ID A0A096MDT2_POEFO Unreviewed; 1018 AA.
AC A0A096MDT2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Adhesion G protein-coupled receptor F5-like {ECO:0000313|Ensembl:ENSPFOP00000029573.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000029573.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000029573.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYCK01009006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096MDT2; -.
DR Ensembl; ENSPFOT00000029504.1; ENSPFOP00000029573.1; ENSPFOG00000022589.1.
DR GeneTree; ENSGT00940000161541; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
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; IPR000203; GPS.
DR PANTHER; PTHR45813:SF10; ADHESION G PROTEIN-COUPLED RECEPTOR F5-RELATED; 1.
DR PANTHER; PTHR45813; EF-HAND DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Signal {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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1018
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001920270"
FT TRANSMEM 718..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 796..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 875..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 931..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 957..979
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 716..985
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
SQ SEQUENCE 1018 AA; 113405 MW; DA03F87598FA48A1 CRC64;
MWVFIFLYIL SLNCQNVSEN STQMYYAKLK IDRSAIQNIS SKLNFNVKGN LSIEDVTMTT
KCKENNNGNK TCKCKEGHKW SDEVRLTGVD CDEKNCTLKA DSNSMCTLSS AVDITGRFTL
EGAEFESCLT DKNSGTYKVC HNGLLNKMKI EYSKIRGFDS LAITQFSVGS VIVDFTMKIV
SDVSSGELFN KSTALTKTLT GKMTLETKGI VTLDISKTSV PYDNKTVVIC KTERQLEAKP
NWNLQRKDGE FLITNGSIST VEDEEKISTV TIKHVSELWQ GEYICLFVEQ EDQITINHKA
NATMDICLKP KIDISADPAF PLCKTESTVF VVKVKCEIKN TTETYSVSWQ EGAIEKPMTP
ADKVVNCKSG GDSSSTGSPL VYCNFTNECN QTYGASMKVE VIYPDEKYCS AEGEWANTKA
GFTAEIKCKD KAGTRKRKCS SGETGREGIW GDEVSECVEK DLASVLETAA ISDIGLGKLE
SNAAIVFERF VKVTKTLKLP GYANINTSVT VFTTMNEKLN LTTITNDSAI ENYLYSSSHL
LNKSLEDSWT KDTTDNSSLS MAERFMISVE NLIKISNLTV GTRRENLQVD LCNISSCNIN
VFNVTISVPG GVNVKTTAFK QLDKYLPHLD NKSEVNSIIV SATAENANDI SINFQMIKPR
PRNFQLKCVY WDTKNHKFSS EGCDWKGPSE EGRCDCKHFS SFALLLSKEP LEVPGLTYVT
YVALSVSVLS LVVTLVIELI VWSDVVKTST LYLRHTAHVN ICLCLLIGNL CFLASSSNPE
SISDLWCRTS AVLKHFCYLA MFFWTFCLSA TLLHQAVFLF HKVSRANYLR FSLVVGYAIP
LIIVFVTFLT CNGGAEGVYY FRKTCWLVYG GLFKGTFYTF IIPVGAIVFI NVFSMLVVIM
KLVSHHSEIH QKTDISPEKE KAAAKTVVRS IILLTPIFGV TWIFGFAILI FDLTSGPAAY
AFEYIFTILN GFQGFFILLT TCFGDRMTRE ALLRYIKKKA PASSVSESTS KSEVTWKK
//
