ID F1NKK8_CHICK Unreviewed; 559 AA.
AC F1NKK8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 4.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Nectin cell adhesion molecule 3 {ECO:0000313|Ensembl:ENSGALP00010006640.1};
GN Name=NECTIN3 {ECO:0000313|Ensembl:ENSGALP00010006640.1};
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 {ECO:0000313|Ensembl:ENSGALP00010006640.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010006640.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010006640.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the nectin family.
CC {ECO:0000256|ARBA:ARBA00007810}.
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DR AlphaFoldDB; F1NKK8; -.
DR SMR; F1NKK8; -.
DR STRING; 9031.ENSGALP00000024751; -.
DR PaxDb; 9031-ENSGALP00000024751; -.
DR Ensembl; ENSGALT00010011857.1; ENSGALP00010006640.1; ENSGALG00010005035.1.
DR VEuPathDB; HostDB:geneid_100857875; -.
DR VEuPathDB; HostDB:geneid_418415; -.
DR GeneTree; ENSGT00940000156028; -.
DR InParanoid; F1NKK8; -.
DR Reactome; R-GGA-418990; Adherens junctions interactions.
DR Reactome; R-GGA-420597; Nectin/Necl trans heterodimerization.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000015367; Expressed in spermatocyte and 11 other cell types or tissues.
DR ExpressionAtlas; F1NKK8; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:1902414; P:protein localization to cell junction; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; IEA:InterPro.
DR CDD; cd07704; IgC1_2_Nectin-3-4_like; 1.
DR CDD; cd05887; IgV_1_Nectin-3_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR033320; IgC1_2_Nectin-3-4-like.
DR InterPro; IPR033319; Nectin-3_IgV_dom.
DR PANTHER; PTHR23277:SF12; NECTIN-3; 1.
DR PANTHER; PTHR23277; NECTIN-RELATED; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1NKK8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 66..171
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 176..264
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 275..360
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 559 AA; 62363 MW; C69193658C8F5EA9 CRC64;
MAAIGAVSRV SPAPIGRREL FPAAGASPRW WWWQQRRRRA GSALPPGLGL LGLVFSRFCC
SALAGPVVDP HVTAVWGKKV ALKCIIDVNE TITQVSWEKI HGKTSETIAV HHPEYGISIQ
EKYQGKVSFK NYSLTDATII LKNVSFSDAG EYICKAVTFP LGNSQSSITV TVLVEPVVSL
TKGPNPLIDG ANQTIAAICT AATGKPAAEI DWEGGLGEME SSSTLFPNET VTVISQYTII
PTRFARGRRI TCIVRHPALE KEIRFSHVLD IQYAPEVSVT GYDGNWFIGR ENVQLRCNAD
ANPLPMEFMW TRLDGQWPEG LLSVNNTLQF SSPLTYNYTG TYICKVTNSL GQRSDQKTIY
ILDPPTTTTR LPTVPWHPST DGITGLATEP RIIDFPSSTL PAMQEDTWGT VIGSAVGGAL
FLILVSVLVG IICYRRRRTF RGDYFAKNYI PPSDMQKESQ IDVLQSDDVD SYPDSIKKEI
KHPMNSLISK DYLEDPEKPE WNNIDNINRY QERYERPMDY YESGTLGMKY MGGDCYDDNE
EDFVSHIDGS VISRREWYV
//
