NCAM1_CHICK
ID NCAM1_CHICK Reviewed; 1091 AA.
AC P13590; Q90918; Q90919;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Neural cell adhesion molecule 1;
DE Short=N-CAM-1;
DE Short=NCAM-1;
DE Flags: Precursor;
GN Name=NCAM1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-175, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3576199; DOI=10.1126/science.3576199;
RA Cunningham B.A., Hemperly J.J., Murray B.A., Prediger E.A., Brackenbury R.,
RA Edelman G.M.;
RT "Neural cell adhesion molecule: structure, immunoglobulin-like domains,
RT cell surface modulation, and alternative RNA splicing.";
RL Science 236:799-806(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-1091, AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=3458261; DOI=10.1073/pnas.83.9.3037;
RA Hemperly J.J., Murray B.A., Edelman G.M., Cunningham B.A.;
RT "Sequence of a cDNA clone encoding the polysialic acid-rich and cytoplasmic
RT domains of the neural cell adhesion molecule N-CAM.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3037-3041(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM D).
RX PubMed=3467341; DOI=10.1073/pnas.83.24.9822;
RA Hemperly J.J., Edelman G.M., Cunningham B.A.;
RT "cDNA clones of the neural cell adhesion molecule (N-CAM) lacking a
RT membrane-spanning region consistent with evidence for membrane attachment
RT via a phosphatidylinositol intermediate.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9822-9826(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 810-1069.
RX PubMed=3771645; DOI=10.1083/jcb.103.4.1431;
RA Murray B.A., Owens G.C., Prediger E.A., Crossin K.L., Cunningham B.A.,
RA Edelman G.M.;
RT "Cell surface modulation of the neural cell adhesion molecule resulting
RT from alternative mRNA splicing in a tissue-specific developmental
RT sequence.";
RL J. Cell Biol. 103:1431-1439(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=1478668; DOI=10.1016/s0888-7543(05)80108-9;
RA Colwell G., Li B., Forrest D., Brackenbury R.;
RT "Conserved regulatory elements in the promoter region of the N-CAM gene.";
RL Genomics 14:875-882(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=White leghorn; TISSUE=Erythrocyte;
RA Sasner M., Covault J.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-29.
RX PubMed=2430978; DOI=10.1083/jcb.103.5.1739;
RA Cole G.J., Loewy A., Cross N.V., Akeson R., Glaser L.;
RT "Topographic localization of the heparin-binding domain of the neural cell
RT adhesion molecule N-CAM.";
RL J. Cell Biol. 103:1739-1744(1986).
RN [8]
RP CELL-BINDING.
RX PubMed=1380002; DOI=10.1083/jcb.118.4.937;
RA Rao Y., Wu X.F., Gariepy J., Rutishauser U., Siu C.H.;
RT "Identification of a peptide sequence involved in homophilic binding in the
RT neural cell adhesion molecule NCAM.";
RL J. Cell Biol. 118:937-949(1992).
RN [9]
RP STRUCTURE BY NMR OF 202-307.
RX PubMed=11469865; DOI=10.1006/jmbi.2001.4861;
RA Atkins A.R., Chung J., Deechongkit S., Little E.B., Edelman G.M.,
RA Wright P.E., Cunningham B.A., Dyson H.J.;
RT "Solution structure of the third immunoglobulin domain of the neural cell
RT adhesion molecule N-CAM: can solution studies define the mechanism of
RT homophilic binding?";
RL J. Mol. Biol. 311:161-172(2001).
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A; Synonyms=N-CAM 180;
CC IsoId=P13590-1; Sequence=Displayed;
CC Name=B; Synonyms=N-CAM 140;
CC IsoId=P13590-2; Sequence=VSP_002585;
CC Name=C;
CC IsoId=P13590-3; Sequence=VSP_002586;
CC Name=D;
CC IsoId=P13590-4; Sequence=VSP_002583, VSP_002584;
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DR EMBL; M15861; AAB59958.1; -; Genomic_DNA.
DR EMBL; M15860; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15922; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15923; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15924; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M21178; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M21179; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M21180; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15929; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15930; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15931; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15932; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15933; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15934; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; L29437; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15935; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15937; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15938; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15939; AAB59958.1; JOINED; Genomic_DNA.
DR EMBL; M15861; AAB59959.1; -; Genomic_DNA.
DR EMBL; M15860; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15922; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15923; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15924; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M21178; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M21179; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M21180; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15929; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15930; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15931; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15932; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15934; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; L29437; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15935; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15937; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15939; AAB59959.1; JOINED; Genomic_DNA.
DR EMBL; M15936; AAB59957.1; -; Genomic_DNA.
DR EMBL; M15860; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15922; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15923; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15924; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M21178; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M21179; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M21180; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15929; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15930; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15931; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15932; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15934; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; L29437; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; M15935; AAB59957.1; JOINED; Genomic_DNA.
