L1CAM_MOUSE
ID L1CAM_MOUSE Reviewed; 1260 AA.
AC P11627;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 205.
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;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=3412448; DOI=10.1038/334701a0;
RA Moos M., Tacke R., Scherer H., Teplow D., Frueh K., Schachner M.;
RT "Neural adhesion molecule L1 as a member of the immunoglobulin superfamily
RT with binding domains similar to fibronectin.";
RL Nature 334:701-703(1988).
RN [2]
RP PROTEIN SEQUENCE OF 45-56; 449-472 AND 515-524, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP INTERACTION WITH BSG.
RX PubMed=12558975; DOI=10.1046/j.1471-4159.2003.01537.x;
RA Heller M., von der Ohe M., Kleene R., Mohajeri M.H., Schachner M.;
RT "The immunoglobulin-superfamily molecule basigin is a binding protein for
RT oligomannosidic carbohydrates: an anti-idiotypic approach.";
RL J. Neurochem. 84:557-565(2003).
RN [4]
RP TISSUE SPECIFICITY.
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-670; ASN-725; ASN-968 AND
RP ASN-978.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1181; SER-1184; SER-1246;
RP SER-1247 AND SER-1251, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
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 (By similarity). Interacts with isoform 2 of BSG
CC (PubMed:12558975). {ECO:0000250|UniProtKB:Q05695,
CC ECO:0000269|PubMed:12558975}.
CC -!- INTERACTION:
CC P11627; P34152: Ptk2; NbExp=4; IntAct=EBI-397964, EBI-77070;
CC P11627; Q8VI36: Pxn; NbExp=2; IntAct=EBI-397964, EBI-983394;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05695};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q05695}.
CC Cell projection, growth cone {ECO:0000250|UniProtKB:Q05695}.
CC Note=Colocalized with SHTN1 in close apposition with actin filaments in
CC filopodia and lamellipodia of axonalne growth cones of hippocampal
CC neurons. {ECO:0000250|UniProtKB:Q05695}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, including in the molecular
CC layer of the cerebellar cortex, the fiber-rich layers of the
CC hippocampus (alveus, and strata lacunosum moleculare, radiatum, and
CC oriens), the nerve fiber layer and the inner and outer plexiform layers
CC of the retina, and in the molecular layer of the olfactory bulb (at
CC protein level). {ECO:0000269|PubMed:12514225}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=N-CAM 140;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_190";
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; X12875; CAA31368.1; -; mRNA.
DR PIR; S05479; S05479.
DR AlphaFoldDB; P11627; -.
DR SMR; P11627; -.
DR CORUM; P11627; -.
DR IntAct; P11627; 7.
DR MINT; P11627; -.
DR STRING; 10090.ENSMUSP00000099935; -.
DR GlyConnect; 2537; 40 N-Linked glycans (13 sites).
DR GlyGen; P11627; 21 sites, 39 N-linked glycans (13 sites).
DR iPTMnet; P11627; -.
DR PhosphoSitePlus; P11627; -.
DR MaxQB; P11627; -.
DR PaxDb; P11627; -.
DR PeptideAtlas; P11627; -.
DR PRIDE; P11627; -.
DR ProteomicsDB; 263478; -.
DR ABCD; P11627; 8 sequenced antibodies.
DR MGI; MGI:96721; L1cam.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; P11627; -.
DR PhylomeDB; P11627; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-373760; L1CAM interactions.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR ChiTaRS; L1cam; mouse.
DR PRO; PR:P11627; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P11627; protein.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0044294; C:dendritic growth cone; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR GO; GO:0008046; F:axon guidance receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IDA:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; IPI:MGI.
DR GO; GO:0033691; F:sialic acid binding; IDA:MGI.
DR GO; GO:0061564; P:axon development; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0007413; P:axonal fasciculation; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IMP:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:MGI.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IMP:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
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; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell projection; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT CHAIN 20..1260
FT /note="Neural cell adhesion molecule L1"
FT /id="PRO_0000015023"
FT TOPO_DOM 20..1123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1124..1146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1147..1260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..130
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..1015
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1014..1112
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 1183..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1260
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 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32004"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32004"
FT MOD_RES 1246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000255"
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 478
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 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
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:0000269|PubMed:19349973"
FT CARBOHYD 978
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
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 1073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1107
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"
SQ SEQUENCE 1260 AA; 140969 MW; 22BE57001CB2A538 CRC64;
MVVMLRYVWP LLLCSPCLLI QIPDEYKGHH VLEPPVITEQ SPRRLVVFPT DDISLKCEAR
GRPQVEFRWT KDGIHFKPKE ELGVVVHEAP YSGSFTIEGN NSFAQRFQGI YRCYASNKLG
TAMSHEIQLV AEGAPKWPKE TVKPVEVEEG ESVVLPCNPP PSAAPPRIYW MNSKIFDIKQ
DERVSMGQNG DLYFANVLTS DNHSDYICNA HFPGTRTIIQ KEPIDLRVKP TNSMIDRKPR
LLFPTNSSSR LVALQGQSLI LECIAEGFPT PTIKWLHPSD PMPTDRVIYQ NHNKTLQLLN
VGEEDDGEYT CLAENSLGSA RHAYYVTVEA APYWLQKPQS HLYGPGETAR LDCQVQGRPQ
PEITWRINGM SMETVNKDQK YRIEQGSLIL SNVQPTDTMV TQCEARNQHG LLLANAYIYV
VQLPARILTK DNQTYMAVEG STAYLLCKAF GAPVPSVQWL DEEGTTVLQD ERFFPYANGT
LSIRDLQAND TGRYFCQAAN DQNNVTILAN LQVKEATQIT QGPRSAIEKK GARVTFTCQA
SFDPSLQASI TWRGDGRDLQ ERGDSDKYFI EDGKLVIQSL DYSDQGNYSC VASTELDEVE
SRAQLLVVGS PGPVPHLELS DRHLLKQSQV HLSWSPAEDH NSPIEKYDIE FEDKEMAPEK
WFSLGKVPGN QTSTTLKLSP YVHYTFRVTA INKYGPGEPS PVSESVVTPE AAPEKNPVDV
RGEGNETNNM VITWKPLRWM DWNAPQIQYR VQWRPQGKQE TWRKQTVSDP FLVVSNTSTF
VPYEIKVQAV NNQGKGPEPQ VTIGYSGEDY PQVSPELEDI TIFNSSTVLV RWRPVDLAQV
KGHLKGYNVT YWWKGSQRKH SKRHIHKSHI VVPANTTSAI LSGLRPYSSY HVEVQAFNGR
GLGPASEWTF STPEGVPGHP EALHLECQSD TSLLLHWQPP LSHNGVLTGY LLSYHPVEGE
SKEQLFFNLS DPELRTHNLT NLNPDLQYRF QLQATTQQGG PGEAIVREGG TMALFGKPDF
GNISATAGEN YSVVSWVPRK GQCNFRFHIL FKALPEGKVS PDHQPQPQYV SYNQSSYTQW
NLQPDTKYEI HLIKEKVLLH HLDVKTNGTG PVRVSTTGSF ASEGWFIAFV SAIILLLLIL
LILCFIKRSK GGKYSVKDKE DTQVDSEARP MKDETFGEYR SLESDNEEKA FGSSQPSLNG
DIKPLGSDDS LADYGGSVDV QFNEDGSFIG QYSGKKEKEA AGGNDSSGAT SPINPAVALE
