id="VAR_003931" FT VARIANT 366..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078364" FT VARIANT 369 FT /note="N -> K (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078365" FT VARIANT 370 FT /note="G -> R (in HYCX and MASA; dbSNP:rs137852524)" FT /evidence="ECO:0000269|PubMed:10797421, FT ECO:0000269|PubMed:7562969" FT /id="VAR_003932" FT VARIANT 386 FT /note="R -> C (in HYCX; dbSNP:rs1557092299)" FT /evidence="ECO:0000269|PubMed:9744477" FT /id="VAR_003933" FT VARIANT 408 FT /note="N -> I (in HYCX)" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030408" FT VARIANT 415 FT /note="A -> P (in HYCX)" FT /evidence="ECO:0000269|PubMed:12435569, FT ECO:0000269|PubMed:19846429" FT /id="VAR_027512" FT VARIANT 421 FT /note="V -> D (in HYCX)" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030409" FT VARIANT 423..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078366" FT VARIANT 426 FT /note="A -> D (in MASA)" FT /evidence="ECO:0000269|PubMed:9300653" FT /id="VAR_030410" FT VARIANT 439..443 FT /note="Missing (in HYCX)" FT /evidence="ECO:0000269|PubMed:9195224" FT /id="VAR_003934" FT VARIANT 452 FT /note="G -> R (in HYCX; severe; dbSNP:rs137852520)" FT /evidence="ECO:0000269|PubMed:7920659, FT ECO:0000269|PubMed:8556302" FT /id="VAR_003935" FT VARIANT 473 FT /note="R -> C (in HYCX and MASA; dbSNP:rs886039408)" FT /evidence="ECO:0000269|PubMed:9744477" FT /id="VAR_003936" FT VARIANT 480 FT /note="G -> R (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078367" FT VARIANT 482 FT /note="L -> P (in MASA; dbSNP:rs1064794246)" FT /evidence="ECO:0000269|PubMed:9268105" FT /id="VAR_030411" FT VARIANT 497 FT /note="C -> Y (in HYCX)" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030412" FT VARIANT 516 FT /note="D -> N (found in a patient with L1 syndrome; FT uncertain significance; dbSNP:rs782367931)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078368" FT VARIANT 516 FT /note="D -> Y (found in a patient with L1 syndrome; FT uncertain significance)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078369" FT VARIANT 525 FT /note="R -> H (found in a patient with L1 syndrome; FT uncertain significance; dbSNP:rs782401498)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078370" FT VARIANT 526 FT /note="Missing (in HYCX)" FT /evidence="ECO:0000269|PubMed:9268105" FT /id="VAR_030413" FT VARIANT 542 FT /note="S -> P (in HYCX)" FT /evidence="ECO:0000269|PubMed:9268105" FT /id="VAR_030414" FT VARIANT 598 FT /note="D -> N (in MASA; dbSNP:rs137852519)" FT /evidence="ECO:0000269|PubMed:7920660, FT ECO:0000269|PubMed:8556302" FT /id="VAR_003937" FT VARIANT 627 FT /note="T -> M (in dbSNP:rs398123360)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078371" FT VARIANT 632 FT /note="R -> P (in MASA)" FT /evidence="ECO:0000269|PubMed:9452110" FT /id="VAR_003938" FT VARIANT 635 FT /note="W -> C (found in L1 syndrome; likely pathogenic; FT loss of localization at the cell surface; retention in the FT endoplasmic reticulum; loss of transport into axons; loss FT of neurite outgrowth; loss of cell-cell adhesion)" FT /evidence="ECO:0000269|PubMed:22222883" FT /id="VAR_078372" FT VARIANT 645 FT /note="I -> P (found in L1 syndrome; likely pathogenic; FT requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078373" FT VARIANT 655 FT /note="K -> E (in HYCX; dbSNP:rs1375788131)" FT /evidence="ECO:0000269|PubMed:9118141" FT /id="VAR_030415" FT VARIANT 662..