AGRE5_HUMAN
ID AGRE5_HUMAN Reviewed; 835 AA.
AC P48960; A8K7Z4; B2RBJ9; O00718; O76101; Q8NG72; Q8TBQ7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 4.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Adhesion G protein-coupled receptor E5 {ECO:0000312|HGNC:HGNC:1711};
DE AltName: Full=Leukocyte antigen CD97 {ECO:0000303|PubMed:7636245};
DE AltName: CD_antigen=CD97;
DE Contains:
DE RecName: Full=Adhesion G protein-coupled receptor E5 subunit alpha;
DE Contains:
DE RecName: Full=Adhesion G protein-coupled receptor E5 subunit beta;
DE Flags: Precursor;
GN Name=ADGRE5 {ECO:0000312|HGNC:HGNC:1711};
GN Synonyms=CD97 {ECO:0000312|HGNC:HGNC:1711};
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 [MRNA] (ISOFORM 2).
RX PubMed=7636245;
RA Hamann J., Eichler W., Hamann D., Kerstens H.M.J., Poddighe P.J.,
RA Hoovers J.M.N., Hartmann J.M., Strauss M., van Lier R.A.W.;
RT "Expression cloning and chromosomal mapping of the leukocyte activation
RT antigen CD97, a new seven-span transmembrane molecule of the secretion
RT receptor superfamily with an unusual extracellular domain.";
RL J. Immunol. 155:1942-1950(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Foreskin;
RX PubMed=8786105; DOI=10.1006/geno.1996.0092;
RA Hamann J., Hartmann E., van Lier R.A.W.;
RT "Structure of the human CD97 gene: exon shuffling has generated a new type
RT of seven-span transmembrane molecule related to the secretin receptor
RT superfamily.";
RL Genomics 32:144-147(1996).
RN [3]
RP SEQUENCE REVISION.
RA Hamann J.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=8955192;
RA Gray J.X., Haino M., Roth M.J., Maguire J.E., Jensen P.N., Yarme A.,
RA Stetler-Stevenson M.-A., Siebenlist U., Kelly K.;
RT "CD97 is a processed, seven-transmembrane, heterodimeric receptor
RT associated with inflammation.";
RL J. Immunol. 157:5438-5447(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Synovium;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon adenocarcinoma;
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 [10]
RP INTERACTION WITH DAF.
RX PubMed=11297558; DOI=10.1074/jbc.m101770200;
RA Lin H.-H., Stacey M., Saxby C., Knott V., Chaudhry Y., Evans D., Gordon S.,
RA McKnight A.J., Handford P., Lea S.;
RT "Molecular analysis of the epidermal growth factor-like short consensus
RT repeat domain-mediated protein-protein interactions: dissection of the
RT CD97-CD55 complex.";
RL J. Biol. Chem. 276:24160-24169(2001).
RN [11]
RP INTERACTION WITH CHONDROITIN SULFATE.
RX PubMed=12829604; DOI=10.1182/blood-2002-11-3540;
RA Stacey M., Chang G.-W., Davies J.Q., Kwakkenbos M.J., Sanderson R.D.,
RA Hamann J., Gordon S., Lin H.-H.;
RT "The epidermal growth factor-like domains of the human EMR2 receptor
RT mediate cell attachment through chondroitin sulfate glycosaminoglycans.";
RL Blood 102:2916-2924(2003).
RN [12]
RP REVIEW.
RX PubMed=14647991; DOI=10.1007/s00251-003-0625-2;
RA Kwakkenbos M.J., Kop E.N., Stacey M., Matmati M., Gordon S., Lin H.H.,
RA Hamann J.;
RT "The EGF-TM7 family: a postgenomic view.";
RL Immunogenetics 55:655-666(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-453.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-371.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831 AND SER-833, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815; THR-816; SER-818;
RP THR-825 AND SER-831, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Receptor potentially involved in both adhesion and signaling
CC processes early after leukocyte activation. Plays an essential role in
CC leukocyte migration. {ECO:0000250|UniProtKB:Q9Z0M6}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region (alpha subunit) non-covalently linked to a seven-transmembrane
CC moiety (beta subunit). Interacts with complement decay-accelerating
CC factor (DAF). The largest isoform (isoform 1) interacts with
CC chondroitin sulfate. {ECO:0000269|PubMed:11297558,
CC ECO:0000269|PubMed:12829604}.
