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Protein

Neural cell adhesion molecule L1

Gene

L1cam

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell adhesion molecule with an important role in the development of the nervous system. Involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. Binds to axonin on neurons.

GO - Molecular functioni

  • identical protein binding Source: MGI
  • integrin binding Source: MGI
  • protein self-association Source: MGI
  • sialic acid binding Source: MGI

GO - Biological processi

  • axon guidance Source: MGI
  • cell-cell adhesion mediated by integrin Source: MGI
  • cell surface receptor signaling pathway Source: MGI
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: MGI
  • homotypic cell-cell adhesion Source: MGI
  • leukocyte cell-cell adhesion Source: MGI
  • neuron projection development Source: MGI
  • positive regulation of axon extension Source: UniProtKB
  • positive regulation of calcium-mediated signaling Source: MGI
  • positive regulation of cell-cell adhesion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion, Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-MMU-373760. L1CAM interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Neural cell adhesion molecule L1
Short name:
N-CAM-L1
Short name:
NCAM-L1
Alternative name(s):
CD_antigen: CD171
Gene namesi
Name:L1cam
Synonyms:Caml1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96721. L1cam.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Cell projectiongrowth cone By similarity

  • Note: Colocalized with SHTN1 in close apposition with actin filaments in filopodia and lamellipodia of axonalne growth cones of hippocampal neurons.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 1123ExtracellularSequence analysisAdd BLAST1104
Transmembranei1124 – 1146HelicalSequence analysisAdd BLAST23
Topological domaini1147 – 1260CytoplasmicSequence analysisAdd BLAST114

GO - Cellular componenti

  • axonal growth cone Source: UniProtKB
  • cell surface Source: MGI
  • external side of plasma membrane Source: MGI
  • focal adhesion Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • plasma membrane Source: Reactome
  • presynaptic membrane Source: MGI
  • terminal bouton Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Add BLAST19
ChainiPRO_000001502320 – 1260Neural cell adhesion molecule L1Add BLAST1241

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi57 ↔ 113PROSITE-ProRule annotation
Glycosylationi100N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi157 ↔ 208PROSITE-ProRule annotation
Glycosylationi202N-linked (GlcNAc...)Sequence analysis1
Glycosylationi246N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi263 ↔ 311PROSITE-ProRule annotation
Glycosylationi293N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi353 ↔ 403PROSITE-ProRule annotation
Glycosylationi432N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi447 ↔ 496PROSITE-ProRule annotation
Glycosylationi478N-linked (GlcNAc...)Sequence analysis1
Glycosylationi489N-linked (GlcNAc...)Sequence analysis1
Glycosylationi504N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi538 ↔ 590PROSITE-ProRule annotation
Glycosylationi587N-linked (GlcNAc...)Sequence analysis1
Glycosylationi670N-linked (GlcNAc...)1 Publication1
Glycosylationi725N-linked (GlcNAc...)1 Publication1
Glycosylationi776N-linked (GlcNAc...)Sequence analysis1
Glycosylationi824N-linked (GlcNAc...)Sequence analysis1
Glycosylationi848N-linked (GlcNAc...)Sequence analysis1
Glycosylationi875N-linked (GlcNAc...)Sequence analysis1
Glycosylationi968N-linked (GlcNAc...)1 Publication1
Glycosylationi978N-linked (GlcNAc...)1 Publication1
Glycosylationi1022N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1030N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1073N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1107N-linked (GlcNAc...)Sequence analysis1
Modified residuei1166PhosphoserineBy similarity1
Modified residuei1181PhosphoserineCombined sources1
Modified residuei1184PhosphoserineCombined sources1
Modified residuei1197PhosphoserineBy similarity1
Modified residuei1246PhosphoserineCombined sources1
Modified residuei1247PhosphoserineCombined sources1
Modified residuei1251PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP11627.
PaxDbiP11627.
PeptideAtlasiP11627.
PRIDEiP11627.

PTM databases

iPTMnetiP11627.
PhosphoSitePlusiP11627.

Miscellaneous databases

PMAP-CutDBP11627.

Expressioni

Gene expression databases

CleanExiMM_L1CAM.

Interactioni

Subunit structurei

Interacts with SHTN1; the interaction occurs in axonal growth cones.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Ptk2P341524EBI-397964,EBI-77070
PxnQ8VI362EBI-397964,EBI-983394

GO - Molecular functioni

  • identical protein binding Source: MGI
  • integrin binding Source: MGI
  • protein self-association Source: MGI

Protein-protein interaction databases

IntActiP11627. 10 interactors.
MINTiMINT-1177002.
STRINGi10090.ENSMUSP00000099935.

Structurei

3D structure databases

ProteinModelPortaliP11627.
SMRiP11627.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 130Ig-like C2-type 1Add BLAST96
Domaini138 – 225Ig-like C2-type 2Add BLAST88
Domaini239 – 327Ig-like C2-type 3Add BLAST89
Domaini332 – 419Ig-like C2-type 4Add BLAST88
Domaini424 – 506Ig-like C2-type 5Add BLAST83
Domaini517 – 600Ig-like C2-type 6Add BLAST84
Domaini613 – 711Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST99
Domaini716 – 809Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST94
Domaini811 – 916Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST106
Domaini919 – 1015Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST97
Domaini1014 – 1112Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST99

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi553 – 555Cell attachment siteSequence analysis3
Motifi562 – 564Cell attachment siteSequence analysis3

Sequence similaritiesi

Contains 5 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
HOGENOMiHOG000231380.
HOVERGENiHBG000144.
InParanoidiP11627.
PhylomeDBiP11627.

