NFASC_CHICK
ID NFASC_CHICK Reviewed; 1369 AA.
AC O42414; Q90924;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Neurofascin;
DE Flags: Precursor;
GN Name=NFASC;
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] (ISOFORM 2), PROTEIN SEQUENCE OF 26-46; 637-641;
RP 717-730; 758-781 AND 801-815, PROTEOLYTIC CLEAVAGE AT ARG-636, AND
RP GLYCOSYLATION.
RC TISSUE=Brain;
RX PubMed=1377696; DOI=10.1083/jcb.118.1.149;
RA Volkmer H., Hassel B., Wolff J.M., Frank R., Rathjen F.G.;
RT "Structure of the axonal surface recognition molecule neurofascin and its
RT relationship to a neural subgroup of the immunoglobulin superfamily.";
RL J. Cell Biol. 118:149-161(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9353344; DOI=10.1074/jbc.272.45.28742;
RA Hassel B., Rathjen F.G., Volkmer H.;
RT "Organization of the neurofascin gene and analysis of developmentally
RT regulated alternative splicing.";
RL J. Biol. Chem. 272:28742-28749(1997).
CC -!- FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved
CC in neurite extension, axonal guidance, synaptogenesis, myelination and
CC neuron-glial cell interactions. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=O42414-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O42414-2; Sequence=VSP_008935, VSP_008936;
CC -!- DEVELOPMENTAL STAGE: There is one major 'early' isoform and multiple
CC 'late' isoforms. Around 50 isoforms are found at different
CC developmental stages.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000269|PubMed:1377696}.
CC -!- PTM: May be proteolytically cleaved at Arg-636.
CC {ECO:0000269|PubMed:1377696}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
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DR EMBL; X65224; CAA46330.1; -; mRNA.
DR EMBL; Y14341; CAA74726.1; -; Genomic_DNA.
DR EMBL; Y14342; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14343; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14344; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14345; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14346; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14347; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14348; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14349; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14350; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14351; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14352; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14353; CAA74726.1; JOINED; Genomic_DNA.
DR EMBL; Y14354; CAA74726.1; JOINED; Genomic_DNA.
DR PIR; S26180; S26180.
DR RefSeq; NP_001004493.1; NM_001004493.4. [O42414-2]
DR AlphaFoldDB; O42414; -.
DR SMR; O42414; -.
DR BioGRID; 680872; 3.
DR IntAct; O42414; 1.
DR STRING; 9031.ENSGALP00000034591; -.
DR PaxDb; O42414; -.
DR PRIDE; O42414; -.
DR GeneID; 419824; -.
DR KEGG; gga:419824; -.
DR CTD; 23114; -.
DR VEuPathDB; HostDB:geneid_419824; -.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; O42414; -.
DR OrthoDB; 434404at2759; -.
DR PhylomeDB; O42414; -.
DR PRO; PR:O42414; -.
DR Proteomes; UP000000539; 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; ISS:UniProtKB.
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 GO; GO:0042552; P:myelination; IEA:InterPro.
DR GO; GO:0007422; P:peripheral nervous system development; IEA:InterPro.
DR GO; GO:0050808; P:synapse organization; IEA:InterPro.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:InterPro.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 11.
