VK02_SWPVK
ID VK02_SWPVK Reviewed; 370 AA.
AC Q08520;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 23-FEB-2022, entry version 78.
DE RecName: Full=G-protein coupled receptor homolog K2;
GN ORFNames=K2R;
OS Swinepox virus (strain Kasza) (SWPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Suipoxvirus.
OX NCBI_TaxID=10277;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8249275; DOI=10.1006/viro.1993.1625;
RA Massung R.F., Jayarama V., Moyer R.W.;
RT "DNA sequence analysis of conserved and unique regions of swinepox virus:
RT identification of genetic elements supporting phenotypic observations
RT including a novel G protein-coupled receptor homologue.";
RL Virology 197:511-528(1993).
CC -!- FUNCTION: Putative chemokine receptor.
CC -!- SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L21931; AAC37873.1; -; Unassigned_DNA.
DR SMR; Q08520; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004950; F:chemokine receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW G-protein coupled receptor; Glycoprotein; Host cell membrane;
KW Host membrane; Membrane; Receptor; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="G-protein coupled receptor homolog K2"
FT /id="PRO_0000070254"
FT TOPO_DOM 1..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 370 AA; 43171 MW; 76D08613327B0CC0 CRC64;
MTSPTNSTML TYTTNNYYDD DYYEYSTITD YYNTINNDIT SSSVIKAFDN NCTFLEDTKY
HIIVIHIILF LLGSIGNIFV VSLIAFKRNK SITDIYILNL SMSDCIFVFQ IPFIVYSKLD
QWIFGNILCK IMSVLYYVGF FSNMFIITLM SIDRYFAIVH PIKRQPYRTK RIGILMCCSA
WLLSLILSSP VSKLYENIPH MSKDIYQCTL TNENDSIIAF IKRLMQIEIT ILGFLIPIII
FVYCYYRIFT TVVRLRNRRK YKSIKIVLMI VVCSLICWIP LYIVLMIATI VSLYTSNIFR
HLCLYLNLAY AITFSETISL ARCCINPIIY TLIGEHVRSR ISSICSCIYR DNRIRKKLFS
RKSSSSSNII