Family and domain databases

CDDicd00063. FN3. 4 hits.
Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR026966. Neurofascin/L1/NrCAM_C.
[Graphical view]
PfamiPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 4 hits.
PF07679. I-set. 3 hits.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 6 hits.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11627-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVMLRYVWP LLLCSPCLLI QIPDEYKGHH VLEPPVITEQ SPRRLVVFPT
60 70 80 90 100
DDISLKCEAR GRPQVEFRWT KDGIHFKPKE ELGVVVHEAP YSGSFTIEGN
110 120 130 140 150
NSFAQRFQGI YRCYASNKLG TAMSHEIQLV AEGAPKWPKE TVKPVEVEEG
160 170 180 190 200
ESVVLPCNPP PSAAPPRIYW MNSKIFDIKQ DERVSMGQNG DLYFANVLTS
210 220 230 240 250
DNHSDYICNA HFPGTRTIIQ KEPIDLRVKP TNSMIDRKPR LLFPTNSSSR
260 270 280 290 300
LVALQGQSLI LECIAEGFPT PTIKWLHPSD PMPTDRVIYQ NHNKTLQLLN
310 320 330 340 350
VGEEDDGEYT CLAENSLGSA RHAYYVTVEA APYWLQKPQS HLYGPGETAR
360 370 380 390 400
LDCQVQGRPQ PEITWRINGM SMETVNKDQK YRIEQGSLIL SNVQPTDTMV
410 420 430 440 450
TQCEARNQHG LLLANAYIYV VQLPARILTK DNQTYMAVEG STAYLLCKAF
460 470 480 490 500
GAPVPSVQWL DEEGTTVLQD ERFFPYANGT LSIRDLQAND TGRYFCQAAN
510 520 530 540 550
DQNNVTILAN LQVKEATQIT QGPRSAIEKK GARVTFTCQA SFDPSLQASI
560 570 580 590 600
TWRGDGRDLQ ERGDSDKYFI EDGKLVIQSL DYSDQGNYSC VASTELDEVE
610 620 630 640 650
SRAQLLVVGS PGPVPHLELS DRHLLKQSQV HLSWSPAEDH NSPIEKYDIE
660 670 680 690 700
FEDKEMAPEK WFSLGKVPGN QTSTTLKLSP YVHYTFRVTA INKYGPGEPS
710 720 730 740 750
PVSESVVTPE AAPEKNPVDV RGEGNETNNM VITWKPLRWM DWNAPQIQYR
760 770 780 790 800
VQWRPQGKQE TWRKQTVSDP FLVVSNTSTF VPYEIKVQAV NNQGKGPEPQ
810 820 830 840 850
VTIGYSGEDY PQVSPELEDI TIFNSSTVLV RWRPVDLAQV KGHLKGYNVT
860 870 880 890 900
YWWKGSQRKH SKRHIHKSHI VVPANTTSAI LSGLRPYSSY HVEVQAFNGR
910 920 930 940 950
GLGPASEWTF STPEGVPGHP EALHLECQSD TSLLLHWQPP LSHNGVLTGY
960 970 980 990 1000
LLSYHPVEGE SKEQLFFNLS DPELRTHNLT NLNPDLQYRF QLQATTQQGG
1010 1020 1030 1040 1050
PGEAIVREGG TMALFGKPDF GNISATAGEN YSVVSWVPRK GQCNFRFHIL
1060 1070 1080 1090 1100
FKALPEGKVS PDHQPQPQYV SYNQSSYTQW NLQPDTKYEI HLIKEKVLLH
1110 1120 1130 1140 1150
HLDVKTNGTG PVRVSTTGSF ASEGWFIAFV SAIILLLLIL LILCFIKRSK
1160 1170 1180 1190 1200
GGKYSVKDKE DTQVDSEARP MKDETFGEYR SLESDNEEKA FGSSQPSLNG
1210 1220 1230 1240 1250
DIKPLGSDDS LADYGGSVDV QFNEDGSFIG QYSGKKEKEA AGGNDSSGAT
1260
SPINPAVALE
Length:1,260
Mass (Da):140,969
Last modified:October 1, 1989 - v1
Checksum:i22BE57001CB2A538
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12875 mRNA. Translation: CAA31368.1.
PIRiS05479.
UniGeneiMm.260568.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

N-CAM 140

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12875 mRNA. Translation: CAA31368.1.
PIRiS05479.
UniGeneiMm.260568.

3D structure databases

ProteinModelPortaliP11627.
SMRiP11627.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11627. 10 interactors.
MINTiMINT-1177002.
STRINGi10090.ENSMUSP00000099935.

PTM databases

iPTMnetiP11627.
PhosphoSitePlusiP11627.

Proteomic databases

MaxQBiP11627.
PaxDbiP11627.
PeptideAtlasiP11627.
PRIDEiP11627.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:96721. L1cam.

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
HOGENOMiHOG000231380.
HOVERGENiHBG000144.
InParanoidiP11627.
PhylomeDBiP11627.

Enzyme and pathway databases

ReactomeiR-MMU-373760. L1CAM interactions.

Miscellaneous databases

ChiTaRSiL1cam. mouse.
PMAP-CutDBP11627.
PROiP11627.
SOURCEiSearch...

Gene expression databases

CleanExiMM_L1CAM.

Family and domain databases

CDDicd00063. FN3. 4 hits.
Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR026966. Neurofascin/L1/NrCAM_C.
[Graphical view]
PfamiPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 4 hits.
PF07679. I-set. 3 hits.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 6 hits.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiL1CAM_MOUSE
AccessioniPrimary (citable) accession number: P11627
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 30, 2016
This is version 172 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.