ID A0A3Q0S081_AMPCI Unreviewed; 692 AA.
AC A0A3Q0S081;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Frizzled class receptor 3a {ECO:0000313|Ensembl:ENSACIP00000016127.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000016127.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000016127.1}
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 Fz/Smo family.
CC {ECO:0000256|ARBA:ARBA00008077}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR AlphaFoldDB; A0A3Q0S081; -.
DR STRING; 61819.ENSACIP00000016127; -.
DR Ensembl; ENSACIT00000016553.1; ENSACIP00000016127.1; ENSACIG00000012531.1.
DR GeneTree; ENSGT00940000156491; -.
DR OMA; NIMNHYD; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071679; P:commissural neuron axon guidance; IEA:Ensembl.
DR GO; GO:0021754; P:facial nucleus development; IEA:Ensembl.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR PANTHER; PTHR11309; FRIZZLED; 1.
DR PANTHER; PTHR11309:SF144; FRIZZLED-3 ISOFORM X1; 1.
DR Pfam; PF01534; Frizzled; 1.
DR Pfam; PF01392; Fz; 1.
DR PRINTS; PR00489; FRIZZLED.
DR SMART; SM00063; FRI; 1.
DR SMART; SM01330; Frizzled; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..692
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018704586"
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..140
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 202..509
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 547..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 32..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 40..86
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 107..131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 692 AA; 77827 MW; B60DF638FB01FA2D CRC64;
MDLLWVLSVS MLTACVAIPM DTVAGSHSLF TCEPITLRMC QGLPYNATFM PNSLNHYDQQ
TAALAMEPFH PMVNLQCSAE LRMFLCALYA PVCTEYGRIT LPCRRLCLQA KSDCYKLMDM
FGVSWPEEMD CNRFPDCDEP YPRPVDLLSS SDTTESPISV QRDYGFWCPR ELKINPELGY
SFMGVRDCSP PCPNMYFTRE ELTFARYFIG VVSIVCLSAT LFTFLTFLID VSRFRYPERP
IIFYAVCYMM VSLVFFLGFL LEDKVSCNAA SPGRFRASTV TQGSHNKACT LLFMVLYFFT
MAGSVWWVIL TITWFLAAVP KWGSEAIEKK ALLFHACAWG IPGVLTVTLL AMNKIEGDGI
SGVCFVGLYN LTALRWFLLA PLGLDVVVGV VLLLAGIAAL NRVRMEIPLE KENQEKLVKF
MIRIGVFSVL YLVPLLTVLA CYFYESSYRP VWETTWVQEK CRDYHIPCPY QVEQTSHPDL
VLFLIKYLMM LIVGIPSVFW VASKKTCFEW ASFFHGKRRK DGMVNESRQV LQEPDFTQLL
LRDPNTPIVR KSRGTSTQGT STHASSTHLA ILDEPPSAST SRAGSVRSAR SKMSSYHGSL
HRSRDGRYTA SSFRAADDRL PYGSMPRLND QSQSRHCSTN RLDGLSRHGS TQRLESQSRH
SSIRDLSSGA TAVLGVPGNG IHRVLEEDGA TA
//
