NGCA_CHICK
ID NGCA_CHICK Reviewed; 1266 AA.
AC Q03696;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Neuronal-glial cell adhesion molecule;
DE Short=Ng-CAM;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1705558; DOI=10.1083/jcb.112.5.1017;
RA Burgoon M.P., Grumet M., Mauro V., Edelman G.M., Cunningham B.A.;
RT "Structure of the chicken neuron-glia cell adhesion molecule, Ng-CAM:
RT origin of the polypeptides and relation to the Ig superfamily.";
RL J. Cell Biol. 112:1017-1029(1991).
RN [2]
RP SEQUENCE REVISION.
RA Burgoon M.P.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the adhesion of neurons to neurons and neurons to
CC glia. It is involved in neuronal migration, neurite fasciculation and
CC outgrowth.
CC -!- SUBUNIT: Binds to itself and to axonin 1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
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DR EMBL; X56969; CAA40290.1; -; mRNA.
DR PIR; A37967; A37967.
DR RefSeq; NP_990484.1; NM_205153.1.
DR AlphaFoldDB; Q03696; -.
DR SMR; Q03696; -.
DR IntAct; Q03696; 1.
DR PRIDE; Q03696; -.
DR GeneID; 396059; -.
DR CTD; 3897; -.
DR VEuPathDB; HostDB:geneid_396202; -.
DR OrthoDB; 434404at2759; -.
DR PhylomeDB; Q03696; -.
DR PRO; PR:Q03696; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; IDA:AgBase.
DR GO; GO:0044295; C:axonal growth cone; IDA:AgBase.
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; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
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; IPR013151; Immunoglobulin.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
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 Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT CHAIN 21..1266
FT /note="Neuronal-glial cell adhesion molecule"
FT /id="PRO_0000015056"
FT TOPO_DOM 21..1130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1131..1153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1154..1266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..128
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..221
FT /note="Ig-like C2-type 2"
FT DOMAIN 236..322
FT /note="Ig-like C2-type 3"
FT DOMAIN 327..413
FT /note="Ig-like C2-type 4"
FT DOMAIN 418..506
FT /note="Ig-like C2-type 5"
FT DOMAIN 510..597
FT /note="Ig-like C2-type 6"
FT DOMAIN 603..698
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 700..804
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 809..930
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 934..1021
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1022..1118
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 685..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 914..916
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 862..882
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1061
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 154..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 260..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 348..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 441..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 532..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1266 AA; 136571 MW; 32E17912014D5DF1 CRC64;
MALPMVGLLL LLLLGGPGAA ITIPPEYGAH DFLQPPELTE EPPEQLVVFP SDDIVLKCVA
TGNPPVQYRW SREDQPFVPE EHGGVSVVPG SGTLVINATL AARLQGRFRC FATNALGTAV
SPEANVIAEN TPQWPKEKVT PVEVEEGDPV VLPCDPPESA VPPKIYWLNS DIVHIAQDER
VSMGQDGNLY FSNAMVGDSH PDYICHAHFL GPRTIIQKEP LDLRVAPSNA VRSRRPRLLL
PRDPQTTTIA LRGGSVVLEC IAEGLPTPWV RWRRLNGPLL PGGVGNFNKT LRLWGVTESD
DGEYECVAEN GRGTARGTHS VTVEAAPYWV RRPQSGVFGP GETARLDCEV GGKPRPQIQW
SINGVPIEAA GAERRWLRGG ALVLPELRPN DSAVLQCEAR NRHGPLLANA FLHVVELPLR
MLTADEQRYE VVENQTVFLH CRTFGAPAPN VEWLTPTLEP ALQDDRSFVF TNGSLRVSAV
RGGDGGVYTC MAQNAHSNGS LTALLEVRAP TRISAPPRSA TAKKGETVTF HCGATFDPAV
TPGELRWLRG GQPLPDDPRY SVAAEMTVSN VDYGDEGTIQ CRASTPLDSA EAEAQLRVVG
RPPSRDLQVM EVDEHRVRLS WTPGDDHNSP IEKFVVEEEE EREDLQRGFG AADVPGQPWT
PPLPLSPYGR FPFRVVAVNA YGRGEHHAPS APIETPPAAP ERNPGGVHGE GNETGNLVIT
WEPLPPQAWN APWARYRVQW RPLEEPGGGG PSGGFPWAES TVDAPPVVVG GLPPFSPFQI
RVQAVNGAGK GPEATPGVGH SGEDLPLVYP ENVGVELLNS STVRVRWTLG GGPKELRGRL
RGFRVLYWRL GWVGERSRRQ APPDPPQIPQ SPAEDPPPFP PVALTVGGDA RGALLGGLRP
WSRYQLRVLV FNGRGDGPPS EPIAFETPEG VPGPPEELRV ERLDDTALSV VERRTFKRSI
TGYVLRYQQV EPGSALPGGS VLRDPQCDLR GLNARSRYRL ALPSTPRERP ALQTVGSTKP
EPPSPLWSRF GVGGRGGFHG AAVEFGAAQE DDVEFEVQFM NKSTDEPWRT SGRANSSLRR
YRLEGLRPGT AYRVQFVGRN RSGENVAFWE SEVQTNGTVV PQPGGGVCTK GWFIGFVSSV
VLLLLILLIL CFIKRSKGGK YSVKDKEDTQ VDSEARPMKD ETFGEYRSLE SEAEKGSASG
SGAGSGVGSP GRGPCAAGSE DSLAGYGGSG DVQFNEDGSF IGQYRGPGAG PGSSGPASPC
AGPPLD
