ID   NCHL1_MOUSE             Reviewed;        1209 AA.
AC   P70232; A2RRK1; Q8BS24; Q8C6W0; Q8C823; Q8VBY7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Neural cell adhesion molecule L1-like protein;
DE   AltName: Full=Cell adhesion molecule with homology to L1CAM;
DE   AltName: Full=Chl1-like protein;
DE   AltName: Full=Close homolog of L1;
DE   Contains:
DE     RecName: Full=Processed neural cell adhesion molecule L1-like protein;
DE   Flags: Precursor;
GN   Name=Chl1; Synonyms=Call;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GLYCOSYLATION,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=8921253; DOI=10.1111/j.1460-9568.1996.tb01306.x;
RA   Holm J., Hillenbrand R., Steuber V., Bartsch U., Moos M., Luebbert H.,
RA   Montag D., Schachner M.;
RT   "Structural features of a close homologue of L1 (CHL1) in the mouse: a new
RT   member of the L1 family of neural recognition molecules.";
RL   Eur. J. Neurosci. 8:1613-1629(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-425 AND 666-1209 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Head, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=129/Sv;
RX   PubMed=12391163; DOI=10.1128/mcb.22.22.7967-7981.2002;
RA   Montag-Sallaz M., Schachner M., Montag D.;
RT   "Misguided axonal projections, neural cell adhesion molecule 180 mRNA
RT   upregulation, and altered behavior in mice deficient for the close homolog
RT   of L1.";
RL   Mol. Cell. Biol. 22:7967-7981(2002).
RN   [7]
RP   FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH L1CAM, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10103075; DOI=10.1046/j.1460-9568.1999.00496.x;
RA   Hillenbrand R., Molthagen M., Montag D., Schachner M.;
RT   "The close homologue of the neural adhesion molecule L1 (CHL1): patterns of
RT   expression and promotion of neurite outgrowth by heterophilic
RT   interactions.";
RL   Eur. J. Neurosci. 11:813-826(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=10022583;
RX   DOI=10.1002/(sici)1097-4695(19990215)38:3<428::aid-neu10>3.0.co;2-6;
RA   Chen S., Mantei N., Dong L., Schachner M.;
RT   "Prevention of neuronal cell death by neural adhesion molecules L1 and
RT   CHL1.";
RL   J. Neurobiol. 38:428-439(1999).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14659567; DOI=10.1016/s0166-4328(03)00114-1;
RA   Pratte M., Rougon G., Schachner M., Jamon M.;
RT   "Mice deficient for the close homologue of the neural adhesion cell L1
RT   (CHL1) display alterations in emotional reactivity and motor
RT   coordination.";
RL   Behav. Brain Res. 147:31-39(2003).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12812975; DOI=10.1093/hmg/ddg165;
RA   Frints S.G.M., Marynen P., Hartmann D., Fryns J.-P., Steyaert J.,
RA   Schachner M., Rolf B., Craessaerts K., Snellinx A., Hollanders K.,
RA   D'Hooge R., De Deyn P.P., Froyen G.;
RT   "CALL interrupted in a patient with non-specific mental retardation: gene
RT   dosage-dependent alteration of murine brain development and behavior.";
RL   Hum. Mol. Genet. 12:1463-1474(2003).
RN   [11]
RP   FUNCTION, INTERACTION WITH ANK3; ITGB1/ITGA1 HETERODIMER AND ITGB1/ITGA2
RP   HETERODIMER, MOTIFS, AND MUTAGENESIS OF 555-ASP--ALA-558 AND TYR-1186.
RX   PubMed=12721290; DOI=10.1074/jbc.m303084200;
RA   Buhusi M., Midkiff B.R., Gates A.M., Richter M., Schachner M., Maness P.F.;
RT   "Close homolog of L1 is an enhancer of integrin-mediated cell migration.";
RL   J. Biol. Chem. 278:25024-25031(2003).
RN   [12]
RP   FUNCTION, AND CLEAVAGE BY ADAM8.
RX   PubMed=14761956; DOI=10.1074/jbc.m400560200;
RA   Naus S., Richter M., Wildeboer D., Moss M., Schachner M., Bartsch J.W.;
RT   "Ectodomain shedding of the neural recognition molecule CHL1 by the
RT   metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses
RT   neuronal cell death.";
RL   J. Biol. Chem. 279:16083-16090(2004).
RN   [13]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15504324; DOI=10.1016/j.neuron.2004.10.016;
RA   Demyanenko G.P., Schachner M., Anton E., Schmid R., Feng G., Sanes J.,
RA   Maness P.F.;
RT   "Close homolog of L1 modulates area-specific neuronal positioning and
RT   dendrite orientation in the cerebral cortex.";
RL   Neuron 44:423-437(2004).
