ID M3YLW6_MUSPF Unreviewed; 1386 AA.
AC M3YLW6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Adhesion G protein-coupled receptor F5 {ECO:0000313|Ensembl:ENSMPUP00000012323.1, ECO:0000313|RefSeq:XP_012917059.1};
GN Name=ADGRF5 {ECO:0000313|Ensembl:ENSMPUP00000012323.1,
GN ECO:0000313|RefSeq:XP_012917059.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000012323.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000012323.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_012917059.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_012917059.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily.
CC {ECO:0000256|ARBA:ARBA00007343}.
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DR EMBL; AEYP01006005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01006006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01006007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01006008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012917059.1; XM_013061605.2.
DR STRING; 9669.ENSMPUP00000012323; -.
DR Ensembl; ENSMPUT00000012524.1; ENSMPUP00000012323.1; ENSMPUG00000012417.1.
DR GeneID; 101672064; -.
DR CTD; 221395; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000154603; -.
DR HOGENOM; CLU_002753_3_5_1; -.
DR OMA; VADTWFI; -.
DR OrthoDB; 3876300at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006112; P:energy reserve metabolic process; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR CDD; cd15254; 7tmB2_GPR116_Ig-Hepta; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR008078; GPCR_2_Ig-hepta-like_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR PANTHER; PTHR45813:SF4; ADHESION G PROTEIN-COUPLED RECEPTOR F5; 1.
DR PANTHER; PTHR45813; EF-HAND DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF01390; SEA; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01695; IGHEPTARCPTR.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF82671; SEA domain; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50024; SEA; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|RefSeq:XP_012917059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1386
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041198590"
FT TRANSMEM 1054..1081
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1093..1115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1135..1157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1169..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1211..1238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1259..1280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1286..1309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 166..273
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 274..366
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 509..596
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1052..1310
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1365..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 153827 MW; BE88C465544ED0C1 CRC64;
MKSPRRTTLC FMIVVIYFSQ ATLNLNLESI VHPLILHEHE PAGKDSLRQK RAVASSSPTA
EEYTVDVEIS FENASFLESI KASLYSLSFP IQGNSTDQAT TILSIEVTTV CRPTGNEIWC
SCETGYRWPR ERCLQNLTCQ ERDSIPAGHQ CSCLKGLPPK GPFCQLQGDV TLRMSVRLNV
GFQEDLKNTS SALYRSYKTD LETAFWKGYS ILPGFKLVTV TGFRPGSVVV TYEVQTTTPS
PDLMRKANEQ VMQNLNQTYK MDYGSFQAVT SNETKFTVIP EIIFEGDTVN LVCENEVLSS
NVSWHHVERR FDIQNSSRFL VYTTVLNNMT SISRLTIYNI TQGDAGEYIC KLTLDIFEYE
SRKKIDVTPI RIVATEEMKV TCDNNPVSLN CCSEINVNWS AIEWKQEGKI NIPGNPETDL
ESGCSRYTFR ADGTQCPSGS AGTTVIYECE FVSIHGAKGS KNIEVTFTSV GDNSSHNREV
HQLPRQEMEM STVESTTGNS LETKKAQEPQ ANLTITPDPI SVSEGQNFSI KCISDVSNYD
EVYWNTSAGI KIYQKFYTAR RSAAGAESVL TVETATREWN GTYHCIFRYK KSYSVATKDV
MVHPLPLEPD IMVDPLEATV PCKGSRHFRC CIEEDEDYKV TFQVDSLFFL AEKEVNGKQV
CYKHSFSASS VSWCPKKLDI FCHFTNAANN SVRSSAMKIN LVPGEKIMCR DPTIGVGEPG
KVIQKLCQFS DVPSSPAGPT GGTVTYKCVG SHWEVKKNDC ISAPIHSLLQ LAKALIKSPC
QDTKLPTYLK DLSVSTGKVK HEASSFPGSL GAIINILDLL STVPTQVNSE MMTNILSTVN
TILSKPMLST WKVSQHQPTN QSSQLLDSVE RFSRALWSED STFLSINQTN VQMRSIIIKP
GHPKPYKQSF VFSDSDLWGN VAIEKCELGS LPWGSSIVTV AFPTLKTILT QDSQGKNVAN
SLVMTTTVSH NITMPFQISM TFKNINPSGG EPQCVFWNFS LANHTGGWDS SGCEVRRVDG
DSVSCICDHL TSFSILMSPD SPYPGSLLEI LLDIISYIGL CFSILSLAAC LVVEAVVWKS
VTKNRTSYMR HICIVNIAAS LLVADIWFIV AAAIHDHFYP LNNTACVAAT FFIHFFYLSV
FFWMLTLGLM LFYRLVFILH DTSKSIQKTI AFSLGYGCPL VISVITVGAT QPQEVYTRKN
ACWLNWEDTK ALLAFVIPAL IIVVVNMTIT VVVISKILRP SIGDKPSKQE KSSLFQISKS
IGVLTPLLGL TWGFGLATVF QGSNAVFHII FTLLNAFQGL FILLFGCLWD QKVQESLLKK
FSQSRWSSQH SKSTSLGSST PVFSMSSPIS RRFNNLFGKT GTYNVSTPET SSSSLENTSS
AYSLLN
//
