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Adhesion G-protein coupled receptor G2 (G-protein coupled receptor 64) (Rat epididymis-specific protein 6) (Re6)

 AGRG2_RAT               Reviewed;        1013 AA.
Q8CJ11; Q8CJ06; Q8CJ07;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 118.
RecName: Full=Adhesion G-protein coupled receptor G2;
AltName: Full=G-protein coupled receptor 64;
AltName: Full=Rat epididymis-specific protein 6;
Short=Re6;
Flags: Precursor;
Name=Adgrg2 {ECO:0000312|RGD:628618}; Synonyms=Gpr64, Re6;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), GLYCOSYLATION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=Lewis; TISSUE=Epididymis;
PubMed=12420295; DOI=10.1002/mrd.10220;
Obermann H., Samalecos A., Osterhoff C., Schroeder B., Heller R.,
Kirchhoff C.;
"HE6, a two-subunit heptahelical receptor associated with apical
membranes of efferent and epididymal duct epithelia.";
Mol. Reprod. Dev. 64:13-26(2003).
-!- FUNCTION: Orphan receptor. Could be involved in a signal
transduction pathway controlling epididymal function and male
fertility. May regulate fluid exchange within epididymis.
{ECO:0000250|UniProtKB:Q8CJ12}.
-!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic
processing; the large extracellular N-terminal fragment and the
membrane-bound C-terminal fragment predominantly remain associated
and non-covalently linked. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:12420295}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long;
IsoId=Q8CJ11-1; Sequence=Displayed;
Name=2; Synonyms=d2;
IsoId=Q8CJ11-2; Sequence=VSP_009810;
Name=3; Synonyms=d1;
IsoId=Q8CJ11-3; Sequence=VSP_009811;
-!- TISSUE SPECIFICITY: Epididymis-specific expression (at protein
level). Associated with apical membranes of efferent ductule and
proximal epididymal duct epithelia (PubMed:12420295).
{ECO:0000269|PubMed:12420295}.
-!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
subunit and a seven-transmembrane subunit. {ECO:0000305}.
-!- PTM: Highly glycosylated. {ECO:0000269|PubMed:12420295}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
Adhesion G-protein coupled receptor (ADGR) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF538953; AAN33055.1; -; mRNA.
EMBL; AF538958; AAN33060.1; -; mRNA.
EMBL; AF538959; AAN33061.1; -; mRNA.
RefSeq; NP_001257800.1; NM_001270871.1. [Q8CJ11-3]
RefSeq; NP_001257801.1; NM_001270872.1. [Q8CJ11-2]
RefSeq; NP_852031.1; NM_181366.2. [Q8CJ11-1]
RefSeq; XP_017457416.1; XM_017601927.1. [Q8CJ11-1]
UniGene; Rn.57243; -.
ProteinModelPortal; Q8CJ11; -.
STRING; 10116.ENSRNOP00000039239; -.
MEROPS; P02.007; -.
PhosphoSitePlus; Q8CJ11; -.
PaxDb; Q8CJ11; -.
PRIDE; Q8CJ11; -.
Ensembl; ENSRNOT00000040770; ENSRNOP00000039239; ENSRNOG00000032472. [Q8CJ11-1]
Ensembl; ENSRNOT00000058833; ENSRNOP00000055623; ENSRNOG00000032472. [Q8CJ11-2]
Ensembl; ENSRNOT00000058834; ENSRNOP00000055624; ENSRNOG00000032472. [Q8CJ11-3]
GeneID; 266735; -.
KEGG; rno:266735; -.
CTD; 10149; -.
RGD; 628618; Adgrg2.
eggNOG; KOG4193; Eukaryota.
eggNOG; ENOG410XSD2; LUCA.
GeneTree; ENSGT00910000143993; -.
HOGENOM; HOG000231476; -.
HOVERGEN; HBG051817; -.
InParanoid; Q8CJ11; -.
KO; K08451; -.
OMA; CVAKENV; -.
OrthoDB; EOG091G00P5; -.
PhylomeDB; Q8CJ11; -.
TreeFam; TF321769; -.
PRO; PR:Q8CJ11; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000032472; -.
