ID A0A287A236_PIG Unreviewed; 1376 AA.
AC A0A287A236;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Neurofascin {ECO:0000313|Ensembl:ENSSSCP00000037997.1};
GN Name=NFASC {ECO:0000313|Ensembl:ENSSSCP00000037997.1,
GN ECO:0000313|VGNC:VGNC:90707};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000037997.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000037997.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000037997.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000037997.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000256|ARBA:ARBA00008588}.
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DR Ensembl; ENSSSCT00000061692.3; ENSSSCP00000037997.1; ENSSSCG00000022951.4.
DR VGNC; VGNC:90707; NFASC.
DR GeneTree; ENSGT00940000157024; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000022951; Expressed in prefrontal cortex and 17 other cell types or tissues.
DR ExpressionAtlas; A0A287A236; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR CDD; cd05731; Ig3_L1-CAM_like; 1.
DR CDD; cd05845; IgI_2_L1-CAM_like; 1.
DR CDD; cd05875; IgI_hNeurofascin_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
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_Ig-like.
DR PANTHER; PTHR44170:SF12; NEUROFASCIN; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287A236};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1246..1267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..357
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 363..444
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 464..552
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 557..644
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 649..737
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 741..823
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 850..945
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 947..1043
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1047..1143
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1145..1235
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 65..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1376 AA; 152783 MW; 0C2457FCEB9AC724 CRC64;
MVEGHIQNKL VIPLGLQSTS SRVFPWGAVG DQRTETENYH FLQRSPWVGE KVKTVLVLQI
APQRAPAGPR GSSLPCSSSV PVPARRAKGG ARGRARRVSG TRRLLGDAHG LVSALMRRLA
ARGAAGDAGE VAPPAADSTD CAPGRSPSPC RLIDLCAIWD AGVFLPAAVA AAWKGAPSGV
PRRRLNEAET LSSVQKAQLQ RLEAARPRGP GSGDRGPVPR MARQQPPPWV HAAILFSLLS
LSTAIEIPMD PSIQNELSQP PTITKQSVKD HIVDPRDNIL IECEAKGNPA PSFHWTRNSR
FFNIAKDPRV SMRRRSGTLV IDFRSGGRPE EYEGEYQCFA RNKFGTALSN RIRLQVSKSP
LWPKENLDPV VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM EPITQDKRVS QGHNGDLYFS
NVMLQDMQTD YSCNARFHFT HTIQQKNPFN LKVLTTRGVA ERTPSFMYPQ GTASSQMVLR
GMDLLLECIA SGVPTPDIAW YKKGGDLPSD KAKLENFNKA LRITNVSEED SGEYFCLASN
KMGSIRHTIS VRVKAAPYWL DEPKNLILAP GEDGRLVCRA NGNPKPTVQW MVNGEPLQSA
PPNPNREVAG DTIIFRDTQI SSRAVYQCNT SNEHGYLLAN AFVSVLDVPP RMLSPRNQLI
RVILYNRTRL DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV YENGSLEIKM IRKEDQGIYT
CVATNILGKA ENQVRLEVKD PTRIYRMPED QVAQRGTTVQ LECRVKHDPS LKLTVSWLKD
DEPLYIGNRM KKEEDSLTIF GVAERDQGSY TCVASTELDQ DLAKAYLTVL ADQATPTNRL
AALPKGRPDR PRDLELTDLA ERSVRLTWIP GDDNNSPITD YVVQFEEDQF QPGVWHDHSK
FPGSVNSAVL QLSPYVNYQF RVIAINEVGS SHPSLPSERY RTSGAPPESN PSDVKGEGTR
KNNMEITWTP MNATSAFGPN LRYIVKWRRR ETRETWNNVT VWGSRYVVGQ TPVYVPYEIR
VQAENDFGKG PEPDTVIGYS GEDLPSAPRR FRVRQPNLET INLEWDHPEH PNGILIGYTL
KYVAFNGTKV GKQIVENFSP NQTKFTVQRA DPVSRYRFSL SARTQVGSGE AVTEESPAPP
NEAPDEQSIW NVTVLPNSKW ANITWKHNFG PGTDFVVEYI DSNHTKKTVP VKAQAQPIQL
TDLYPGMTYT LRVYSRDNEG ISSTVITFMT STAYTNNQAD IATQGWFIGL MCAIALLVLI
LLIVCFIKRS RGGKYPVREK KDVPLGPEDP KEEDGSFDYS DEDNKPLQGS QTSLDGTIKQ
QESDDSLVDY GEGGEGQFNE DGSFIGQYTV KKDKEETEGN ESSEATSPVN AIYSLA
//