CC -!- INTERACTION:
CC P48960; P08174: CD55; NbExp=2; IntAct=EBI-1756009, EBI-1033846;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Z0M6};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor E5 subunit
CC alpha]: Secreted, extracellular space {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=EGF(1,2,3,4,5);
CC IsoId=P48960-1; Sequence=Displayed;
CC Name=2; Synonyms=EGF(1,2,5);
CC IsoId=P48960-2; Sequence=VSP_009411;
CC Name=3; Synonyms=EGF(1,2,3,5);
CC IsoId=P48960-3; Sequence=VSP_009412;
CC -!- TISSUE SPECIFICITY: Broadly expressed, found on most hematopoietic
CC cells, including activated lymphocytes, monocytes, macrophages,
CC dendritic cells, and granulocytes. Expressed also abundantly by smooth
CC muscle cells. Expressed in thyroid, colorectal, gastric, esophageal and
CC pancreatic carcinomas too. Expression are increased under inflammatory
CC conditions in the CNS of multiple sclerosis and in synovial tissue of
CC patients with rheumatoid arthritis. Increased expression of CD97 in the
CC synovium is accompanied by detectable levels of soluble CD97 in the
CC synovial fluid.
CC -!- INDUCTION: Rapid up-regulation during lymphocyte activation.
CC -!- DOMAIN: The first two EGF domains mediate the interaction with DAF. A
CC third tandemly arranged EGF domain is necessary for the structural
CC integrity of the binding region.
CC -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth EGF
CC domain.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha
CC subunit and a seven-transmembrane subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27673.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC06178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CD97ID996ch19p13.html";
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DR EMBL; X84700; CAA59173.1; -; mRNA.
DR EMBL; X94630; CAA64333.1; -; Genomic_DNA.
DR EMBL; X94631; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94632; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94633; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; Z99830; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; Z99831; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94634; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94635; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94636; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94637; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94638; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94639; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94640; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94641; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94642; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94643; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94644; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94645; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94646; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; X94647; CAA64333.1; JOINED; Genomic_DNA.
DR EMBL; U76764; AAB36682.1; -; mRNA.
DR EMBL; AB065966; BAC06178.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005327; AAC27673.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK292159; BAF84848.1; -; mRNA.
DR EMBL; AK314697; BAG37246.1; -; mRNA.
DR EMBL; CH471106; EAW84412.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84413.1; -; Genomic_DNA.
DR EMBL; BC026690; AAH26690.1; -; mRNA.
DR CCDS; CCDS32929.1; -. [P48960-1]
DR CCDS; CCDS32930.1; -. [P48960-3]
DR CCDS; CCDS32931.1; -. [P48960-2]
DR PIR; I37225; I37225.
DR RefSeq; NP_001020331.1; NM_001025160.2. [P48960-3]
DR RefSeq; NP_001775.2; NM_001784.4. [P48960-2]
DR RefSeq; NP_510966.1; NM_078481.3. [P48960-1]
DR RefSeq; XP_016883036.1; XM_017027547.1.
DR PDB; 2BOU; X-ray; 1.90 A; A=22-32.
DR PDB; 7DO4; X-ray; 3.20 A; A=21-258.
DR PDBsum; 2BOU; -.
DR PDBsum; 7DO4; -.
DR AlphaFoldDB; P48960; -.
DR SMR; P48960; -.
DR BioGRID; 107414; 189.
DR DIP; DIP-52292N; -.
DR IntAct; P48960; 62.
DR MINT; P48960; -.
DR STRING; 9606.ENSP00000242786; -.
DR ChEMBL; CHEMBL4523865; -.
DR MEROPS; P02.002; -.
DR TCDB; 9.A.14.6.2; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 1090; 10 N-Linked glycans (3 sites).
DR GlyGen; P48960; 11 sites, 10 N-linked glycans (3 sites), 3 O-linked glycans (1 site).
DR iPTMnet; P48960; -.
DR PhosphoSitePlus; P48960; -.
DR SwissPalm; P48960; -.
DR BioMuta; ADGRE5; -.
DR DMDM; 90110013; -.
DR EPD; P48960; -.
DR jPOST; P48960; -.
DR MassIVE; P48960; -.
DR MaxQB; P48960; -.
DR PaxDb; P48960; -.
DR PeptideAtlas; P48960; -.
DR PRIDE; P48960; -.
DR ProteomicsDB; 55949; -. [P48960-1]
DR ProteomicsDB; 55950; -. [P48960-2]
DR ProteomicsDB; 55951; -. [P48960-3]
DR TopDownProteomics; P48960-2; -. [P48960-2]
DR Antibodypedia; 2852; 876 antibodies from 43 providers.
DR DNASU; 976; -.
DR Ensembl; ENST00000242786.6; ENSP00000242786.4; ENSG00000123146.20. [P48960-1]
DR Ensembl; ENST00000357355.7; ENSP00000349918.2; ENSG00000123146.20. [P48960-3]
DR Ensembl; ENST00000358600.7; ENSP00000351413.2; ENSG00000123146.20. [P48960-2]
DR GeneID; 976; -.
DR KEGG; hsa:976; -.
DR MANE-Select; ENST00000242786.6; ENSP00000242786.4; NM_078481.4; NP_510966.1.
DR UCSC; uc002myl.4; human. [P48960-1]
DR CTD; 976; -.
