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P13590 (NCAM1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neural cell adhesion molecule 1

Short name=N-CAM-1
Short name=NCAM-1
Gene names
Name:NCAM1
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1091 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.

Subcellular location

Cell membrane; Single-pass membrane protein Potential.

Sequence similarities

Contains 2 fibronectin type-III domains.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P13590-1)

Also known as: N-CAM 180;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P13590-2)

Also known as: N-CAM 140;

The sequence of this isoform differs from the canonical sequence as follows:
     771-809: Missing.
Isoform C (identifier: P13590-3)

The sequence of this isoform differs from the canonical sequence as follows:
     810-1070: Missing.
Isoform D (identifier: P13590-4)

The sequence of this isoform differs from the canonical sequence as follows:
     702-726: STSPTSGLGTAAIVGILIVIFVLLL → TLGSPSTSSSFVSLLLSAVTLLLLC
     727-1091: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 10911072Neural cell adhesion molecule 1
PRO_0000015007

Regions

Topological domain20 – 711692Extracellular Potential
Transmembrane712 – 72918Helical; Potential
Topological domain730 – 1091362Cytoplasmic Potential
Domain20 – 11394Ig-like C2-type 1
Domain116 – 20590Ig-like C2-type 2
Domain212 – 30190Ig-like C2-type 3
Domain308 – 40396Ig-like C2-type 4
Domain406 – 49590Ig-like C2-type 5
Domain496 – 595100Fibronectin type-III 1
Domain597 – 69296Fibronectin type-III 2
Region152 – 1565Heparin-binding Potential
Region161 – 1655Heparin-binding Potential

Amino acid modifications

Glycosylation2221N-linked (GlcNAc...)
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential
Glycosylation4491N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 96 By similarity
Disulfide bond139 ↔ 189 By similarity
Disulfide bond235 ↔ 287
Disulfide bond329 ↔ 385 By similarity
Disulfide bond426 ↔ 479 By similarity

Natural variations

Alternative sequence702 – 72625STSPT…FVLLL → TLGSPSTSSSFVSLLLSAVT LLLLC in isoform D.
VSP_002583
Alternative sequence727 – 1091365Missing in isoform D.
VSP_002584
Alternative sequence771 – 80939Missing in isoform B.
VSP_002585
Alternative sequence810 – 1070261Missing in isoform C.
VSP_002586

Secondary structure

....................... 1091
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (N-CAM 180) [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: B151367002DF88E0

FASTA1,091117,415
        10         20         30         40         50         60 
MLPAAALPWT LFFLGAAASL QVDIVPSQGE ISVGESKFFL CQVAGEAKYK DISWFSPNGE 

        70         80         90        100        110        120 
KLTPNQQRIS VVRNDDFSST LTIYNANIDD AGIYKCVVSS VEEGDSEATV NVKIFQKLMF 

       130        140        150        160        170        180 
KNAPTPQEFK EGDDAVIVCD VVSSLPPTII WKHKGRDVML KKDVRFIVLS NNYLQIRGIK 

       190        200        210        220        230        240 
KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPSVRARQST MNATANLSQS VTLACDADGF 

       250        260        270        280        290        300 
PEPTMTWTKD GEPIEQEDNE EKYSFNYDGS ELIIKKVDKS DEAEYICIAE NKAGEQDATI 

       310        320        330        340        350        360 
HLKVFAKPKI TYVENKTAME LEDQITLTCE ASGDPIPSIT WKTSTRNISN EEKTLDGRIV 

       370        380        390        400        410        420 
VRSHARVSSL TLKEIQYTDA GEYVCTASNT IGQDSQAMYL EVQYAPKLQG PVAVYTWEGN 

       430        440        450        460        470        480 
QVNITCEVFA YPSAVISWFR DGQLLPSSNY SNIKIYNTPS ASYLEVTPDS ENDFGNYNCT 

       490        500        510        520        530        540 
AVNRIGQESS EFILVQADTP SSPSIDRVEP YSSTARVEFD EPEATGGVPI LKYKAEWRAL 

       550        560        570        580        590        600 
GEGEWHSRLY DAKEANVEGT ITISGLKPET TYSVRLSAVN GKGVGEISLP SDFKTQPVRE 

       610        620        630        640        650        660 
PSAPKLEGQM GEDGNSIKVN VIKQDDGGSP IRHYLIKYKA KHSSEWKPEI RLPSGIDHVM 

       670        680        690        700        710        720 
LKSLDWNAEY EVYVIAENQQ GKSKPAHYAF RTSAQPTVIP ASTSPTSGLG TAAIVGILIV 

       730        740        750        760        770        780 
IFVLLLVAVD VTCYFLNKCG LLMCIAVNLC GKSGPGAKGK DMEEGKAAFS KDESKEPIVE 

       790        800        810        820        830        840 
VRTEEERTPN HDGGKHTEPN ETTPLTEPEH TADTAATVED MLPSVTTGTT NSDTITETFA 

       850        860        870        880        890        900 
TAQNSPTSET TTLTSSIAPP ATAIPDSNAM SPGQATPAKA GASPVSPPPP SSTPKVAPLV 

       910        920        930        940        950        960 
DLSDTPSSAP ATNNLSSSVL SNQGAVLSPS TVANMAETSK AAAGNKSAAP TPANLTSPPA 

       970        980        990       1000       1010       1020 
PSEPKQEVSS TKSPEKEAAQ PSTVKSPTET AKNPSNPKSE AASGGTTNPS QNEDFKMDEG 

      1030       1040       1050       1060       1070       1080 
TFKTPDIDLA KDVFAALGTT TPASVASGQA RELASSTADS SVPAAPAKTE KTPVEDKSEV 

      1090 
QATEIRHLQQ K 

« Hide

Isoform B (N-CAM 140) [UniParc].