DR EMBL; X04479; CAB51638.1; -; Genomic_DNA.
DR EMBL; X70342; CAA49807.1; -; Genomic_DNA.
DR EMBL; Z12128; CAA78113.1; -; Genomic_DNA.
DR PIR; A43613; IJCHNL.
DR PDB; 1IE5; NMR; -; A=202-307.
DR PDBsum; 1IE5; -.
DR AlphaFoldDB; P13590; -.
DR SMR; P13590; -.
DR IntAct; P13590; 1.
DR STRING; 9031.ENSGALP00000012709; -.
DR PaxDb; P13590; -.
DR VEuPathDB; HostDB:geneid_428253; -.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; P13590; -.
DR OrthoDB; 129648at2759; -.
DR PhylomeDB; P13590; -.
DR EvolutionaryTrace; P13590; -.
DR PRO; PR:P13590; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:SynGO.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
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; 1.
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 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT CHAIN 20..1091
FT /note="Neural cell adhesion molecule 1"
FT /id="PRO_0000015007"
FT TOPO_DOM 20..711
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..1091
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 116..205
FT /note="Ig-like C2-type 2"
FT DOMAIN 212..301
FT /note="Ig-like C2-type 3"
FT DOMAIN 308..403
FT /note="Ig-like C2-type 4"
FT DOMAIN 406..495
FT /note="Ig-like C2-type 5"
FT DOMAIN 499..598
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 600..696
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 756..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1091
FT /note="Basic and acidic 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 CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
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..287
FT /evidence="ECO:0000269|PubMed:11469865,
FT ECO:0007744|PDB:1IE5"
FT DISULFID 329..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 426..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 702..726
FT /note="STSPTSGLGTAAIVGILIVIFVLLL -> TLGSPSTSSSFVSLLLSAVTLLL
FT LC (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_002583"
FT VAR_SEQ 727..1091
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_002584"
FT VAR_SEQ 771..809
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_002585"
FT VAR_SEQ 810..1070
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_002586"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1IE5"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:1IE5"
FT STRAND 295..305
FT /evidence="ECO:0007829|PDB:1IE5"
SQ SEQUENCE 1091 AA; 117415 MW; B151367002DF88E0 CRC64;
MLPAAALPWT LFFLGAAASL QVDIVPSQGE ISVGESKFFL CQVAGEAKYK DISWFSPNGE
KLTPNQQRIS VVRNDDFSST LTIYNANIDD AGIYKCVVSS VEEGDSEATV NVKIFQKLMF
KNAPTPQEFK EGDDAVIVCD VVSSLPPTII WKHKGRDVML KKDVRFIVLS NNYLQIRGIK
KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPSVRARQST MNATANLSQS VTLACDADGF
PEPTMTWTKD GEPIEQEDNE EKYSFNYDGS ELIIKKVDKS DEAEYICIAE NKAGEQDATI
HLKVFAKPKI TYVENKTAME LEDQITLTCE ASGDPIPSIT WKTSTRNISN EEKTLDGRIV
VRSHARVSSL TLKEIQYTDA GEYVCTASNT IGQDSQAMYL EVQYAPKLQG PVAVYTWEGN
QVNITCEVFA YPSAVISWFR DGQLLPSSNY SNIKIYNTPS ASYLEVTPDS ENDFGNYNCT
AVNRIGQESS EFILVQADTP SSPSIDRVEP YSSTARVEFD EPEATGGVPI LKYKAEWRAL
GEGEWHSRLY DAKEANVEGT ITISGLKPET TYSVRLSAVN GKGVGEISLP SDFKTQPVRE
PSAPKLEGQM GEDGNSIKVN VIKQDDGGSP IRHYLIKYKA KHSSEWKPEI RLPSGIDHVM
LKSLDWNAEY EVYVIAENQQ GKSKPAHYAF RTSAQPTVIP ASTSPTSGLG TAAIVGILIV
IFVLLLVAVD VTCYFLNKCG LLMCIAVNLC GKSGPGAKGK DMEEGKAAFS KDESKEPIVE
VRTEEERTPN HDGGKHTEPN ETTPLTEPEH TADTAATVED MLPSVTTGTT NSDTITETFA
TAQNSPTSET TTLTSSIAPP ATAIPDSNAM SPGQATPAKA GASPVSPPPP SSTPKVAPLV
DLSDTPSSAP ATNNLSSSVL SNQGAVLSPS TVANMAETSK AAAGNKSAAP TPANLTSPPA
PSEPKQEVSS TKSPEKEAAQ PSTVKSPTET AKNPSNPKSE AASGGTTNPS QNEDFKMDEG
TFKTPDIDLA KDVFAALGTT TPASVASGQA RELASSTADS SVPAAPAKTE KTPVEDKSEV
QATEIRHLQQ K