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078374" FT VARIANT 674 FT /note="S -> C (in HYCX)" FT /evidence="ECO:0000269|PubMed:9832035" FT /id="VAR_027513" FT VARIANT 691 FT /note="A -> D (in HYCX and MASA)" FT /evidence="ECO:0000269|PubMed:9521424, FT ECO:0000269|PubMed:9832035" FT /id="VAR_003939" FT VARIANT 691 FT /note="A -> T (in HYCX)" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030416" FT VARIANT 698 FT /note="G -> R (in HYCX and MASA; also found in a patient FT affected by hydrocephalus with Hirschsprung disease; FT dbSNP:rs886039409)" FT /evidence="ECO:0000269|PubMed:22344793, FT ECO:0000269|PubMed:9521424, ECO:0000269|PubMed:9832035" FT /id="VAR_003940" FT VARIANT 714 FT /note="P -> S (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078375" FT VARIANT 739 FT /note="R -> W (in dbSNP:rs142424573)" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030417" FT VARIANT 741 FT /note="M -> T (in HYCX; dbSNP:rs1557091083)" FT /evidence="ECO:0000269|PubMed:9268105" FT /id="VAR_030418" FT VARIANT 751 FT /note="R -> P (in HYCX)" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030419" FT VARIANT 752 FT /note="V -> M (in HYCX and MASA; also found in a patient FT with the diagnosis of L1 syndrome; also in a patient with FT hydrocephalus and Hirschsprung disease; dbSNP:rs137852525)" FT /evidence="ECO:0000269|PubMed:11857550, FT ECO:0000269|PubMed:19846429, ECO:0000269|PubMed:9268105" FT /id="VAR_014421" FT VARIANT 754 FT /note="W -> R (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078376" FT VARIANT 760..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078377" FT VARIANT 768 FT /note="V -> F (in HYCX)" FT /evidence="ECO:0000269|PubMed:7762552" FT /id="VAR_003941" FT VARIANT 768 FT /note="V -> I (decreased cell-cell adhesion; no effect on FT subcellular localization; no effect on neurite outgrowth; FT dbSNP:rs36021462)" FT /evidence="ECO:0000269|PubMed:22222883, FT ECO:0000269|PubMed:9268105" FT /id="VAR_030420" FT VARIANT 770 FT /note="D -> N (in MASA; dbSNP:rs148516831)" FT /evidence="ECO:0000269|PubMed:16816908" FT /id="VAR_027514" FT VARIANT 784 FT /note="Y -> C (in HYCX; dbSNP:rs797045674)" FT /evidence="ECO:0000269|PubMed:9195224" FT /id="VAR_003942" FT VARIANT 789..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429, FT ECO:0000269|PubMed:26891472" FT /id="VAR_078378" FT VARIANT 811..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078379" FT VARIANT 891..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078380" FT VARIANT 901..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078381" FT VARIANT 935 FT /note="L -> P (in HYCX)" FT /evidence="ECO:0000269|PubMed:9521424" FT /id="VAR_003943" FT VARIANT 936..948 FT /note="Missing (in HYCX)" FT /evidence="ECO:0000269|PubMed:9195224" FT /id="VAR_003944" FT VARIANT 941 FT /note="P -> L (in HYCX and MASA; decrease in neurite FT outgrowth, when assayed in NGF-treated pheochromocytoma FT PC12 cells; decrease in cell-matrix adhesion; decreased FT cell migration; no effect on the localization at the cell FT surface; no effect on cell proliferation, when transfected FT in pheochromocytoma PC12 cells)" FT /evidence="ECO:0000269|PubMed:22973895, FT ECO:0000269|PubMed:7762552" FT /id="VAR_003945" FT VARIANT 958 FT /note="L -> V (in dbSNP:rs35902890)" FT /id="VAR_059413" FT VARIANT 1036 FT /note="W -> L (in HYCX; partial loss of localization at the FT cell surface; retention in the endoplasmic reticulum; in FT neurons, partial loss of localization to axons, but FT enriched on proximal dendrites)" FT /evidence="ECO:0000269|PubMed:20621658" FT /id="VAR_078382" FT VARIANT 1064..1257 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078383" FT VARIANT 1070 FT /note="Y -> C (in HYCX; partial loss of