DR DisGeNET; 976; -.
DR GeneCards; ADGRE5; -.
DR HGNC; HGNC:1711; ADGRE5.
DR HPA; ENSG00000123146; Tissue enhanced (bone).
DR MIM; 601211; gene.
DR neXtProt; NX_P48960; -.
DR OpenTargets; ENSG00000123146; -.
DR PharmGKB; PA26248; -.
DR VEuPathDB; HostDB:ENSG00000123146; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000160578; -.
DR HOGENOM; CLU_002753_3_7_1; -.
DR InParanoid; P48960; -.
DR OMA; SEFSYSH; -.
DR OrthoDB; 210309at2759; -.
DR PhylomeDB; P48960; -.
DR TreeFam; TF316380; -.
DR PathwayCommons; P48960; -.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P48960; -.
DR SIGNOR; P48960; -.
DR BioGRID-ORCS; 976; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; ADGRE5; human.
DR GeneWiki; CD97; -.
DR GenomeRNAi; 976; -.
DR Pharos; P48960; Tbio.
DR PRO; PR:P48960; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P48960; protein.
DR Bgee; ENSG00000123146; Expressed in granulocyte and 138 other tissues.
DR ExpressionAtlas; P48960; baseline and differential.
DR Genevisible; P48960; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003056; GPCR_2_ADGRE2_ADGRE5.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 4.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01278; CD97PROTEIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 4.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Disulfide bond; EGF-like domain; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
KW Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..835
FT /note="Adhesion G protein-coupled receptor E5"
FT /id="PRO_0000012868"
FT CHAIN 21..530
FT /note="Adhesion G protein-coupled receptor E5 subunit
FT alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000296235"
FT CHAIN 531..835
FT /note="Adhesion G protein-coupled receptor E5 subunit beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000296236"
FT TOPO_DOM 21..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..572
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..601
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..620
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..642
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..739
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..766
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..789
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 790..835
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..63
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 64..115
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 116..159
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 160..208
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 209..257
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 492..542
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 814..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 530..531
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 816
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 825
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 30..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 44..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 68..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 76..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 93..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 120..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 127..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 144..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 164..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 171..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 188..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 213..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 220..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 237..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 116..208
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7636245,
FT ECO:0000303|PubMed:8955192"
FT /id="VSP_009411"
FT VAR_SEQ 160..208
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8955192"
FT /id="VSP_009412"
FT VARIANT 367
FT /note="R -> Q (in dbSNP:rs2230748)"
FT /id="VAR_017760"
FT CONFLICT 103
FT /note="A -> T (in Ref. 4; AAB36682)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="G -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="A -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7DO4"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7DO4"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7DO4"
SQ SEQUENCE 835 AA; 91869 MW; 06DDDE9178BC494B CRC64;
MGGRVFLAFC VWLTLPGAET QDSRGCARWC PQNSSCVNAT ACRCNPGFSS FSEIITTPTE
TCDDINECAT PSKVSCGKFS DCWNTEGSYD CVCSPGYEPV SGAKTFKNES ENTCQDVDEC
QQNPRLCKSY GTCVNTLGSY TCQCLPGFKF IPEDPKVCTD VNECTSGQNP CHSSTHCLNN
VGSYQCRCRP GWQPIPGSPN GPNNTVCEDV DECSSGQHQC DSSTVCFNTV GSYSCRCRPG
WKPRHGIPNN QKDTVCEDMT FSTWTPPPGV HSQTLSRFFD KVQDLGRDSK TSSAEVTIQN
VIKLVDELME APGDVEALAP PVRHLIATQL LSNLEDIMRI LAKSLPKGPF TYISPSNTEL
TLMIQERGDK NVTMGQSSAR MKLNWAVAAG AEDPGPAVAG ILSIQNMTTL LANASLNLHS
KKQAELEEIY ESSIRGVQLR RLSAVNSIFL SHNNTKELNS PILFAFSHLE SSDGEAGRDP
PAKDVMPGPR QELLCAFWKS DSDRGGHWAT EGCQVLGSKN GSTTCQCSHL SSFAILMAHY
DVEDWKLTLI TRVGLALSLF CLLLCILTFL LVRPIQGSRT TIHLHLCICL FVGSTIFLAG
IENEGGQVGL RCRLVAGLLH YCFLAAFCWM SLEGLELYFL VVRVFQGQGL STRWLCLIGY
GVPLLIVGVS AAIYSKGYGR PRYCWLDFEQ GFLWSFLGPV TFIILCNAVI FVTTVWKLTQ
KFSEINPDMK KLKKARALTI TAIAQLFLLG CTWVFGLFIF DDRSLVLTYV FTILNCLQGA
FLYLLHCLLN KKVREEYRKW ACLVAGGSKY SEFTSTTSGT GHNQTRALRA SESGI
