Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00933
Entry Name
UniProt Accession
Theoretical PI
4.73
Molecular Weight
119427.42
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Neural cell adhesion molecule 1
Protein Synonyms/Alias
N-CAM-1; NCAM-1; CD56;
Gene Name
Ncam1
Gene Synonyms/Alias
Ncam;
Created Date
01-JAN-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
733
Canonical
LVVMDITCYFLNKCG
[1]
S-Palmitoylation
739
Canonical
TCYFLNKCGLLMCIA
[1]
S-Palmitoylation
744
Canonical
NKCGLLMCIAVNLCG
[1]
S-Palmitoylation
750
Canonical
MCIAVNLCGKAGPGA
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Niethammer P, Delling M, Sytnyk V, Dityatev A, Fukami K, Schachner M.Cosignaling of NCAM via lipid rafts and the FGF receptor is required forneuritogenesis. J Cell Biol. 2002 Apr 29;157(3):521-32. Epub 2002 Apr 29.[PMID:11980923]
Functional Description
This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
Sequence Annotation
Topological domain: 20 711 Extracellular.
Transmembrane: 712 729 Helical.
Topological domain: 730 1115 Cytoplasmic.
Domain: 20 111 Ig-like C2-type 1.
Domain: 116 205 Ig-like C2-type 2.
Domain: 212 302 Ig-like C2-type 3.
Domain: 309 402 Ig-like C2-type 4.
Domain: 407 492 Ig-like C2-type 5.
Domain: 500 599 Fibronectin type-III 1.
Domain: 601 696 Fibronectin type-III 2.
Region: 152 156 Heparin-binding.
Region: 161 165 Heparin-binding.
Modified residue: 774 774 Phosphoserine.
Modified residue: 946 946 Phosphoserine.
Modified residue: 958 958 Phosphoserine.
Modified residue: 1005 1005 Phosphoserine.
Protein Length
1115 AA.
Protein Sequence
(Canonical)
MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE  60
KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF  120
KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK  180
KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF  240
PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS  300
IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKTLDGHM  360
VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEFQYAPKLQ GPVAVYTWEG  420
NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD SENDFGNYNC  480
TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS  540
LGEESWHFKW YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR  600
EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI RLPSGSDHVM  660
LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTAGLS TGAIVGILIV  720
IFVLLLVVMD ITCYFLNKCG LLMCIAVNLC GKAGPGAKGK DMEEGKAAFS KDESKEPIVE  780
VRTEEERTPN HDGGKHTEPN ETTPLTEPEL PADTTATVED MLPSVTTVTT NSDTITETFA  840
TAQNSPTSET TTLTSSIAPP ATTVPDSNSV PAGQATPSKG VTASSSSPAS APKVAPLVDL  900
SDTPTSAPSA SNLSSTVLAN QGAVLSPSTP ASAGETSKAP PASKASPAPT PTPAGAASPL  960
AAVAAPATDA PQAKQEAPST KGPDPEPTQP GTVKNPPEAA TAPASPKSKA ATTNPSQGED  1020
LKMDEGNFKT PDIDLAKDVF AALGSPRPAT GASGQASELA PSPADSAVPP APAKTEKGPV  1080
ETKSEPPESE AKPAPTEVKT VPNDATQTKE NESKA                             1115
FASTA
(Canonical)
>LipidDB-10090-00933|P13595
MLRTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGE
KLSPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVTAEDGTQSEATVNVKIFQKLMF
KNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIK
KTDEGTYRCEGRILARGEINFKDIQVIVNVPPTVQARQSIVNATANLGQSVTLVCDADGF
PEPTMSWTKDGEPIENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDAS
IHLKVFAKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKTLDGHM
VVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEFQYAPKLQGPVAVYTWEG
NQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNC
TAVNRIGQESLEFILVQADTPSSPSIDRVEPYSSTAQVQFDEPEATGGVPILKYKAEWKS
LGEESWHFKWYDAKEANMEGIVTIMGLKPETRYSVRLAALNGKGLGEISAATEFKTQPVR
EPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVKYRALASEWKPEIRLPSGSDHVM
LKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSAQPTAIPANGSPTAGLSTGAIVGILIV
IFVLLLVVMDITCYFLNKCGLLMCIAVNLCGKAGPGAKGKDMEEGKAAFSKDESKEPIVE
VRTEEERTPNHDGGKHTEPNETTPLTEPELPADTTATVEDMLPSVTTVTTNSDTITETFA
TAQNSPTSETTTLTSSIAPPATTVPDSNSVPAGQATPSKGVTASSSSPASAPKVAPLVDL
SDTPTSAPSASNLSSTVLANQGAVLSPSTPASAGETSKAPPASKASPAPTPTPAGAASPL
AAVAAPATDAPQAKQEAPSTKGPDPEPTQPGTVKNPPEAATAPASPKSKAATTNPSQGED
LKMDEGNFKTPDIDLAKDVFAALGSPRPATGASGQASELAPSPADSAVPPAPAKTEKGPV
ETKSEPPESEAKPAPTEVKTVPNDATQTKENESKA
Gene Ontology
GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW
GO:0030424; C:axon; IDA:MGI
GO:0005911; C:cell-cell junction; IDA:MGI
GO:0009897; C:external side of plasma membrane; IDA:MGI
GO:0030426; C:growth cone; IDA:MGI
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0043025; C:neuronal cell body; IDA:MGI
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0008201; F:heparin binding; IEA:UniProtKB-KW
GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI
GO:0034109; P:homotypic cell-cell adhesion; IMP:MGI
GO:0031175; P:neuron projection development; IGI:MGI
GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI
GO:0001928; P:regulation of exocyst assembly; IMP:MGI
Interpro
InterPro; IPR003961; Fibronectin_type3
InterPro; IPR007110; Ig-like_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR013098; Ig_I-set
InterPro; IPR003598; Ig_sub2
InterPro; IPR009138; Neural_cell_adh
Pfam
Pfam; PF00041; fn3;
Pfam; PF07679; I-set;
SMART
SMART; SM00060; FN3;
SMART; SM00408; IGc2;
PROSITE
PROSITE; PS50853; FN3;
PROSITE; PS50835; IG_LIKE;
PRINTS
PRINTS; PR01838; NCAMFAMILY;