ID   L1CAM_RAT               Reviewed;        1259 AA.
AC   Q05695;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 3.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Neural cell adhesion molecule L1;
DE            Short=N-CAM-L1;
DE            Short=NCAM-L1;
DE   AltName: Full=Nerve-growth factor-inducible large external glycoprotein;
DE            Short=NILE;
DE   AltName: CD_antigen=CD171;
DE   Flags: Precursor;
GN   Name=L1cam; Synonyms=Caml1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION.
RX   PubMed=1894011; DOI=10.1016/0014-5793(91)80915-p;
RA   Miura M., Kobayashi M., Asou H., Uyemura K.;
RT   "Molecular cloning of cDNA encoding the rat neural cell adhesion molecule
RT   L1. Two L1 isoforms in the cytoplasmic region are produced by differential
RT   splicing.";
RL   FEBS Lett. 289:91-95(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1159-1237.
RX   PubMed=2466966; DOI=10.1523/jneurosci.09-03-00876.1989;
RA   Prince J.T., Milona N., Stallcup W.B.;
RT   "Characterization of a partial cDNA clone for the NILE glycoprotein and
RT   identification of the encoded polypeptide domain.";
RL   J. Neurosci. 9:876-883(1989).
RN   [3]
RP   ERRATUM OF PUBMED:2466966.
RX   PubMed=2723751; DOI=10.1523/jneurosci.09-05-01825.1989;
RA   Prince J.T., Milona N., Stallcup W.B.;
RL   J. Neurosci. 9:1825-1834(1989).
RN   [4]
RP   INTERACTION WITH SHTN1, AND SUBCELLULAR LOCATION.
RX   PubMed=18519736; DOI=10.1083/jcb.200712138;
RA   Shimada T., Toriyama M., Uemura K., Kamiguchi H., Sugiura T., Watanabe N.,
RA   Inagaki N.;
RT   "Shootin1 interacts with actin retrograde flow and L1-CAM to promote axon
RT   outgrowth.";
RL   J. Cell Biol. 181:817-829(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1180; SER-1183; SER-1196;
RP   SER-1245 AND SER-1246, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179
RP   (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202; ASN-670; ASN-725; ASN-978
RP   AND ASN-1072, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
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:0000250|UniProtKB:P32004}.
CC   -!- SUBUNIT: Interacts with SHTN1; the interaction occurs in axonal growth
CC       cones (PubMed:18519736). Interacts with isoform 2 of BSG (By
CC       similarity). {ECO:0000250|UniProtKB:P11627,
CC       ECO:0000269|PubMed:18519736}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:1894011};
CC       Single-pass type I membrane protein {ECO:0000305|PubMed:1894011}. Cell
CC       projection, growth cone {ECO:0000269|PubMed:18519736}. Note=Colocalized
CC       with SHTN1 in close apposition with actin filaments in filopodia and
CC       lamellipodia of axonal growth cones of hippocampal neurons
CC       (PubMed:18519736). {ECO:0000269|PubMed:18519736}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q05695-1; Sequence=Displayed;
CC       Name=2; Synonyms=L1cs;
CC         IsoId=Q05695-2; Sequence=VSP_002592;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is predominantly found in the brain,
CC       while isoform 1 is found in the peripheral nervous system.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC       L1/neurofascin/NgCAM family. {ECO:0000305}.
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DR   EMBL; X59149; CAA41860.1; -; mRNA.
DR   PIR; S36126; S36126.
DR   RefSeq; NP_059041.1; NM_017345.1.
DR   AlphaFoldDB; Q05695; -.
DR   SMR; Q05695; -.
DR   BioGRID; 248425; 3.
DR   STRING; 10116.ENSRNOP00000075314; -.
DR   GlyCosmos; Q05695; 19 sites, 17 glycans.
DR   GlyGen; Q05695; 19 sites, 17 N-linked glycans (7 sites).
DR   iPTMnet; Q05695; -.
DR   PhosphoSitePlus; Q05695; -.
DR   SwissPalm; Q05695; -.
DR   jPOST; Q05695; -.
DR   PaxDb; 10116-ENSRNOP00000053191; -.
DR   GeneID; 50687; -.
DR   KEGG; rno:50687; -.
DR   AGR; RGD:619777; -.
DR   CTD; 3897; -.
DR   RGD; 619777; L1cam.
DR   eggNOG; KOG3513; Eukaryota.
DR   InParanoid; Q05695; -.
DR   OrthoDB; 2912783at2759; -.
DR   PhylomeDB; Q05695; -.
DR   Reactome; R-RNO-373760; L1CAM interactions.
DR   Reactome; R-RNO-437239; Recycling pathway of L1.
DR   Reactome; R-RNO-445095; Interaction between L1 and Ankyrins.
DR   Reactome; R-RNO-445144; Signal transduction by L1.
DR   PRO; PR:Q05695; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0044294; C:dendritic growth cone; IDA:RGD.
DR   GO; GO:0005768; C:endosome; IDA:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0043195; C:terminal bouton; ISO:RGD.
DR   GO; GO:0008046; F:axon guidance receptor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0005178; F:integrin binding; ISO:RGD.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0043621; F:protein self-association; ISO:RGD.