Genevisible; Q8CJ11; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
InterPro; IPR000203; GPS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF01825; GPS; 1.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00303; GPS; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 37 {ECO:0000255}.
CHAIN 38 1013 Adhesion G-protein coupled receptor G2.
/FTId=PRO_0000012888.
TOPO_DOM 38 623 Extracellular. {ECO:0000305}.
TRANSMEM 624 644 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 645 663 Cytoplasmic. {ECO:0000305}.
TRANSMEM 664 684 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 685 688 Extracellular. {ECO:0000305}.
TRANSMEM 689 709 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 710 733 Cytoplasmic. {ECO:0000305}.
TRANSMEM 734 754 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 755 785 Extracellular. {ECO:0000305}.
TRANSMEM 786 806 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 807 830 Cytoplasmic. {ECO:0000305}.
TRANSMEM 831 851 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 852 853 Extracellular. {ECO:0000305}.
TRANSMEM 854 874 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 875 1013 Cytoplasmic. {ECO:0000305}.
DOMAIN 563 614 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
COMPBIAS 249 252 Poly-Ser.
COMPBIAS 668 673 Poly-Leu.
COMPBIAS 812 815 Poly-Lys.
COMPBIAS 921 926 Poly-Ser.
MOD_RES 1006 1006 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP9}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 457 457 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 538 538 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 543 543 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 547 547 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 593 593 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 777 777 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 853 853 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 40 67 Missing (in isoform 2).
{ECO:0000303|PubMed:12420295}.
/FTId=VSP_009810.
VAR_SEQ 52 67 Missing (in isoform 3).
{ECO:0000303|PubMed:12420295}.
/FTId=VSP_009811.
SEQUENCE 1013 AA; 110701 MW; 03C5467D84527216 CRC64;
MLFSGGQYSP VGRPEEVLLI YKIFLVIICF HAILVTSLKE NAGNSSLLSP SAESSLVSLV
PYSNGTPDAA SEVLSTLNRT EKSKITILKT FNASGVKSQR NICNLSSICS DSVFFRGEIV
FQHDDHYNVT QNQDIVNSTF AGVLSLSELK RTELNKTLQT LSETYFIVCA TAEAQNTLNC
TFTVKLNETM NVCAMMVTFK SVQIRPMEQC CCSPRTPCPS SPEELEKLQC DLQDPIVCLA
DQPHGPPVSS SSKPVPVVPQ ATIFSHVASD FSLAEPLDHA LMTSSTPSLA QETRLPSPQP
TISLTSSPAI DLPVQHVVAS SSLPQTDLSH TLSPVQSSIP SPTTAAPSVP EKVVAISTPP
GETVVNTSSV PDLEAQVSQM EKALSLGSLE PNLAGEMVNR VSKLLHSPLA LLAPLAQRLL
KVVDAIGLQL NFSSTTISLT SPSLALAVIR VNASNFNTTT FAAQDPANLQ VSLEAQAPKN
SIGAITLPSS LMSNLPASEV ELASRVQFNF FETPALFQDP SLENLSLISY VISSSVTNMT
IKNLTRNVTV ALKHINPSQD DLTVKCVFWD LNRNGGRGGW SSDGCSVKEK RMNETICTCS
HLTSFGILLD LSRTSLPPSQ MMALTFITYI GCGLSSIFLS VTLVTYIAFE KIRRDYPSKI
LIQLCAALLL LNLVFLLDSW IALYNARGFC ISVAVFLHYF LLVSFTWMGL EAFHMYLALV
KVFNTYIRKY ILKFCIVGWG IPAVVVSIVL TISPDNYGIG SYGKFPNGTP DDFCWINSSV
VFYITVVGYF CVIFLLNVSM FIVVLVQLCR IKKKKQLGAQ RKTSIQDLRS IAGLTFLLGI
TWGFAFFAWG PVNLTFMYLF AIFNTLQGFF IFIFYCAAKE NVRKQWRRYL CCGKLRLAEN
SDWSKTATNG LKKQTVNQGV SSSSNSLQSS CNSTNSTTLL VNSDCSVHAS GNGNASTERN
GVSFSVQNGD VCLHDLTGKQ HMFSDKEDSC NGKSRMALRR TSKRGSLHFI EQM


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