ID   NECT4_BOVIN             Reviewed;         510 AA.
AC   Q5E9Z9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Nectin-4;
DE   AltName: Full=Nectin cell adhesion molecule 4 {ECO:0000250|UniProtKB:Q96NY8};
DE   AltName: Full=Poliovirus receptor-related protein 4;
DE   Flags: Precursor;
GN   Name=NECTIN4 {ECO:0000250|UniProtKB:Q96NY8}; Synonyms=PVRL4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Seems to be involved in cell adhesion through trans-
CC       homophilic and -heterophilic interactions, the latter including
CC       specifically interactions with NECTIN1. {ECO:0000250}.
CC   -!- SUBUNIT: Self-associates. Interacts via its Ig-like V-type domain with
CC       NECTIN1 Ig-like V-type domain. Interacts via its C-terminus with AFDN
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Cell junction, adherens junction
CC       {ECO:0000250|UniProtKB:Q96NY8}.
CC   -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR   EMBL; BT020770; AAX08787.1; -; mRNA.
DR   RefSeq; NP_001019665.1; NM_001024494.1.
DR   AlphaFoldDB; Q5E9Z9; -.
DR   SMR; Q5E9Z9; -.
DR   STRING; 9913.ENSBTAP00000023767; -.
DR   PaxDb; Q5E9Z9; -.
DR   GeneID; 507718; -.
DR   KEGG; bta:507718; -.
DR   CTD; 81607; -.
DR   eggNOG; ENOG502R9I0; Eukaryota.
DR   InParanoid; Q5E9Z9; -.
DR   OrthoDB; 509401at2759; -.
DR   Proteomes; UP000009136; 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: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:0046718; P:viral entry into host cell; IEA:InterPro.
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; IPR033320; Nectin-4.
DR   PANTHER; PTHR23277:SF11; PTHR23277:SF11; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..510
FT                   /note="Nectin-4"
FT                   /id="PRO_0000297672"
FT   TOPO_DOM        32..349
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        371..510
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..144
FT                   /note="Ig-like V-type"
FT   DOMAIN          148..237
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          248..331
FT                   /note="Ig-like C2-type 2"
FT   REGION          400..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..426
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        171..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        270..315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   510 AA;  55416 MW;  754CE6A2F1CCCCC5 CRC64;
     MPLSLGAEMW GPAAWLLLLL LLASFTGQRL AGELETSDLV TVVLGQDAKL PCFYRGDPGE
     QVEHVAWARV DAGEGGRELA LLNSKYGLHV SSAYEGRVEQ PPPPRNPLDG AVLLRNAVHA
     DEGEYECRVS TFPAGSFQAR LRLRVLVPPL PSLNPGPPLE EGQGLTLAAS CTAEGSPAPS
     VTWDTEVKGT ASHRSFTHSR SAAVTSEFHL VPSRSMNGQP LTCVVSHPGL LQDQRITHIL
     QVAFLAEASV RGLEDRKLWQ VGREGAMLKC LSEGQPPPSY NWTRLDGPLP SGVRAEGDTL
     GFPTLTPEHS GTYVCRVSNA LSSRDSQVVV DVLDPEDAPG KQVDLVSASV VVVGVIAALL
     FCLLVVVVVL MSRYHRRKAQ QMTQKYEEEL TLTRENSIRR LHSHHSDPRN QPEESVGLRA
     EGHPDSLKDN SSCSVMSEEP EGRSYSTLTT VREIETQTEL PSPGPGRAEE EEDRDEGIKQ
     AMNHFVQENG TLRAKPTGNG IYINGRGHLV