DR   GO; GO:0033691; F:sialic acid binding; ISO:RGD.
DR   GO; GO:0061564; P:axon development; ISS:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0007413; P:axonal fasciculation; IMP:RGD.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR   GO; GO:0033631; P:cell-cell adhesion mediated by integrin; ISO:RGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISS:UniProtKB.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR   GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR   GO; GO:0097069; P:cellular response to thyroxine stimulus; IEP:RGD.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR   GO; GO:0071542; P:dopaminergic neuron differentiation; IEP:RGD.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR   GO; GO:0034109; P:homotypic cell-cell adhesion; ISO:RGD.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0045773; P:positive regulation of axon extension; IMP:UniProtKB.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:RGD.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:RGD.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:RGD.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR   GO; GO:0014823; P:response to activity; IEP:RGD.
DR   GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
DR   GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
DR   CDD; cd00063; FN3; 4.
DR   CDD; cd05876; Ig3_L1-CAM; 1.
DR   CDD; cd05733; IgI_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: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; 4.
DR   Pfam; PF13927; Ig_3; 1.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..1259
FT                   /note="Neural cell adhesion molecule L1"
FT                   /id="PRO_0000015024"
FT   TOPO_DOM        20..1122
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1123..1145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1146..1259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..128
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          138..225
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          239..327
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          332..419
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          424..506
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          517..600
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          613..711
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          716..809
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          811..916
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          919..1014
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1016..1116
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          697..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1182..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1228..1259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           553..555
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           562..564
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32004"
FT   MOD_RES         1180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1250
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32004"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        504
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        670
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        725
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        776
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        824
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        848
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        875
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        968
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        978
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        1021
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1029
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1072
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        1106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        157..208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        263..311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        353..403
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        447..496
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        538..590
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1179..1182
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1894011"
FT                   /id="VSP_002592"
FT   CONFLICT        1200
FT                   /note="D -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1236
FT                   /note="E -> K (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q05695-2:1179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   1259 AA;  140935 MW;  0F12A7C4415F3C08 CRC64;
     MVMMLWYVLP LLLCSPCLLI QIPDEYKGHH VLEPPVITEQ SPRRLVVFPT DDISLKCEAR
     GRPQVEFRWT KDGIHFKPKE ELGVVVHEAP YSGSFTIEGN NSFAQRFQGI YRCYASNNLG
     TAMSHEIQLV AEGAPKWPKE TVKPVEVEEG ESVVLPCNPP PSAAPLRIYW MNSKILHIKQ
     DERVSMGQNG DLYFANVLTS DNHSDYICNA HFPGTRTIIQ KEPIDLRVKP TNSMIDRKPR
     LLFPTNSSSH LVALQGQSLI LECIAEGFPT PTIKWLHPSD PMPTDRVIYQ NHNKTLQLLN
     VGEEDDGEYT CLAENSLGSA RHAYYVTVEA APYWLQKPQS HLYGPGETAR LDCQVQGRPQ
     PEVTWRINGM SIEKVNKDQK YRIEQGSLIL SNVQPSDTMV TQCEARNQHG LLLANAYIYV
     VQLPARILTK DNQTYMAVEG STAYLLCKAF GAPVPSVQWL DEEGTTVLQD ERFFPYANGH
     LGIRDLQAND TGRYFCQAAN DQNNVTILAN LQVKEATQIT QGPRSTIEKK GARVTFTCQA
     SFDPSLQASI TWRGDGRDLQ ERGDSDKYFI EDGQLVIKSL DYSDQGDYSC VASTELDEVE
     SRAQLLVVGS PGPVPHLELS DRHLLKQSQV HLSWSPAEDH NSPIEKYDIE FEDKEMAPEK
     WFSLGKVPGN QTSTTLKLSP YVHYTFRVTA INKYGPGEPS PVSETVVTPE AAPEKNPVDV
     RGEGNETNNM VITWKPLRWM DWNAPQIQYR VQWRPLGKQE TWKEQTVSDP FLVVSNTSTF
     VPYEIKVQAV NNQGKGPEPQ VTIGYSGEDY PQVSPELEDI TIFNSSTVLV RWRPVDLAQV
     KGHLRGYNVT YWWKGSQRKH SKRHVHKSHM VVPANTTSAI LSGLRPYSSY HVEVQAFNGR
     GLGPASEWTF STPEGVPGHP EALHLECQSD TSLLLHWQPP LSHNGVLTGY LLSYHPLDGE
     SKEQLFFNLS DPELRTHNLT NLNPDLQYRF QLQATTHQGP GEAIVREGGT MALFGKPDFG
     NISVTAGENY SVVSWVPREG QCNFRFHILF KALPEGKVSP DHQPQPQYVS YNQSSYTQWD
     LQPDTKYEIH LMREKVLLHH LAVKTNGTGP VRVSTTGSFA SEGWFIAFVS AIILLLLILL
     ILCFIKRSKG GKYSVKDKED TQVDSEARPM KDETFGEYRS LESDNEEKAF GSSQPSLNGD
     IKPLGSDDSL ADYGGSVDVQ FNEDGSFIGQ YSGKKEKEAA GGNDSSGATS PINPAVALE
//