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Database: UniProt
Entry: F4WXL7_ACREC
LinkDB: F4WXL7_ACREC
Original site: F4WXL7_ACREC 
ID   F4WXL7_ACREC            Unreviewed;       653 AA.
AC   F4WXL7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Frizzled-4 {ECO:0000256|ARBA:ARBA00018149};
GN   ORFNames=G5I_10702 {ECO:0000313|EMBL:EGI61087.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI61087.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) 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 Fz/Smo family.
CC       {ECO:0000256|ARBA:ARBA00008077}.
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DR   EMBL; GL888425; EGI61087.1; -; Genomic_DNA.
DR   RefSeq; XP_011061693.1; XM_011063391.1.
DR   AlphaFoldDB; F4WXL7; -.
DR   STRING; 103372.F4WXL7; -.
DR   EnsemblMetazoa; XM_011063391.1; XP_011061693.1; LOC105150367.
DR   GeneID; 105150367; -.
DR   KEGG; aec:105150367; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   InParanoid; F4WXL7; -.
DR   OrthoDB; 3058928at2759; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd07448; CRD_FZ4; 1.
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; IPR041765; FZ4_CRD.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF99; FRIZZLED-4; 1.
DR   Pfam; PF01534; Frizzled; 2.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00090}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..653
FT                   /note="Frizzled-4"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003319061"
FT   TRANSMEM        198..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        404..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        542..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..138
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          196..509
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          623..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..646
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        22..83
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        30..76
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        67..105
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        94..135
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        98..122
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   653 AA;  72021 MW;  907012AA311DC48B CRC64;
     MRWILLPLLT LIRAIWCAHG ACEPIRIEMC RGLGYNVTVM PNLVGHEIQG DADFTLQTFS
     PLIQYGCSAQ LHLFLCSVYA PMCTEKVPAP IGPCRGLCEQ VRARCYPVLQ GFGFPWPAAL
     NCSKFPPENN HQHMCMEGPG EPGPANPIQA VSTSNGPWGC SWYAKSGLYI FLNRSGRCAA
     ACDADILWSQ KDKKLAEAWM AVFVTVSLVS VAIAILTLLK PRKRPILTSP AERAIVFLTI
     CHAAVAIGYV IRLAAGRLNV ACTPAIQLHP QEQAVLAQQQ QQLQQQQQQY LTQDGLANPY
     CAVVFLLLYY FGNAAIVWWV VICAWWCIMA RKWTRTAGNY KEDSFGLQQG FSTIATVAAW
     SLPAAHTIAV LVTRDVDADE LTASCFVGQQ NAHSLLVLVL APQFVYLSFG ATFLLIGLAT
     LVLPRRPTVT PTSTSMSTTS SSSSTAAAAA AAAVLTALTA SHANPLRSQR SEISGKSSPG
     EIHRRQKQLL TRVGIFGCLY AILIICLAST TFYEWWGRET WLRAPEPSTA PRVPARPLLQ
     VFILRLVVTL GAGVMAAAWI WWPEVPNACR KLPHCKQPPH KCHPVPLVHT CQYNAANPIP
     HQIHHLAHLT PPQHPLLHQH STLTNSQLPH RNHKNKKHRK HRKHYHSGSE TQV
//
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