axon guidance and FT loss of proper synapse formation, when assayed in a FT heterologous system)" FT /evidence="ECO:0000269|PubMed:24155914, FT ECO:0000269|PubMed:7762552" FT /id="VAR_003946" FT VARIANT 1071 FT /note="Missing (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078384" FT VARIANT 1080 FT /note="L -> Q (found in L1 syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:19846429" FT /id="VAR_078385" FT VARIANT 1194 FT /note="S -> L (in HYCX and MASA; dbSNP:rs137852522)" FT /evidence="ECO:0000269|PubMed:7881431, FT ECO:0000269|PubMed:8556302" FT /id="VAR_003947" FT VARIANT 1224 FT /note="S -> L (in HYCX)" FT /evidence="ECO:0000269|PubMed:9744477" FT /id="VAR_003948" FT VARIANT 1239 FT /note="G -> E" FT /evidence="ECO:0000269|PubMed:10797421" FT /id="VAR_030421" FT MUTAGEN 1147..1153 FT /note="KGGKYSV->AGGAASA: Loss of axon guidance, when FT assayed in a heterologous system, but normal synapse FT formation." FT /evidence="ECO:0000269|PubMed:24155914" FT CONFLICT 4 FT /note="A -> V (in Ref. 1; CAA42508)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="T -> I (in Ref. 1; CAA42508)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="S -> T (in Ref. 1; CAA42508)" FT /evidence="ECO:0000305" FT CONFLICT 276..277 FT /note="WL -> SV (in Ref. 1; CAA42508)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="V -> A (in Ref. 6; ABP88252)" FT /evidence="ECO:0000305" FT CONFLICT 357 FT /note="Q -> E (in Ref. 1; CAA42508)" FT /evidence="ECO:0000305" FT CONFLICT 515 FT /note="K -> T (in Ref. 6; ABP88252)" FT /evidence="ECO:0000305" FT CONFLICT 626 FT /note="L -> V (in Ref. 1; CAA42508)" FT /evidence="ECO:0000305" FT CONFLICT 660 FT /note="E -> G (in Ref. 6; ABP88252)" FT /evidence="ECO:0000305" FT CONFLICT 936 FT /note="L -> V (in Ref. 12; CAB37831)" FT /evidence="ECO:0000305" FT CONFLICT 1116..1117 FT /note="GF -> WLC (in Ref. 13; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1164 FT /note="E -> V (in Ref. 6; ABP88252)" FT /evidence="ECO:0000305" FT MOD_RES P32004-2:1177 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES P32004-3:1172 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" SQ SEQUENCE 1257 AA; 140003 MW; 5EDD764DA86C0E63 CRC64; MVVALRYVWP LLLCSPCLLI QIPEEYEGHH VMEPPVITEQ SPRRLVVFPT DDISLKCEAS GKPEVQFRWT RDGVHFKPKE ELGVTVYQSP HSGSFTITGN NSNFAQRFQG IYRCFASNKL GTAMSHEIRL MAEGAPKWPK ETVKPVEVEE GESVVLPCNP PPSAEPLRIY WMNSKILHIK QDERVTMGQN GNLYFANVLT SDNHSDYICH AHFPGTRTII QKEPIDLRVK ATNSMIDRKP RLLFPTNSSS HLVALQGQPL VLECIAEGFP TPTIKWLRPS GPMPADRVTY QNHNKTLQLL KVGEEDDGEY RCLAENSLGS ARHAYYVTVE AAPYWLHKPQ SHLYGPGETA RLDCQVQGRP QPEVTWRING IPVEELAKDQ KYRIQRGALI LSNVQPSDTM VTQCEARNRH GLLLANAYIY VVQLPAKILT ADNQTYMAVQ GSTAYLLCKA FGAPVPSVQW LDEDGTTVLQ DERFFPYANG TLGIRDLQAN DTGRYFCLAA NDQNNVTIMA NLKVKDATQI TQGPRSTIEK KGSRVTFTCQ ASFDPSLQPS ITWRGDGRDL QELGDSDKYF IEDGRLVIHS LDYSDQGNYS CVASTELDVV ESRAQLLVVG SPGPVPRLVL SDLHLLTQSQ VRVSWSPAED HNAPIEKYDI EFEDKEMAPE KWYSLGKVPG NQTSTTLKLS PYVHYTFRVT AINKYGPGEP SPVSETVVTP EAAPEKNPVD VKGEGNETTN MVITWKPLRW MDWNAPQVQY RVQWRPQGTR GPWQEQIVSD PFLVVSNTST FVPYEIKVQA VNSQGKGPEP QVTIGYSGED YPQAIPELEG IEILNSSAVL VKWRPVDLAQ VKGHLRGYNV TYWREGSQRK HSKRHIHKDH VVVPANTTSV ILSGLRPYSS YHLEVQAFNG RGSGPASEFT FSTPEGVPGH PEALHLECQS NTSLLLRWQP PLSHNGVLTG YVLSYHPLDE GGKGQLSFNL RDPELRTHNL TDLSPHLRYR FQLQATTKEG PGEAIVREGG TMALSGISDF GNISATAGEN YSVVSWVPKE GQCNFRFHIL FKALGEEKGG ASLSPQYVSY NQSSYTQWDL QPDTDYEIHL FKERMFRHQM AVKTNGTGRV RLPPAGFATE GWFIGFVSAI ILLLLVLLIL CFIKRSKGGK YSVKDKEDTQ VDSEARPMKD ETFGEYRSLE SDNEEKAFGS SQPSLNGDIK PLGSDDSLAD YGGSVDVQFN EDGSFIGQYS GKKEKEAAGG NDSSGATSPI NPAVALE //