NRCAM_CHICK
ID NRCAM_CHICK Reviewed; 1284 AA.
AC P35331;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Neuronal cell adhesion molecule;
DE Short=Nr-CAM;
DE AltName: Full=Neuronal surface protein Bravo;
DE Short=gBravo;
DE AltName: Full=NgCAM-related cell adhesion molecule;
DE Short=Ng-CAM-related;
DE Flags: Precursor;
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 [MRNA], AND PROTEIN SEQUENCE OF 25-52; 178-184 AND
RP 581-594.
RC STRAIN=White leghorn; TISSUE=Embryonic brain;
RX PubMed=2045418; DOI=10.1083/jcb.113.6.1399;
RA Grumet M., Mauro V., Burgoon M.P., Edelman G.M., Cunningham B.A.;
RT "Structure of a new nervous system glycoprotein, Nr-CAM, and its
RT relationship to subgroups of neural cell adhesion molecules.";
RL J. Cell Biol. 113:1399-1412(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-1284, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Embryonic brain, and Retina;
RX PubMed=1512296; DOI=10.1083/jcb.118.5.1259;
RA Kayyem J.F., Roman J.M., de la Rosa E.J., Schwarz U., Dreyer W.J.;
RT "Bravo/Nr-CAM is closely related to the cell adhesion molecules L1 and Ng-
RT CAM and has a similar heterodimer structure.";
RL J. Cell Biol. 118:1259-1270(1992).
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC Specifically involved in the development of optic fibres in the retina.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P35331-1; Sequence=Displayed;
CC Name=2; Synonyms=AS10;
CC IsoId=P35331-2; Sequence=VSP_002603;
CC Name=3; Synonyms=AS12;
CC IsoId=P35331-3; Sequence=VSP_002604;
CC Name=4; Synonyms=AS93;
CC IsoId=P35331-4; Sequence=VSP_002605;
CC Name=5; Synonyms=AS-CYT2;
CC IsoId=P35331-5; Sequence=VSP_002606;
CC -!- TISSUE SPECIFICITY: Retina and developing brain.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing neural retina and
CC embryonic brain tissue.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
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DR EMBL; X58482; CAA41391.1; -; mRNA.
DR EMBL; L08960; AAA48632.1; -; mRNA.
DR PIR; A39640; A39640.
DR PIR; A43425; A43425.
DR RefSeq; NP_990597.1; NM_205266.1.
DR AlphaFoldDB; P35331; -.
DR SMR; P35331; -.
DR BioGRID; 676462; 1.
DR IntAct; P35331; 1.
DR STRING; 9031.ENSGALP00000015476; -.
DR PaxDb; P35331; -.
DR GeneID; 396202; -.
DR KEGG; gga:396202; -.
DR CTD; 4897; -.
DR VEuPathDB; HostDB:geneid_396202; -.
DR eggNOG; KOG3513; Eukaryota.
DR PhylomeDB; P35331; -.
DR PRO; PR:P35331; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IDA:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030506; F:ankyrin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:AgBase.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:AgBase.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0030247; F:polysaccharide binding; IDA:AgBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:AgBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:AgBase.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:AgBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:AgBase.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IDA:AgBase.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 11.
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; IPR026966; Neurofascin/L1/NrCAM_C.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 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..24
FT /evidence="ECO:0000269|PubMed:2045418"
FT CHAIN 25..1284
FT /note="Neuronal cell adhesion molecule"
FT /id="PRO_0000015060"
FT TOPO_DOM 25..1143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1144..1166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1167..1284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..129
FT /note="Ig-like C2-type 1"
FT DOMAIN 136..230
FT /note="Ig-like C2-type 2"
FT DOMAIN 243..332
FT /note="Ig-like C2-type 3"
FT DOMAIN 337..424
FT /note="Ig-like C2-type 4"
FT DOMAIN 430..517
FT /note="Ig-like C2-type 5"
FT DOMAIN 521..608
FT /note="Ig-like C2-type 6"
FT DOMAIN 625..720
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 725..819
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 824..926
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 930..1026
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1040..1132
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 707..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 995
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1059
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1091
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 268..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 358..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 452..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 543..592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 612..621
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002603"
FT VAR_SEQ 1027..1038
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002604"
FT VAR_SEQ 1039..1131
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_002605"
FT VAR_SEQ 1202..1205
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_002606"
FT CONFLICT 209
FT /note="V -> E (in Ref. 2; AAA48632)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="H -> Q (in Ref. 2; AAA48632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1284 AA; 141852 MW; A3570BF9C3D47A0F CRC64;
MMKEKSISAS KASLVFFLCQ MISALDVPLD SKLLEELSQP PTITQQSPKD YIVDPRENIV
IQCEAKGKPP PSFSWTRNGT HFDIDKDAQV TMKPNSGTLV VNIMNGVKAE AYEGVYQCTA
RNERGAAISN NIVIRPSRSP LWTKEKLEPN HVREGDSLVL NCRPPVGLPP PIIFWMDNAF
QRLPQSERVS QGLNGDLYFS NVQPEDTRVD YICYARFNHT QTIQQKQPIS VKVFSTKPVT
ERPPVLLTPM GSTSNKVELR GNVLLLECIA AGLPTPVIRW IKEGGELPAN RTFFENFKKT
LKIIDVSEAD SGNYKCTARN TLGSTHHVIS VTVKAAPYWI TAPRNLVLSP GEDGTLICRA
NGNPKPSISW LTNGVPIAIA PEDPSRKVDG DTIIFSAVQE RSSAVYQCNA SNEYGYLLAN
AFVNVLAEPP RILTPANKLY QVIADSPALI DCAYFGSPKP EIEWFRGVKG SILRGNEYVF
HDNGTLEIPV AQKDSTGTYT CVARNKLGKT QNEVQLEVKD PTMIIKQPQY KVIQRSAQAS
FECVIKHDPT LIPTVIWLKD NNELPDDERF LVGKDNLTIM NVTDKDDGTY TCIVNTTLDS
VSASAVLTVV AAPPTPAIIY ARPNPPLDLE LTGQLERSIE LSWVPGEENN SPITNFVIEY
EDGLHEPGVW HYQTEVPGSH TTVQLKLSPY VNYSFRVIAV NEIGRSQPSE PSEQYLTKSA
NPDENPSNVQ GIGSEPDNLV ITWESLKGFQ SNGPGLQYKV SWRQKDVDDE WTSVVVANVS
KYIVSGTPTF VPYEIKVQAL NDLGYAPEPS EVIGHSGEDL PMVAPGNVQV HVINSTLAKV
HWDPVPLKSV RGHLQGYKVY YWKVQSLSRR SKRHVEKKIL TFRGNKTFGM LPGLEPYSSY
KLNVRVVNGK GEGPASPDKV FKTPEGVPSP PSFLKITNPT LDSLTLEWGS PTHPNGVLTS
YILKFQPINN THELGPLVEI RIPANESSLI LKNLNYSTRY KFYFNAQTSV GSGSQITEEA
VTIMDEAGIL RPAVGAGKVQ PLYPRIRNVT TAAAETYANI SWEYEGPDHA NFYVEYGVAG
SKEDWKKEIV NGSRSFFVLK GLTPGTAYKV RVGAEGLSGF RSSEDLFETG PAMASRQVDI
ATQGWFIGLM CAVALLILIL LIVCFIRRNK GGKYPVKEKE DAHADPEIQP MKEDDGTFGE
YRSLESDAED HKPLKKGSRT PSDRTVKKED SDDSLVDYGE GVNGQFNEDG SFIGQYSGKK
EKEPAEGNES SEAPSPVNAM NSFV
