L1CAM_RAT
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 25-MAY-2022, entry version 175.
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. [Q05695-2]
DR AlphaFoldDB; Q05695; -.
DR SMR; Q05695; -.
DR BioGRID; 248425; 3.
DR STRING; 10116.ENSRNOP00000053191; -.
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; Q05695; -.
DR PRIDE; Q05695; -.
DR GeneID; 50687; -.
DR KEGG; rno:50687; -.
DR CTD; 3897; -.
DR RGD; 619777; L1cam.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; Q05695; -.
DR OrthoDB; 434404at2759; -.
DR PhylomeDB; Q05695; -.
DR Reactome; R-RNO-210991; Basigin interactions.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA: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; EXP: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: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; EXP: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 Gene3D; 2.60.40.10; -; 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 Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
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