RN   [14]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16623841; DOI=10.1111/j.1460-9568.2006.04710.x;
RA   Nikonenko A.G., Sun M., Lepsveridze E., Apostolova I., Petrova I.,
RA   Irintchev A., Dityatev A., Schachner M.;
RT   "Enhanced perisomatic inhibition and impaired long-term potentiation in the
RT   CA1 region of juvenile CHL1-deficient mice.";
RL   Eur. J. Neurosci. 23:1839-1852(2006).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148; SER-1161 AND SER-1181,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [16]
RP   CLEAVAGE BY BACE1.
RX   PubMed=29325091; DOI=10.1093/jmcb/mjy001;
RA   Wang X., Wang C., Pei G.;
RT   "alpha-secretase ADAM10 physically interacts with beta-secretase BACE1 in
RT   neurons and regulates CHL1 proteolysis.";
RL   J. Mol. Cell Biol. 10:411-422(2018).
CC   -!- FUNCTION: Extracellular matrix and cell adhesion protein that plays a
CC       role in nervous system development and in synaptic plasticity. Both
CC       soluble and membranous forms promote neurite outgrowth of cerebellar
CC       and hippocampal neurons and suppress neuronal cell death. Plays a role
CC       in neuronal positioning of pyramidal neurons as well as in regulation
CC       of both the number of interneurons and the efficacy of GABAergic
CC       synapses. May play a role in regulating cell migration in nerve
CC       regeneration and cortical development. Potentiates integrin-dependent
CC       cell migration towards extracellular matrix proteins. Recruits ANK3 to
CC       the plasma membrane. {ECO:0000269|PubMed:10022583,
CC       ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:12391163,
CC       ECO:0000269|PubMed:12721290, ECO:0000269|PubMed:12812975,
CC       ECO:0000269|PubMed:14659567, ECO:0000269|PubMed:14761956,
CC       ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:16623841}.
CC   -!- SUBUNIT: May interact with L1CAM. May interact with ITGB1/ITGA1
CC       heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3.
CC   -!- INTERACTION:
CC       P70232; Q9JMB8: Cntn6; NbExp=5; IntAct=EBI-7703109, EBI-7703151;
CC       P70232; P18052: Ptpra; NbExp=4; IntAct=EBI-7703109, EBI-6597520;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Note=Soluble forms produced by cleavage/shedding also exist.
CC   -!- SUBCELLULAR LOCATION: [Processed neural cell adhesion molecule L1-like
CC       protein]: Secreted, extracellular space, extracellular matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70232-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70232-2; Sequence=VSP_020083, VSP_020084, VSP_020085;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, in the cerebellum and in
CC       the spinal cord. Detected in the retina and the optic nerve. Expressed
CC       in neurons and glial cells in the central nervous system and by Schwann
CC       cells in the peripheral nervous system. {ECO:0000269|PubMed:10103075,
CC       ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:8921253}.
CC   -!- DEVELOPMENTAL STAGE: Not detectable in the forebrain at 11 dpc, weakly
CC       detectable at 13 dpc with highest detection at 18 dpc to postnatal day
CC       7. Down-regulated at postnatal day 15 and further reduced in four-week-
CC       old animals. {ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:15504324,
CC       ECO:0000269|PubMed:8921253}.
CC   -!- DOMAIN: The FIG[AQ]Y motif seems to be an ankyrin recruitment region.
CC   -!- DOMAIN: The DGEA motif seems to be a recognition site for integrin.
CC   -!- PTM: Cleavage by metalloprotease ADAM8 in the extracellular part
CC       generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is
CC       inhibited by metalloprotease inhibitors. In brain extracts, these two
CC       soluble forms are also present and are dramatically reduced in mice
CC       lacking ADAM8 (PubMed:14761956). Cleaved by BACE1 (PubMed:29325091).
CC       {ECO:0000269|PubMed:14761956, ECO:0000269|PubMed:29325091}.
CC   -!- PTM: N-glycosylated. Contains N-linked oligosaccharides with a sulfated
CC       carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc).
CC       {ECO:0000269|PubMed:8921253}.
CC   -!- PTM: O-glycosylated. {ECO:0000269|PubMed:8921253}.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit misguided axonal projections and
CC       aberrant axonal connectivity. They show alterations of hippocampal
CC       fiber organization and olfactory axon projections. Their exploratory
CC       behavior in novel environments is altered suggesting deficits in
CC       information processing and in attention. They also display signs of
CC       decreased stress and are more sociable and less aggressive.
CC       Heterozygous mice exhibit half levels of CHL1 expression in the
CC       hippocampus compared to their wild-type littermates, reflecting a gene
CC       dosage effect. {ECO:0000269|PubMed:12391163,
CC       ECO:0000269|PubMed:12812975, ECO:0000269|PubMed:14659567,
CC       ECO:0000269|PubMed:16623841}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC       L1/neurofascin/NgCAM family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30699.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X94310; CAA63972.1; -; mRNA.