Checksum: 9177244881747480
Show »

FASTA1,052112,977
Isoform C [UniParc].

Checksum: A07527ADC5CCCBD1
Show »

FASTA83091,573
Isoform D [UniParc].

Checksum: E08171FD649020C5
Show »

FASTA72680,219

References

[1]"Neural cell adhesion molecule: structure, immunoglobulin-like domains, cell surface modulation, and alternative RNA splicing."
Cunningham B.A., Hemperly J.J., Murray B.A., Prediger E.A., Brackenbury R., Edelman G.M.
Science 236:799-806(1987) [PubMed: 3576199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-175, PARTIAL PROTEIN SEQUENCE.
[2]"Sequence of a cDNA clone encoding the polysialic acid-rich and cytoplasmic domains of the neural cell adhesion molecule N-CAM."
Hemperly J.J., Murray B.A., Edelman G.M., Cunningham B.A.
Proc. Natl. Acad. Sci. U.S.A. 83:3037-3041(1986) [PubMed: 3458261] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-1091, PARTIAL PROTEIN SEQUENCE.
[3]"cDNA clones of the neural cell adhesion molecule (N-CAM) lacking a membrane-spanning region consistent with evidence for membrane attachment via a phosphatidylinositol intermediate."
Hemperly J.J., Edelman G.M., Cunningham B.A.
Proc. Natl. Acad. Sci. U.S.A. 83:9822-9826(1986) [PubMed: 3467341] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM D).
[4]"Cell surface modulation of the neural cell adhesion molecule resulting from alternative mRNA splicing in a tissue-specific developmental sequence."
Murray B.A., Owens G.C., Prediger E.A., Crossin K.L., Cunningham B.A., Edelman G.M.
J. Cell Biol. 103:1431-1439(1986) [PubMed: 3771645] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 810-1069.
[5]"Conserved regulatory elements in the promoter region of the N-CAM gene."
Colwell G., Li B., Forrest D., Brackenbury R.
Genomics 14:875-882(1992) [PubMed: 1478668] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
[6]Sasner M., Covault J.
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
Strain: White leghorn.
Tissue: Erythrocyte.
[7]"Topographic localization of the heparin-binding domain of the neural cell adhesion molecule N-CAM."
Cole G.J., Loewy A., Cross N.V., Akeson R., Glaser L.
J. Cell Biol. 103:1739-1744(1986) [PubMed: 2430978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-29.
[8]"Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM."
Rao Y., Wu X.F., Gariepy J., Rutishauser U., Siu C.H.
J. Cell Biol. 118:937-949(1992) [PubMed: 1380002] [Abstract]
Cited for: CELL-BINDING.
[9]"Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: can solution studies define the mechanism of homophilic binding?"
Atkins A.R., Chung J., Deechongkit S., Little E.B., Edelman G.M., Wright P.E., Cunningham B.A., Dyson H.J.
J. Mol. Biol. 311:161-172(2001) [PubMed: 11469865] [Abstract]
Cited for: STRUCTURE BY NMR OF 202-307.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15861 expand/collapse EMBL AC list , M15860, M15922, M15923, M15924, M21178, M21179, M21180, M15929, M15930, M15931, M15932, M15933, M15934, L29437, M15935, M15937, M15938, M15939 Genomic DNA. Translation: AAB59958.1.
M15861 expand/collapse EMBL AC list , M15860, M15922, M15923, M15924, M21178, M21179, M21180, M15929, M15930, M15931, M15932, M15934, L29437, M15935, M15937, M15939 Genomic DNA. Translation: AAB59959.1.
M15936 expand/collapse EMBL AC list , M15860, M15922, M15923, M15924, M21178, M21179, M21180, M15929, M15930, M15931, M15932, M15934, L29437, M15935 Genomic DNA. Translation: AAB59957.1.
X04479 Genomic DNA. Translation: CAB51638.1.
X70342 Genomic DNA. Translation: CAA49807.1.
Z12128 Genomic DNA. Translation: CAA78113.1.
IPIIPI00591580.
IPI00591739.
IPI00595516.
IPI00680755.
PIRIJCHNL. A43613.
RefSeqNP_001122300.1. NM_001128828.1.
UniGeneGga.47595.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IE5NMR-A202-307[»]
ProteinModelPortalP13590.
SMRP13590. Positions 20-307, 496-693.
ModBaseSearch...

Protein-protein interaction databases

IntActP13590. 1 interaction.
STRINGP13590.

Proteomic databases

PRIDEP13590.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID428253.
KEGGgga:428253.

Organism-specific databases

CTD255239.

Phylogenomic databases

eggNOGveNOG05507.
GeneTreeENSGT00600000084036.
HOGENOMHBG444274.
HOVERGENHBG052579.
InParanoidP13590.
OrthoDBEOG40VVP1.

Enzyme and pathway databases

ReactomeREACT_115433. Developmental Biology.

Family and domain databases

InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR009138. Neural_cell_adh.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 7 hits.
KOK06491.
PfamPF00041. fn3. 2 hits.
PF07679. I-set. 5 hits.
[Graphical view]
PRINTSPR01838. NCAMFAMILY.
SMARTSM00060. FN3. 2 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 2 hits.
PROSITEPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNCAM1_CHICK
AccessionPrimary (citable) accession number: P13590
Secondary accession number(s): Q90918, Q90919
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 15, 1998
Last modified: November 16, 2011
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families