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Adhesion G-protein coupled receptor G2 (G-protein coupled receptor 64) (Mouse epididymis-specific protein 6) (Me6)

 AGRG2_MOUSE             Reviewed;        1009 AA.
Q8CJ12; A2AHP8; A2AHP9; A2AHQ0; A2AHQ3; Q8BL10; Q8CJ08; Q8CJ09;
Q8CJ10;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 121.
RecName: Full=Adhesion G-protein coupled receptor G2;
AltName: Full=G-protein coupled receptor 64;
AltName: Full=Mouse epididymis-specific protein 6;
Short=Me6;
Flags: Precursor;
Name=Adgrg2 {ECO:0000312|MGI:MGI:2446854}; Synonyms=Gpr64, Me6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5), TISSUE
SPECIFICITY, SUBUNIT, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
STRAIN=NMRI; 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15367682; DOI=10.1128/MCB.24.19.8642-8648.2004;
Davies B., Baumann C., Kirchhoff C., Ivell R., Nubbemeyer R.,
Habenicht U.F., Theuring F., Gottwald U.;
"Targeted deletion of the epididymal receptor HE6 results in fluid
dysregulation and male infertility.";
Mol. Cell. Biol. 24:8642-8648(2004).
[5]
TISSUE SPECIFICITY.
PubMed=18469038; DOI=10.1530/REP-08-0078;
Kirchhoff C., Osterhoff C., Samalecos A.;
"HE6/GPR64 adhesion receptor co-localizes with apical and subapical F-
actin scaffold in male excurrent duct epithelia.";
Reproduction 136:235-245(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1002, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Orphan receptor. Could be involved in a signal
transduction pathway controlling epididymal function and male
fertility. May regulate fluid exchange within epididymis.
{ECO:0000269|PubMed:15367682}.
-!- 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=5;
Name=1; Synonyms=Long;
IsoId=Q8CJ12-1; Sequence=Displayed;
Name=2; Synonyms=d2;
IsoId=Q8CJ12-2; Sequence=VSP_009808;
Name=3; Synonyms=d1;
IsoId=Q8CJ12-3; Sequence=VSP_009809;
Name=4; Synonyms=d3;
IsoId=Q8CJ12-4; Sequence=VSP_009807;
Name=5;
IsoId=Q8CJ12-5; Sequence=VSP_009806;
-!- TISSUE SPECIFICITY: Epididymis-specific expression (at protein
level). Associated with apical membranes of efferent ductule and
proximal epididymal duct epithelia. Mainly expressed in the
nonciliated principal cells of the proximal excurrent ducts.
{ECO:0000269|PubMed:12420295, ECO:0000269|PubMed:18469038}.
-!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
subunit and a seven-transmembrane subunit. {ECO:0000305}.
-!- PTM: Highly glycosylated. {ECO:0000269|PubMed:12420295}.
-!- DISRUPTION PHENOTYPE: Mutant male are infertile. Targeted
disruption leads to sperm stasis and duct obstruction, resulting
from dysregulation of fluid reabsorption.
{ECO:0000269|PubMed:15367682}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
Adhesion G-protein coupled receptor (ADGR) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF538952; AAN33054.1; -; mRNA.
EMBL; AF538955; AAN33057.1; -; mRNA.
EMBL; AF538956; AAN33058.1; -; mRNA.
EMBL; AF538957; AAN33059.1; -; mRNA.
EMBL; AK046871; BAC32902.1; -; mRNA.
EMBL; AL731801; CAM16675.1; -; Genomic_DNA.
EMBL; AL731801; CAM16676.1; -; Genomic_DNA.
EMBL; AL731801; CAM16677.1; -; Genomic_DNA.
EMBL; AL731801; CAM16680.1; -; Genomic_DNA.
CCDS; CCDS41196.1; -. [Q8CJ12-1]
CCDS; CCDS41197.1; -. [Q8CJ12-3]
CCDS; CCDS41199.1; -. [Q8CJ12-5]
CCDS; CCDS72459.1; -. [Q8CJ12-2]
CCDS; CCDS81192.1; -. [Q8CJ12-4]
RefSeq; NP_001073317.1; NM_001079848.2. [Q8CJ12-5]
RefSeq; NP_001073326.1; NM_001079857.2. [Q8CJ12-3]
RefSeq; NP_001277374.1; NM_001290445.1. [Q8CJ12-4]
RefSeq; NP_001277375.1; NM_001290446.1. [Q8CJ12-2]
RefSeq; NP_848827.1; NM_178712.4. [Q8CJ12-1]
UniGene; Mm.213016; -.
ProteinModelPortal; Q8CJ12; -.
STRING; 10090.ENSMUSP00000108019; -.
MEROPS; P02.007; -.
iPTMnet; Q8CJ12; -.
PhosphoSitePlus; Q8CJ12; -.
PaxDb; Q8CJ12; -.
PRIDE; Q8CJ12; -.
Ensembl; ENSMUST00000112400; ENSMUSP00000108019; ENSMUSG00000031298. [Q8CJ12-1]
Ensembl; ENSMUST00000112402; ENSMUSP00000108021; ENSMUSG00000031298. [Q8CJ12-3]
Ensembl; ENSMUST00000112404; ENSMUSP00000108023; ENSMUSG00000031298. [Q8CJ12-5]
Ensembl; ENSMUST00000112405; ENSMUSP00000108024; ENSMUSG00000031298. [Q8CJ12-4]
Ensembl; ENSMUST00000112408; ENSMUSP00000108027; ENSMUSG00000031298. [Q8CJ12-2]
GeneID; 237175; -.
