ID A0A1I8FSZ9_9PLAT Unreviewed; 765 AA.
AC A0A1I8FSZ9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=G_PROTEIN_RECEP_F2_4 domain-containing protein {ECO:0000313|WBParaSite:maker-unitig_5295-snap-gene-0.2-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-unitig_5295-snap-gene-0.2-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-unitig_5295-snap-gene-0.2-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A1I8FSZ9; -.
DR WBParaSite; maker-unitig_5295-snap-gene-0.2-mRNA-1; maker-unitig_5295-snap-gene-0.2-mRNA-1; maker-unitig_5295-snap-gene-0.2.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0016020; C: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 CDD; cd13952; 7tm_classB; 1.
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; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR12011:SF473; FI21270P1-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 549..570
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 576..595
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..601
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 75..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 82884 MW; 8D5BE815B68E3E89 CRC64;
ARLRCPSARR RRTVLNPLTG FCETLADLTG QECRQLAEPA AVSNRIALAP PGRSDLARLP
AGRPGRMLSG FAKSQPFRDL GPGAPVRQPC CRPTAGRRQR LRALSAPDSL ADSRPPCWTL
WPEFAAKACW PGPDAPESEA EFPQPRRGGE LRAGPAWTTS GGALQFGTGR ASAPPPVSVQ
RLRPDGTQLV RSADRSSTVK LRLLPDSAQG TAVSMVTTVL NLPHLTRRLG TAKQPVVSNV
IQATYAASSG QPAAEVLLLI PHSRISGQLR HRCLLAPEFL SPSGCRVAVE LSSPTVTACL
CRHLSSFAVT VLPGTAWLGV ETHRLWRLHS EPLRILTWIC LSVSIVCLLL TSITYIVVRM
QTPMADKSIA TLHRVHRSLC LALMLGQALF LAAFQPLDAT PIAACKLLSV LTLYALLCAF
CWLLCEGLMY THSLVKFWHY CLASGVAPLL IVLPTAALRP EQLIQTEADA SADSGGLLRP
SVCWLSGDHG VSFAFIGPAM AVCLVNLCLF AVIMRRLAGT RSDAADAVGG SAATSASLRL
SYLSRQMKVT ATLACLLGLT WLLGLMFLFA ETHLFIVAQY LFTLLNGLQG CFIFATQVCA
HKRVREDWEK FLIDGRRTPG SLRRLLEQRR NARLSAPGSG STPANKAQQG RLRQPLLPRA
GAAAAAADRR QQSSRRPQQL ESGFFDSRAF GDTRLDDQSL FDITHSQAEP ALRSPKSPLP
EPPPIDTLPA RCPGSRELLY DVTDTQASSE YLVPDCKPTE QLTKV
//