AGRG5_HUMAN
ID AGRG5_HUMAN Reviewed; 528 AA.
AC Q8IZF4; A0A024R6S3; A8K9R8; B3KXZ5; Q6ZMH7; Q6ZML4; Q86SL8; Q8IZ14;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Adhesion G-protein coupled receptor G5;
DE AltName: Full=G-protein coupled receptor 114;
DE AltName: Full=G-protein coupled receptor PGR27;
DE Flags: Precursor;
GN Name=ADGRG5; Synonyms=GPR114, PGR27; ORFNames=UNQ2524/PRO6017;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Spleen, Thymus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-225.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [6]
RP IDENTIFICATION.
RX PubMed=12435584; DOI=10.1016/s0014-5793(02)03574-3;
RA Fredriksson R., Lagerstroem M.C., Hoeglund P.J., Schioeth H.B.;
RT "Novel human G protein-coupled receptors with long N-terminals containing
RT GPS domains and Ser/Thr-rich regions.";
RL FEBS Lett. 531:407-414(2002).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=21724806; DOI=10.1189/jlb.0211092;
RA Peng Y.M., van de Garde M.D., Cheng K.F., Baars P.A., Remmerswaal E.B.,
RA van Lier R.A., Mackay C.R., Lin H.H., Hamann J.;
RT "Specific expression of GPR56 by human cytotoxic lymphocytes.";
RL J. Leukoc. Biol. 90:735-740(2011).
RN [8]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=25713288; DOI=10.1124/pr.114.009647;
RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT protein-coupled receptors.";
RL Pharmacol. Rev. 67:338-367(2015).
CC -!- FUNCTION: Adhesion G protein-coupled receptor (GPCR). Transduces
CC intracellular signals through coupling to guanine nucleotide-binding
CC protein G(s) subunit alpha and activation of adenylate cyclase pathway.
CC Isoform 1, but not isoform 2, is constitutively active, as evidenced by
CC elevated basal cAMP levels, and responds to mechanical activation
CC (shaking). {ECO:0000250|UniProtKB:Q3V3Z3, ECO:0000305|PubMed:25713288}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3V3Z3};
CC Multi-pass membrane protein {ECO:0000305|PubMed:25713288}.
CC -!- TISSUE SPECIFICITY: Expressed in immune cells. Primarily found in
CC granulocytes. Found in eosinophils. {ECO:0000269|PubMed:21724806}.
CC -!- PTM: Autoproteolysis between residues Leu-226 and Thr-227 occurs in the
CC lumen of the endoplasmic reticulum during receptor biosynthesis. The N-
CC terminal fragment (NTF) subsequently reassociates with the C-terminal
CC fragment (CTF) either in a homogeneric heterodimerization, or with
CC another family member through heterogeneric heterodimerization.
CC Autocatalytic cleavage is thought to be critical for the maturation,
CC stability, trafficking, and function. {ECO:0000305|PubMed:25713288}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN46670.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD18748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY358447; AAQ88812.1; -; mRNA.
DR EMBL; AK128298; BAG54657.1; -; mRNA.
DR EMBL; AK160368; BAD18711.1; -; mRNA.
DR EMBL; AK172765; BAD18748.1; ALT_INIT; mRNA.
DR EMBL; AK292783; BAF85472.1; -; mRNA.
DR EMBL; CH471092; EAW82936.1; -; Genomic_DNA.
DR EMBL; CH471092; EAW82938.1; -; Genomic_DNA.
DR EMBL; BC032401; AAH32401.1; -; mRNA.
DR EMBL; AY255609; AAO85121.1; -; mRNA.
DR EMBL; AY140956; AAN46670.1; ALT_SEQ; mRNA.
DR CCDS; CCDS10785.1; -.
DR RefSeq; NP_001291305.1; NM_001304376.2.
DR RefSeq; NP_001305410.1; NM_001318481.1.
DR RefSeq; NP_722579.1; NM_153837.3.
DR RefSeq; XP_011521251.1; XM_011522949.2.
DR RefSeq; XP_011521252.1; XM_011522950.2.
DR AlphaFoldDB; Q8IZF4; -.
DR SMR; Q8IZF4; -.
DR BioGRID; 128696; 193.
DR IntAct; Q8IZF4; 80.
DR STRING; 9606.ENSP00000342981; -.
DR ChEMBL; CHEMBL4523890; -.
DR MEROPS; P02.016; -.
DR GlyGen; Q8IZF4; 8 sites.
DR iPTMnet; Q8IZF4; -.
