ID   CCR7_BOVIN              Reviewed;         379 AA.
AC   Q5MD62;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=C-C chemokine receptor type 7;
DE            Short=C-C CKR-7;
DE            Short=CC-CKR-7;
DE            Short=CCR-7;
DE   AltName: CD_antigen=CD197;
DE   Flags: Precursor;
GN   Name=CCR7;
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 [MRNA].
RX   PubMed=16762412; DOI=10.1016/j.dci.2006.03.008;
RA   Blumerman S.L., Wang F., Herzig C.T., Baldwin C.L.;
RT   "Molecular cloning of bovine chemokine receptors and expression by WC1+
RT   gammadelta T cells.";
RL   Dev. Comp. Immunol. 31:87-102(2007).
CC   -!- FUNCTION: Receptor for the MIP-3-beta chemokine. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: 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; AY834253; AAV97930.1; -; mRNA.
DR   AlphaFoldDB; Q5MD62; -.
DR   SMR; Q5MD62; -.
DR   STRING; 9913.ENSBTAP00000052953; -.
DR   PaxDb; Q5MD62; -.
DR   PRIDE; Q5MD62; -.
DR   eggNOG; ENOG502QUZ9; Eukaryota.
DR   InParanoid; Q5MD62; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR   GO; GO:0038117; F:C-C motif chemokine 19 receptor activity; IBA:GO_Central.
DR   GO; GO:0035757; F:chemokine (C-C motif) ligand 19 binding; IBA:GO_Central.
DR   GO; GO:0035758; F:chemokine (C-C motif) ligand 21 binding; IBA:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   InterPro; IPR001718; Chemokine_CCR7.
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; PR00641; CHEMOKINER7.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..379
FT                   /note="C-C chemokine receptor type 7"
FT                   /id="PRO_0000291858"
FT   TOPO_DOM        25..59
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..86
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..95
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..130
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..152
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..247
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        248..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..289
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..314
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..332
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        129..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   379 AA;  42875 MW;  E90D69FA0BC6C80D CRC64;
     MDLGKPMKNV LVVALLVIFQ VCLCQDEVTD NYIGDNTTVD YTLYESVCFK KDVRNFKAWF
     LPIMYSIICF VGLLGNGLVM LTYIYFKRLK TMTDTYLLNL ALADILFLLT LPFWAYSAAK
     SWVFGVHVCK LIFGIYKISF FSGMLLLLCI SIDRYVAIVQ AVSAHRHRAR VLLISKLSCL
     GIWMLAIVLS TPEVMYSGIQ KSSSEQALRC SLVTEHVEAL ITIQVAQMVV GFLIPLMAMS
     FCYLVIIRTL LQARNFERNK AIKVIIAVVV VFVAFQLPYN GVVLAHTVAN FNITSGTSCE
     LSKQLNIAYD VTYSLACVRC CVNPFLYAFI GVKFRSDLFK LFKDLGCLSQ EQLRQWSFCR
     HTRRSSMSVE AETTTTFSP