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   24-JAN-2024, entry version 163.
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   PDB; 7EQ1; EM; 3.30 A; R=227-528.
DR   PDBsum; 7EQ1; -.
DR   AlphaFoldDB; Q8IZF4; -.
DR   EMDB; EMD-31254; -.
DR   SMR; Q8IZF4; -.
DR   BioGRID; 128696; 193.
DR   IntAct; Q8IZF4; 80.
DR   STRING; 9606.ENSP00000342981; -.
DR   ChEMBL; CHEMBL4523890; -.
DR   MEROPS; P02.016; -.
DR   GlyCosmos; Q8IZF4; 8 sites, No reported glycans.
DR   GlyGen; Q8IZF4; 8 sites.
DR   iPTMnet; Q8IZF4; -.
DR   PhosphoSitePlus; Q8IZF4; -.
DR   BioMuta; ADGRG5; -.
DR   DMDM; 148886621; -.
DR   MassIVE; Q8IZF4; -.
DR   PaxDb; 9606-ENSP00000342981; -.
DR   PeptideAtlas; Q8IZF4; -.
DR   ProteomicsDB; 71342; -.
DR   Antibodypedia; 1937; 85 antibodies from 22 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   AGR; HGNC:19010; -.
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; RIHVNLH; -.
DR   OrthoDB; 5477252at2759; -.
DR   PhylomeDB; Q8IZF4; -.
DR   TreeFam; TF321769; -.
DR   PathwayCommons; Q8IZF4; -.
DR   SignaLink; Q8IZF4; -.
DR   BioGRID-ORCS; 221188; 20 hits in 1148 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 99 other cell types or tissues.
DR   ExpressionAtlas; Q8IZF4; baseline and differential.
DR   GO; GO:0016020; C:membrane; TAS:GDB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   CDD; cd15443; 7tmB2_GPR114; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR003910; GPR1/GPR3/GPR5.
DR   InterPro; IPR000203; GPS.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR12011:SF326; ADHESION G-PROTEIN COUPLED RECEPTOR G5; 1.
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.
DR   Genevisible; Q8IZF4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; G-protein coupled receptor; Glycoprotein;
KW   Membrane; 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"
FT   HELIX           229..232
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   STRAND          242..244
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           245..272
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           281..298
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           300..303
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           313..343
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           354..363
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   TURN            364..370
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           371..375
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   TURN            391..396
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   TURN            409..411
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           412..416
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           417..441
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           457..466
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           469..472
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           481..492
FT                   /evidence="ECO:0007829|PDB:7EQ1"
FT   HELIX           495..519
FT                   /evidence="ECO:0007829|PDB:7EQ1"
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
//