DR PhosphoSitePlus; Q8IZF4; -.
DR BioMuta; ADGRG5; -.
DR DMDM; 148886621; -.
DR MassIVE; Q8IZF4; -.
DR PaxDb; Q8IZF4; -.
DR PeptideAtlas; Q8IZF4; -.
DR PRIDE; Q8IZF4; -.
DR ProteomicsDB; 71342; -.
DR Antibodypedia; 1937; 71 antibodies from 21 providers.
DR DNASU; 221188; -.
DR Ensembl; ENST00000340339.4; ENSP00000342981.4; ENSG00000159618.16.
DR Ensembl; ENST00000349457.8; ENSP00000290823.4; ENSG00000159618.16.
DR GeneID; 221188; -.
DR KEGG; hsa:221188; -.
DR MANE-Select; ENST00000349457.8; ENSP00000290823.4; NM_001304376.3; NP_001291305.1.
DR UCSC; uc002elx.5; human.
DR CTD; 221188; -.
DR DisGeNET; 221188; -.
DR GeneCards; ADGRG5; -.
DR HGNC; HGNC:19010; ADGRG5.
DR HPA; ENSG00000159618; Group enriched (intestine, lymphoid tissue).
DR MIM; 616965; gene.
DR neXtProt; NX_Q8IZF4; -.
DR OpenTargets; ENSG00000159618; -.
DR PharmGKB; PA134896363; -.
DR VEuPathDB; HostDB:ENSG00000159618; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000161359; -.
DR HOGENOM; CLU_002753_3_9_1; -.
DR InParanoid; Q8IZF4; -.
DR OMA; HFALLSC; -.
DR OrthoDB; 501343at2759; -.
DR PhylomeDB; Q8IZF4; -.
DR TreeFam; TF321769; -.
DR PathwayCommons; Q8IZF4; -.
DR SignaLink; Q8IZF4; -.
DR BioGRID-ORCS; 221188; 19 hits in 1070 CRISPR screens.
DR ChiTaRS; ADGRG5; human.
DR GeneWiki; GPR114; -.
DR GenomeRNAi; 221188; -.
DR Pharos; Q8IZF4; Tdark.
DR PRO; PR:Q8IZF4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8IZF4; protein.
DR Bgee; ENSG00000159618; Expressed in granulocyte and 98 other tissues.
DR ExpressionAtlas; Q8IZF4; baseline and differential.
DR Genevisible; Q8IZF4; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR003910; GPR1/GPR3/GPR5.
DR InterPro; IPR000203; GPS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01422; GPR56ORPHANR.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..528
FT /note="Adhesion G-protein coupled receptor G5"
FT /id="PRO_0000012894"
FT TOPO_DOM 22..250
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 251..271
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 291..311
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..323
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 324..344
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..374
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..413
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 414..434
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 457..479
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..482
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 483..505
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 186..238
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT SITE 226..227
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305|PubMed:25713288"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 177..182
FT /note="WHNQSL -> PSISTQ (in Ref. 2; BAD18711)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="F -> S (in Ref. 2; BAF85472)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="I -> T (in Ref. 2; BAF85472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59000 MW; 35DE5E5C34FD2A3C CRC64;
MDHCGALFLC LCLLTLQNAT TETWEELLSY MENMQVSRGR SSVFSSRQLH QLEQMLLNTS
FPGYNLTLQT PTIQSLAFKL SCDFSGLSLT SATLKRVPQA GGQHARGQHA MQFPAELTRD
ACKTRPRELR LICIYFSNTH FFKDENNSSL LNNYVLGAQL SHGHVNNLRD PVNISFWHNQ
SLEGYTLTCV FWKEGARKQP WGGWSPEGCR TEQPSHSQVL CRCNHLTYFA VLMQLSPALV
PAELLAPLTY ISLVGCSISI VASLITVLLH FHFRKQSDSL TRIHMNLHAS VLLLNIAFLL
SPAFAMSPVP GSACTALAAA LHYALLSCLT WMAIEGFNLY LLLGRVYNIY IRRYVFKLGV
LGWGAPALLV LLSLSVKSSV YGPCTIPVFD SWENGTGFQN MSICWVRSPV VHSVLVMGYG
GLTSLFNLVV LAWALWTLRR LRERADAPSV RACHDTVTVL GLTVLLGTTW ALAFFSFGVF
LLPQLFLFTI LNSLYGFFLF LWFCSQRCRS EAEAKAQIEA FSSSQTTQ