DR   EMBL; AK040765; BAC30699.1; ALT_FRAME; mRNA.
DR   EMBL; AK048639; BAC33405.1; -; mRNA.
DR   EMBL; AK053039; BAC35247.2; -; mRNA.
DR   EMBL; AC153595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466523; EDK99388.1; -; Genomic_DNA.
DR   EMBL; BC131670; AAI31671.1; -; mRNA.
DR   EMBL; BC131671; AAI31672.1; -; mRNA.
DR   EMBL; AJ319655; CAC88131.1; -; Genomic_DNA.
DR   EMBL; AJ319656; CAC88131.1; JOINED; Genomic_DNA.
DR   EMBL; AJ319657; CAC88131.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS39582.1; -. [P70232-1]
DR   PIR; T42718; T42718.
DR   RefSeq; NP_031723.2; NM_007697.2. [P70232-1]
DR   RefSeq; XP_006505535.1; XM_006505472.3. [P70232-1]
DR   RefSeq; XP_017176864.1; XM_017321375.1.
DR   RefSeq; XP_017176865.1; XM_017321376.1. [P70232-1]
DR   AlphaFoldDB; P70232; -.
DR   SMR; P70232; -.
DR   BioGRID; 198702; 6.
DR   IntAct; P70232; 2.
DR   MINT; P70232; -.
DR   STRING; 10090.ENSMUSP00000063933; -.
DR   GlyConnect; 2538; 11 N-Linked glycans (5 sites).
DR   GlyCosmos; P70232; 10 sites, 11 glycans.
DR   GlyGen; P70232; 11 sites, 11 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P70232; -.
DR   PhosphoSitePlus; P70232; -.
DR   SwissPalm; P70232; -.
DR   CPTAC; non-CPTAC-3993; -.
DR   jPOST; P70232; -.
DR   MaxQB; P70232; -.
DR   PaxDb; 10090-ENSMUSP00000063933; -.
DR   PeptideAtlas; P70232; -.
DR   ProteomicsDB; 252651; -. [P70232-1]
DR   ProteomicsDB; 252652; -. [P70232-2]
DR   ABCD; P70232; 2 sequenced antibodies.
DR   Antibodypedia; 1160; 154 antibodies from 25 providers.
DR   DNASU; 12661; -.
DR   Ensembl; ENSMUST00000066905.9; ENSMUSP00000063933.7; ENSMUSG00000030077.12. [P70232-1]
DR   Ensembl; ENSMUST00000203830.3; ENSMUSP00000144758.2; ENSMUSG00000030077.12. [P70232-1]
DR   Ensembl; ENSMUST00000203912.3; ENSMUSP00000145026.2; ENSMUSG00000030077.12. [P70232-2]
DR   GeneID; 12661; -.
DR   KEGG; mmu:12661; -.
DR   UCSC; uc009dcj.1; mouse. [P70232-1]
DR   UCSC; uc009dck.1; mouse. [P70232-2]
DR   AGR; MGI:1098266; -.
DR   CTD; 10752; -.
DR   MGI; MGI:1098266; Chl1.
DR   VEuPathDB; HostDB:ENSMUSG00000030077; -.
DR   eggNOG; KOG3513; Eukaryota.
DR   GeneTree; ENSGT00940000160080; -.
DR   HOGENOM; CLU_005756_1_1_1; -.
DR   InParanoid; P70232; -.
DR   OMA; RARHEFH; -.
DR   PhylomeDB; P70232; -.
DR   TreeFam; TF351098; -.
DR   BioGRID-ORCS; 12661; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Chl1; mouse.
DR   PRO; PR:P70232; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P70232; Protein.
DR   Bgee; ENSMUSG00000030077; Expressed in spermatid and 167 other cell types or tissues.
DR   ExpressionAtlas; P70232; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0050890; P:cognition; IMP:MGI.
DR   GO; GO:0035640; P:exploration behavior; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR   CDD; cd00063; FN3; 4.
DR   CDD; cd04978; Ig4_L1-NrCAM_like; 1.
DR   CDD; cd05845; IgI_2_L1-CAM_like; 1.
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:SF51; NEURAL CELL ADHESION MOLECULE L1-LIKE PROTEIN ISOFORM X1; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF13882; Bravo_FIGEY; 1.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
DR   Genevisible; P70232; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Developmental protein;
KW   Differentiation; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1209
FT                   /note="Neural cell adhesion molecule L1-like protein"
FT                   /id="PRO_0000247897"
FT   CHAIN           26..?