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 InterPro; IPR026965; NFASC.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF35; PTHR10075:SF35; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
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..25
FT /evidence="ECO:0000269|PubMed:1377696"
FT CHAIN 26..1369
FT /note="Neurofascin"
FT /id="PRO_0000015048"
FT TOPO_DOM 26..1235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1236..1256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1257..1369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..138
FT /note="Ig-like C2-type 1"
FT DOMAIN 144..231
FT /note="Ig-like C2-type 2"
FT DOMAIN 262..350
FT /note="Ig-like C2-type 3"
FT DOMAIN 355..442
FT /note="Ig-like C2-type 4"
FT DOMAIN 448..535
FT /note="Ig-like C2-type 5"
FT DOMAIN 539..626
FT /note="Ig-like C2-type 6"
FT DOMAIN 645..740
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 745..838
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 843..945
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 949..1057
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1133..1222
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 730..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 636..637
FT /note="Cleavage"
FT /evidence="ECO:0000305|PubMed:1377696"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
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 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 163..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 286..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 376..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 470..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 561..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 987..993
FT /note="SCLSSPV -> F (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1377696"
FT /id="VSP_008935"
FT VAR_SEQ 1132..1222
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1377696"
FT /id="VSP_008936"
FT CONFLICT 1105
FT /note="T -> A (in Ref. 2; CAA46330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1369 AA; 152955 MW; 835F27D086B2BFF6 CRC64;
MVLHSHQLTY AGIAFALCLH HLISAIEVPL DSNIQSELPQ PPTITKQSVK DYIVDPRDNI
FIECEAKGNP VPTFSWTRNG KFFNVAKDPK VSMRRRSGTL VIDFHGGGRP DDYEGEYQCF
ARNDYGTALS SKIHLQVSRS PLWPKEKVDV IEVDEGAPLS LQCNPPPGLP PPVIFWMSSS
MEPIHQDKRV SQGQNGDLYF SNVMLQDAQT DYSCNARFHF THTIQQKNPY TLKVKTKKPH
NETSLRNHTD MYSARGVTET TPSFMYPYGT SSSQMVLRGV DLLLECIASG VPAPDIMWYK
KGGELPAGKT KLENFNKALR ISNVSEEDSG EYFCLASNKM GSIRHTISVR VKAAPYWLDE
PQNLILAPGE DGRLVCRANG NPKPSIQWLV NGEPIEGSPP NPSREVAGDT IVFRDTQIGS
SAVYQCNASN EHGYLLANAF VSVLDVPPRI LAPRNQLIKV IQYNRTRLDC PFFGSPIPTL
RWFKNGQGNM LDGGNYKAHE NGSLEMSMAR KEDQGIYTCV ATNILGKVEA QVRLEVKDPT
RIVRGPEDQV VKRGSMPRLH CRVKHDPTLK LTVTWLKDDA PLYIGNRMKK EDDGLTIYGV
AEKDQGDYTC VASTELDKDS AKAYLTVLAI PANRLRDLPK ERPDRPRDLE LSDLAERSVK
LTWIPGDDNN SPITDYIVQF EEDRFQPGTW HNHSRYPGNV NSALLSLSPY VNYQFRVIAV
NDVGSSLPSM PSERYQTSGA RPEINPTGVQ GAGTQKNNME ITWTPLNATQ AYGPNLRYIV
RWRRRDPRGS WYNETVKAPR HVVWNTPIYV PYEIKVQAEN DFGRAPEPET YIGYSGEDYP
KAAPTDVRIR VLNSTAIALT WTRVHLDTIQ GQLKEYRAYF WRDSSLLKNL WVSKKRQYVS
FPGDRNRGIV SRLFPYSNYK LEMVVTNGRG DGPRSEVKEF PTPEGVPSSP RYLRIRQPNL
ESINLEWDHP EHPNGVLTGY NLRYQASCLS SPVNGSKTGR TLVENFSPNQ TRFTVQRTDP
ISRYRFFLRA RTQVGDGEVI VEESPALLNE ATPTPASTWL PPPTTELTPA ATIATTTTTA
TPTTETPPTE IPTTAIPTTT TTTTTTAAST VASTTTTAER AAAATTKQEL ATNGSSIWDI
RAWANSNWAN ITWSHNYSAG TDFVVKYITS NKTEKSIPVK AQTPSSVQLA NLTPGMVYKL
WVFPIWSSPS EHSYITFTTS SAYTKNHVDI ATQGWFIGLM CAIALLVLIL LIVCFIKRSR
GGKYPVRDNK DEHLNPEDKN VEDGSFDYRS LESDEDNKPL PNSQTSLDGT IKQQESDDSL
VDYGEGGEGQ FNEDGSFIGQ YTVKKDKEET EGNESSEATS PVNAIYSLA
