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}.
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; 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
//