FT                   /note="Processed neural cell adhesion molecule L1-like
FT                   protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000314778"
FT   TOPO_DOM        26..1083
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1084..1104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1105..1209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..124
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          128..223
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          235..328
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          331..417
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          423..510
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          515..607
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          614..709
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          714..807
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          812..914
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          918..1015
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          696..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1115..1170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           555..558
FT                   /note="DGEA"
FT   MOTIF           1182..1186
FT                   /note="FIG[AQ]Y"
FT   COMPBIAS        1115..1148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            753..754
FT                   /note="Cleavage; by ADAM8"
FT   SITE            1040..1041
FT                   /note="Cleavage; by ADAM8"
FT   MOD_RES         1148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        562
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        767
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        822
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        945
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1027
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        153..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        262..310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        352..401
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        445..494
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        536..591
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         227
FT                   /note="S -> LKHASDSSSSTEICSQA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020083"
FT   VAR_SEQ         1016..1070
FT                   /note="SKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETR
FT                   GRE -> K (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020084"
FT   VAR_SEQ         1138..1209
FT                   /note="SDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGA
FT                   KEKGSVESNGSSTATFPLRA -> RKMVLKQKLLSWSSSRGRTFYSCTKNTLFDGSSVD
FT                   MKTLQPLRYFSSNKHT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020085"
FT   MUTAGEN         555..558
FT                   /note="DGEA->AGEV: Inhibition of migration potentiation."
FT                   /evidence="ECO:0000269|PubMed:12721290"
FT   MUTAGEN         1186
FT                   /note="Y->A: Inhibition of migration potentiation."
FT                   /evidence="ECO:0000269|PubMed:12721290"
FT   CONFLICT        50
FT                   /note="D -> G (in Ref. 2; BAC35247)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="D -> E (in Ref. 6; CAC88131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="I -> V (in Ref. 2; BAC35247)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        602
FT                   /note="E -> K (in Ref. 1; CAA63972)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        612
FT                   /note="P -> G (in Ref. 1; CAA63972)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1209 AA;  135074 MW;  2C689475920AB84C CRC64;
     MMELPLCGRG LILSLIFLLL KLSAAEIPLS VQQVPTIVKQ SYVQVAFPFD EYFQIECEAK
     GNPEPIFSWT KDDKPFDLSD PRIIAANNSG TFKIPNEGHI SHFQGKYRCF ASNRLGTAVS
     EEIEFIVPGV PKFPKEKIEP IDVEEGDSIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV
     YMSQRGDLYF ANVEENDSRN DYCCFAAFPK LRTIVQKMPM KLTVNSSNSI KQRKPKLLLP
     PAQMGSLSAK TVLKGDTLLL ECFAEGLPTP HIQWSKPGSE LPEGRATIEV HEKTLKIENI
     SYQDRGNYRC TANNLLGKAS HDFHVTVEEP PRWKKKPQSA VYSTGSSGIL LCEAEGEPQP
     TIKWRLNGLP IEKHPFPGDF MFPREISFTN LLPNHTGVYQ CEASNIHGTI LANANIDVID
     VIPLIKTKNE ENYATVVGYS AFLHCEYFAS PKATVVWEVA DETHPLEGDR YHTHENGTLE
     IYRTTEEDAG SYSCWVDNAM GKAVITANLD IRNATKLRVS PKNPRIPKSH VLELYCESQC
     DSHLKHSLKL SWSKDGEAFE MNGTEDGRIV IDGAYLTISN ITAEDQGVYS CSAQTSLDST
     SEKTQVTVLG VPDPPGNLHL SERQNRSVRL SWEAGDDHNS KISEYIVEFE GNREEPGKWE
     ELTRVQGEET DVVLSLAPYV RYQFRVTAVN EVGRSHASLP SDHHETPPAA PDKNPQNIRV
     QASQPKEMII KWEPLKSMEQ NGPGLEYKVS WKPQGAPEEW EEEIVTNHTL RVMTPTVYAP
     YDVKVQAINQ LGSSPDPQPV TLYSGEDYPS TAPVIQRVDV MNSTLVKVTW SSIPKETVHG
     LLRGYQINWW KTKSLLDGRT HPKEVNILRF SGQRNSGMVP SLDPFSEFHL TVLAYNSKGA
     GPESEPYIFQ TPEGVPEQPS FLKVIKVDKD TATLSWGLPK KLNGNLTGYL LQYQIINDTY
     ELGELNEINV TTPSKSSWHL SNLNSTTKYK FYLRACTSRG CGKPISEEGA TLGEGSKGIR
     KITEGVNVTQ KIHPVEVLVP GAEHIVHLMT KNWGDNDSIF QDVIETRGRE YAGLYDDIST
     QGWFIGLMCA IALLTLILLT ICFVKRNRGG KYSVKEKEDL HPDPEVQSAK DETFGEYSDS
     DEKPLKGSLR SLNRNMQPTE SADSLVEYGE GDQSIFNEDG SFIGAYTGAK EKGSVESNGS
     STATFPLRA
//