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Database: UniProt
Entry: A0A091UC25_PHALP
LinkDB: A0A091UC25_PHALP
Original site: A0A091UC25_PHALP 
ID   A0A091UC25_PHALP        Unreviewed;      1209 AA.
AC   A0A091UC25;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative G-protein coupled receptor 125 {ECO:0000313|EMBL:KFQ71588.1};
DE   Flags: Fragment;
GN   ORFNames=N335_07055 {ECO:0000313|EMBL:KFQ71588.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC   Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ71588.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ71588.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ71588.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KK445752; KFQ71588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091UC25; -.
DR   PhylomeDB; A0A091UC25; -.
DR   Proteomes; UP000053638; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd15999; 7tmB2_GPR125; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
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; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45930:SF2; ADHESION G PROTEIN-COUPLED RECEPTOR A3; 1.
DR   PANTHER; PTHR45930; G-PROTEIN COUPLED RECEPTOR 124-LIKE PROTEIN; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF111418; Hormone receptor domain; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFQ71588.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053638};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        650..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        683..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        716..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        765..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        805..828
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        884..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        913..932
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          132..230
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          213..308
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          644..931
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          962..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1086..1148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1069
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1117..1144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ71588.1"
FT   NON_TER         1209
FT                   /evidence="ECO:0000313|EMBL:KFQ71588.1"
SQ   SEQUENCE   1209 AA;  134730 MW;  E159C3612F9A1A0D CRC64;
     DLKNNLISTI GPGAFLGLSS LKRLDLTNNR IGCLNADVFR GLVNLIRLNL SGNLFSTLTQ
     GTFDHLGSLK SLEFQTDYLL CDCNILWMHQ WLKERNITVR ETKCAYPKSL QSQTVTGVKQ
     ELLTCEPPLE LPSFYMTPSH RQVVFEGDSL PFQCMASYID QDMQVLWYQD GKIVETDESQ
     GIFVEKNMIH NCSLIASALT ISNIQAGSTG NWGCHVQTRR GNNTRTVDIV VLESSAQYCP
     PERVVNNKGD FRWPRTLAGI TAYLLCTRYS AGSGIYPGNS QDERRAWRRC DRGGYWAEED
     YSRCQYANDV TRVLYMFNQM PLNLTNAVAT ARQLLAYTVE AANFSDKMDV IFVAEMIEKF
     GRFAEKYKEL GDVMVDIASN IMLADERVLW MAQREAKACT RIVQCLQKIA MYRLANGAQV
     YSTYSPNIAL EAYVIKAAAF TGMTCTVFQK VATSDRTGLS EYGRRDPDGN LDKQLSFKCN
     VSNTLSSLAL KNTIVEASIQ LPASLFTQKQ KREIRPADES VYKLQLIAFR NGKLFPATGN
     STNLADDGKR RTVVTPVILT KIDGLNLASH HVPINVTLRR IAHGADAVAA QWDFDLLNGQ
     GGWKSDGCRI LLSDENITTI QCYSLSNYAV LMDLTGAELY TQPADLLHPV IYATAMVLLM
     CLLMIIISYI YHHSVIRISV KSWHMLVNLS FHIFLTCVMF IGGITQTRHA SICQAVGIIL
     HYSTLATVLW LGVTSRNIYK QVTKKAKRCQ DPDEPPPPPR PMLRFYLIGG GIPIIVCGIT
     AAANIRNYGS RPNAPYCWMT WEPSLGAFYG PASFIIFINC MYFLSIFIQL KRHPERKYEL
     KEPIEEQQRL ATNEHGELAH QDSLSVSLVS TSALENEHSF QAQLLGVGLT LLLYVALWIF
     GALSVSLYYP MDLIFSCFFG ATCLSLSAFL MVHHCVNRED VRHAWITTCC PGRSTYSVQV
     NVQPSSSSGT NGEAPKCTNS SAESSCTNKS VSSLKNSSQG CKLTNLQAAA AQCHPTSLPL
     NTGPQLDNSL TEHSVDNDIK MHVAPLEVQF RTNGHPSRHH KNRSKGHRAS RLAVLREYAY
     DVPTSVEGSV QNGLPKSRQS NSEAHSRSRR AYLAYRERQY NQSQQDSSDA CSTLPKSSRN
     TEKTIATNNK KDILRKPIAV ELENQQKSYG LNLAVQNGPL KSSGQDGPLL TADSTGNIRT
     GLWKHETTV
//
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