NECT1_PIG
ID NECT1_PIG Reviewed; 515 AA.
AC Q9GL76;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Nectin-1;
DE AltName: Full=Herpes virus entry mediator C;
DE Short=Herpesvirus entry mediator C;
DE Short=HveC;
DE AltName: Full=Nectin cell adhesion molecule 1 {ECO:0000250|UniProtKB:Q15223};
DE AltName: Full=Poliovirus receptor-related protein 1;
DE AltName: CD_antigen=CD111;
DE Flags: Precursor;
GN Name=NECTIN1 {ECO:0000250|UniProtKB:Q15223}; Synonyms=HVEC, PRR1, PVRL1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11277703; DOI=10.1006/viro.2000.0798;
RA Milne R.S.B., Connolly S.A., Krummenacher C., Eisenberg R.J., Cohen G.H.;
RT "Porcine HveC, a member of the highly conserved HveC/nectin 1 family, is a
RT functional alphaherpesvirus receptor.";
RL Virology 281:315-328(2001).
CC -!- FUNCTION: Probably involved in cell adhesion. Receptor for
CC alphaherpesvirus (HSV-1, HSV-2 and pseudorabies virus) entry into
CC cells.
CC -!- SUBUNIT: Interacts with HSV glycoprotein D (gD). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9GL76; Q69091: gD; Xeno; NbExp=4; IntAct=EBI-11691211, EBI-11691180;
CC Q9GL76; G3G922: US6; Xeno; NbExp=4; IntAct=EBI-11691211, EBI-11691167;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR EMBL; AF308632; AAG30281.1; -; mRNA.
DR RefSeq; NP_001001262.1; NM_001001262.1.
DR RefSeq; XP_003130000.5; XM_003129952.5.
DR PDB; 5X5W; X-ray; 2.70 A; B/D=37-143.
DR PDBsum; 5X5W; -.
DR AlphaFoldDB; Q9GL76; -.
DR SMR; Q9GL76; -.
DR IntAct; Q9GL76; 2.
DR STRING; 9823.ENSSSCP00000016047; -.
DR PaxDb; Q9GL76; -.
DR PeptideAtlas; Q9GL76; -.
DR PRIDE; Q9GL76; -.
DR GeneID; 397247; -.
DR KEGG; ssc:397247; -.
DR CTD; 5818; -.
DR eggNOG; ENOG502QVRJ; Eukaryota.
DR InParanoid; Q9GL76; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
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:0046598; P:positive regulation of viral entry into host cell; IMP:AgBase.
DR GO; GO:1902414; P:protein localization to cell junction; IBA:GO_Central.
DR GO; GO:0051963; P:regulation of synapse assembly; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:InterPro.
DR CDD; cd05886; Ig1_Nectin-1_like; 1.
DR CDD; cd05890; Ig2_Nectin-1_like; 1.
DR Gene3D; 2.60.40.10; -; 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; IPR041849; Nectin-1_Ig1.
DR InterPro; IPR041850; Nectin-1_Ig2.
DR InterPro; IPR033314; Nectin1.
DR PANTHER; PTHR23277:SF69; PTHR23277:SF69; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..515
FT /note="Nectin-1"
FT /id="PRO_0000015135"
FT TOPO_DOM 31..355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..141
FT /note="Ig-like V-type"
FT DOMAIN 145..243
FT /note="Ig-like C2-type 1"
FT DOMAIN 247..334
FT /note="Ig-like C2-type 2"
FT REGION 400..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15223"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15223"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKF6"
FT MOD_RES 436
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKF6"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKF6"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 172..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 269..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:5X5W"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:5X5W"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:5X5W"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:5X5W"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5X5W"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:5X5W"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:5X5W"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5X5W"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:5X5W"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5X5W"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5X5W"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:5X5W"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:5X5W"
SQ SEQUENCE 515 AA; 57047 MW; BFAB00320DDE3785 CRC64;
MARMGLAGAA GRWWGLALGL TAFFLPGAHT QVVQVNDSMY GFIGTDVVLH CSFANPLPGV
KITQVTWQKA TNGSKQNVAI YNPAMGVSVL APYRERVEFL RPSFTDGTIR LSRLELEDEG
VYICEFATFP AGNRESQLNL TVMAKPTNWI EGTQAVLRAK KGKDDKVLVA TCTSANGKPP
SVVSWETHLK GEAEYQEIRN PNGTVTVISR YRLVPSREDH RQSLACIVNY HMDRFRESLT
LNVQYEPEVT IEGFDGNWYL QRMDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
FFRGPINYSM AGTYICEATN PIGTRSGQVE VNITEFPYTP SPPEHGRRAG QVPTAIIGGV
VGSILLVLFV VGGIVVALCR RRHTFKGDYS TKKHVYGNGY SKAGIPQHHP PMAQNLQYPE
DSDDEKKAGP LGGSSYEEEE EEEGGGGERK VGGPHPKYDE DAKRPYFTVD EAEARQDGYG
DRTLGYQYDP EQLDLAENMV SQNDGSFISK KEWYV
