NCAM1_BOVIN
ID NCAM1_BOVIN Reviewed; 853 AA.
AC P31836;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Neural cell adhesion molecule 1;
DE Short=N-CAM-1;
DE Short=NCAM-1;
DE Flags: Precursor;
GN Name=NCAM1; Synonyms=NCAM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain cortex;
RX PubMed=2776887; DOI=10.1016/0014-5793(89)81011-7;
RA Lipkin V.M., Khramtsov N.V., Andreeva S.G., Moshnyakov M.V.,
RA Petukhova G.V., Rakitina T.V., Feshchenko E.A., Ishchenko K.A.,
RA Mirzoeva S.F., Chernova M.N., Dranytsyna S.M.;
RT "Calmodulin-independent bovine brain adenylate cyclase. Amino acid sequence
RT and nucleotide sequence of the corresponding cDNA.";
RL FEBS Lett. 254:69-73(1989).
RN [2]
RP PROTEIN SEQUENCE OF 20-36.
RX PubMed=3512556; DOI=10.1016/s0021-9258(17)35796-4;
RA Rougon G., Marshak D.R.;
RT "Structural and immunological characterization of the amino-terminal domain
RT of mammalian neural cell adhesion molecules.";
RL J. Biol. Chem. 261:3396-3401(1986).
RN [3]
RP IDENTIFICATION AS N-CAM.
RX PubMed=1765159; DOI=10.1016/0014-5793(91)81425-8;
RA Premont R.T.;
RT "A bovine brain cDNA purported to encode calmodulin-insensitive adenylyl
RT cyclase has extensive identity with neural cell adhesion molecules (N-
RT CAMs).";
RL FEBS Lett. 295:230-231(1991).
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC -!- SUBUNIT: Interacts with MDK. {ECO:0000250|UniProtKB:P13595}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1; Synonyms=N-CAM 140;
CC IsoId=P31836-1; Sequence=Displayed;
CC -!- CAUTION: Was originally thought to be a calmodulin-independent
CC adenylate cyclase. {ECO:0000305|PubMed:2776887}.
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; X16451; CAA34470.1; -; mRNA.
DR PIR; A32976; IJBONC.
DR RefSeq; NP_776824.1; NM_174399.1.
DR AlphaFoldDB; P31836; -.
DR BMRB; P31836; -.
DR SMR; P31836; -.
DR STRING; 9913.ENSBTAP00000049952; -.
DR SwissPalm; P31836; -.
DR PaxDb; P31836; -.
DR PeptideAtlas; P31836; -.
DR PRIDE; P31836; -.
DR DNASU; 281941; -.
DR GeneID; 281941; -.
DR KEGG; bta:281941; -.
DR CTD; 4684; -.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; P31836; -.
DR OrthoDB; 129648at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 7.
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; IPR033019; Ncam1.
DR InterPro; IPR009138; Neural_cell_adh.
DR PANTHER; PTHR12231:SF239; PTHR12231:SF239; 2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 3.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3512556"
FT CHAIN 20..853
FT /note="Neural cell adhesion molecule 1"
FT /id="PRO_0000015008"
FT TOPO_DOM 20..719
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 738..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..111
FT /note="Ig-like C2-type 1"
FT DOMAIN 116..205
FT /note="Ig-like C2-type 2"
FT DOMAIN 212..300
FT /note="Ig-like C2-type 3"
FT DOMAIN 307..412
FT /note="Ig-like C2-type 4"
FT DOMAIN 415..500
FT /note="Ig-like C2-type 5"
FT DOMAIN 508..607
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 609..704
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 764..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152..156
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT BINDING 161..165
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13595"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13595"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
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 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 139..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 235..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 328..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 435..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 853 AA; 93894 MW; E12FD49231A7A368 CRC64;
MLQTKNLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE
KLTPNQQRIS VVWNDDSSST LTIYNANIDD AGIYKCVVTA EDGTESEATV NVKIFQKLMF
KNAPTPQEFR EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLT NNYLQIRGIK
KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCNAEGF
PEPTVSWTKD GEQIENEEDE KYLFSDDSSE LTIRKVDKND EAEYVCIAEN KAGEQDASIH
LKVFAKPKIT YVENQTAMEL EEQVTLTCEA SGDPIPSITW RTSTRNISSE EKASWTRPEK
QETLDGHMVV RSHARVSSLT LKSIQYTDAG EYVCTASNTI GQDSQSMYLE VQYAPKLQGP
VAVYTWEGNQ VNITCEVFAY PSATISWFRD GQLLPSSNYS NIKIYNTPSA SYLEVTPDSE
NDFGNYNCTA VNRIGQESLE FVLVQADTPS SPSIDQVEPY SSTAQVQFDE PEATGGVPIL
KYKAEWRAMG EEVWHSKWYD AKEASMEGIV TIVGLKPETT YAVRLAALNG KGLGEISAAS
EFKTQPVREP SAPKLEGQMG EDGNSIKVKL IKQDDGGSPI RHYLVKYRAL SSEWKPEIRL
PSGSDHVMLK SLDWNAEYEV YVVAENQQGK SKAAHFVFRT SAQPTAIPAN GSPTSGLSTG
AIVGILVVTF VLLLVAVDVT CYFLNKCGLL MCIAVNLCGK AGPGAKGKDM EEGKAAFSKD
ESKEPIVEVR TEEERTPNHD GGKHTEPNET TPLTEPEKGP VEAKPETETK PAPAEVQTVP
NDATQIKVNE SKA