KEGG; mmu:237175; -.
UCSC; uc009utd.2; mouse. [Q8CJ12-1]
UCSC; uc009ute.2; mouse. [Q8CJ12-3]
UCSC; uc009utg.2; mouse. [Q8CJ12-5]
UCSC; uc009uth.2; mouse. [Q8CJ12-2]
UCSC; uc009uti.2; mouse. [Q8CJ12-4]
CTD; 10149; -.
MGI; MGI:2446854; Adgrg2.
eggNOG; KOG4193; Eukaryota.
eggNOG; ENOG410XSD2; LUCA.
GeneTree; ENSGT00900000140853; -.
HOVERGEN; HBG051817; -.
InParanoid; Q8CJ12; -.
KO; K08451; -.
OMA; CVAKENV; -.
OrthoDB; EOG091G00P5; -.
PhylomeDB; Q8CJ12; -.
TreeFam; TF321769; -.
PRO; PR:Q8CJ12; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031298; -.
CleanEx; MM_GPR64; -.
ExpressionAtlas; Q8CJ12; baseline and differential.
Genevisible; Q8CJ12; MM.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
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 1009 Adhesion G-protein coupled receptor G2.
/FTId=PRO_0000012887.
TOPO_DOM 38 619 Extracellular. {ECO:0000305}.
TRANSMEM 620 640 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 641 659 Cytoplasmic. {ECO:0000305}.
TRANSMEM 660 680 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 681 683 Extracellular. {ECO:0000305}.
TRANSMEM 684 704 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 705 729 Cytoplasmic. {ECO:0000305}.
TRANSMEM 730 750 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 751 781 Extracellular. {ECO:0000305}.
TRANSMEM 782 802 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 803 826 Cytoplasmic. {ECO:0000305}.
TRANSMEM 827 847 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 848 849 Extracellular. {ECO:0000305}.
TRANSMEM 850 870 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 871 1009 Cytoplasmic. {ECO:0000305}.
DOMAIN 559 610 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
COMPBIAS 248 251 Poly-Ser.
COMPBIAS 664 669 Poly-Leu.
COMPBIAS 808 811 Poly-Lys.
COMPBIAS 917 922 Poly-Ser.
MOD_RES 1002 1002 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 362 362 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 534 534 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 539 539 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 543 543 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 589 589 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 849 849 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 40 66 Missing (in isoform 5).
{ECO:0000303|PubMed:12420295}.
/FTId=VSP_009806.
VAR_SEQ 51 66 Missing (in isoform 4).
{ECO:0000303|PubMed:12420295}.
/FTId=VSP_009807.
VAR_SEQ 64 66 Missing (in isoform 2).
{ECO:0000303|PubMed:12420295}.
/FTId=VSP_009808.
VAR_SEQ 80 93 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009809.
CONFLICT 781 781 T -> K (in Ref. 2; BAC32902).
{ECO:0000305}.
SEQUENCE 1009 AA; 110200 MW; A53C67C5527A5B6C CRC64;
MLFSGGQYSP VGRPEEVLLI YKIFLVIICF HVILVTSLKE NGNSSLLSPS AESSLVSLIP
YSNGTPDAAS EVLSTLNKTE KSKITIVKTF NASGVKSQRN ICNLSSLCND SVFFRGEIVF
QHDEDHNVTQ NQDTANGTFA GVLSLSELKR SELNKTLQTL SETYFIVCAT AEAQSTVNCT
FTVKLNETMN VCAMMVTFQT VQIRPMEQCC CSPRTPCPSS PEELEKLQCE LQDPIVCLAD
QPHGPPLSSS SKPVVPQATI ISHVASDFSL AEPLDHALMT PSTPSLTQES NLPSPQPTIP
LASSPATDLP VQSVVVSSLP QTDLSHTLSP VQSSIPSPTT PAPSVPTELV TISTPPGETV
VNTSTVSDLE AQVSQMEKAL SLGSLEPNLA GEMVNRVSKL LHSPPALLAP LAQRLLKVVD
AIGLQLNFSS TTISLTSPSL ALAVIRVNAS NFNTTTFAAQ DPTNLQVSLE TPPPENSIGA
ITLPSSLMNN LPANDVELAS RIQFNFFETP ALFQDPSLEN LTLISYVISS SVTNMTIKNL
TRNVTVALKH INPSPDDLTV KCVFWDLGRN GGKGGWSSDG CSVKDKRMNE TICTCSHLTS
FGILLDLSRT SLPPSQMMAL TFITYIGCGL SSIFLSVTLV TYIAFEKIRR DYPSKILIQL
CAALLLLNLI FLLDSWIALY NTRGFCIAVA VFLHYFLLVS FTWMGLEAFH MYLALVKVFN
TYIRKYILKF CIVGWGIPAV VVSIVLTISP DNYGIGSYGK FPNGTPDDFC WINSNVVFYI
TVVGYFCVIF LLNVSMFIVV LVQLCRIKKK KQLGAQRKTS IQDLRSIAGL TFLLGITWGF
AFFAWGPVNV TFMYLFAIFN TLQGFFIFIF YCAAKENVRK QWRRYLCCGK LRLAENSDWS
KTATNGLKKQ TVNQGVSSSS NSLQSSCNST NSTTLLVNSD CSVHASGNGN ASTERNGVSF
SVQNGDVCLH DLTGKQHMFS DKEDSCNGKS RIALRRTSKR GSLHFIEQM


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