AGRE5_BOVIN
ID AGRE5_BOVIN Reviewed; 734 AA.
AC Q8SQA4;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Adhesion G protein-coupled receptor E5 {ECO:0000250|UniProtKB:P48960};
DE AltName: Full=Leukocyte antigen CD97 {ECO:0000250|UniProtKB:P48960};
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:0000250|UniProtKB:P48960};
GN Synonyms=CD97 {ECO:0000250|UniProtKB:P48960};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Eichler W., Haenel C., Vogel B., Stieler J.S.;
RT "Cloning and sequencing of cDNA encoding the bovine homologue of CD97.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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) and with chondroitin sulfate (By similarity).
CC {ECO:0000250}.
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth EGF
CC domain. {ECO:0000250}.
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}.
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DR EMBL; AJ416058; CAC94754.1; -; mRNA.
DR RefSeq; NP_788834.1; NM_176661.1.
DR AlphaFoldDB; Q8SQA4; -.
DR SMR; Q8SQA4; -.
DR MEROPS; P02.002; -.
DR PRIDE; Q8SQA4; -.
DR GeneID; 338066; -.
DR KEGG; bta:338066; -.
DR CTD; 976; -.
DR InParanoid; Q8SQA4; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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 Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01278; CD97PROTEIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Secreted; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..734
FT /note="Adhesion G protein-coupled receptor E5"
FT /id="PRO_0000012867"
FT CHAIN 27..428
FT /note="Adhesion G protein-coupled receptor E5 subunit
FT alpha"
FT /evidence="ECO:0000305"
FT /id="PRO_0000449607"
FT CHAIN 429..734
FT /note="Adhesion G protein-coupled receptor E5 subunit beta"
FT /evidence="ECO:0000305"
FT /id="PRO_0000449608"
FT TOPO_DOM 27..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..593
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..662
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 663..683
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..734
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..70
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 71..122
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 123..171
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 390..440
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 712..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 428..429
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 713
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48960"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48960"
FT MOD_RES 724
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48960"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48960"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48960"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 36..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 50..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 75..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 83..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 100..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 127..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 134..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 151..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 734 AA; 80322 MW; 4EE8AF4A63502998 CRC64;
MGGPHGGPFL LFHVLCFLLT LSEVGSQNSK ACALPCPPNS SCVNGTACRC APGFISFSGE
IFTDPLESCD DINECGPPSP VDCGSSADCQ NTEGGYYCTC SPGYEPVSGA MIFRNESENT
CRDVDECSSG QHQCHNSTVC FNTVGSYTCH CREGWEPKHG LKNKQKDTIC KEISFPAWTA
PPGIKSRSLS AFFERVQKMS RDFKPAMAKK SMQDLVGSVD DLLKNSGDLE SLDQSSKHVT
VTHLLSGLEQ ILRTLAKAMP KGSFTYRSLD NTELSLVVQE QGKGNVTVGQ SHARMLLDWA
VAAAAEESGP TVVGILSSQN MKKLLANASL KLDSEKLKET YKSPVRGAKV TLLSAVSSVF
LSNTNTEKLD SNVSFAFALH EQPELKPRQE LICAFWKKDS NGNGSWATTG CWKMGRGNGS
ITCQCSHLSS FAILMAHYDV EDPKLALITK VGLALSLACL LLCILTFLLV RPIQGSRTTV
HLHLCICLFV GSAIFLAGIE NEGGEVGTRC RLVAVLLHYC FLAAFCWMSL EGVELYFLVV
RVFQGQGMRK LWLCLIGYGV PLIIVGISAG AYSKGYGREK FCWLNFEGGF LWSFVGPVTF
IVLGNAIIFV ITVWKLTQKF SEINPDIKKL KKARVLTITA IAQLFVLGCT WVFGLLLFNP
ESWVLSYIFS ILNCLQGFFL FVLYCLLNKK VREEYRKWAC MVAGNKYSEF ATTTSGSGSS
HNQTQALRPS ESGM
