ID G3UE67_LOXAF Unreviewed; 536 AA.
AC G3UE67;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Frizzled-4 {ECO:0000256|ARBA:ARBA00018149};
GN Name=FZD4 {ECO:0000313|Ensembl:ENSLAFP00000026125.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000026125.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000026125.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000026125.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000026125.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000026125.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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 RefSeq; XP_003418598.1; XM_003418550.2.
DR AlphaFoldDB; G3UE67; -.
DR STRING; 9785.ENSLAFP00000026125; -.
DR Ensembl; ENSLAFT00000035606.1; ENSLAFP00000026125.1; ENSLAFG00000007383.3.
DR GeneID; 100675317; -.
DR KEGG; lav:100675317; -.
DR CTD; 8322; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000157141; -.
DR InParanoid; G3UE67; -.
DR OMA; HWGEFRA; -.
DR OrthoDB; 5483535at2759; -.
DR TreeFam; TF317907; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0019955; F:cytokine binding; IEA:Ensembl.
DR GO; GO:0004896; F:cytokine receptor activity; IEA:Ensembl.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:Ensembl.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0061301; P:cerebellum vasculature morphogenesis; IEA:Ensembl.
DR GO; GO:0045446; P:endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR GO; GO:0035426; P:extracellular matrix-cell signaling; IEA:Ensembl.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IEA:Ensembl.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0110135; P:Norrin signaling pathway; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; IEA:Ensembl.
DR GO; GO:0042701; P:progesterone secretion; IEA:Ensembl.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0061304; P:retinal blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; IEA:Ensembl.
DR CDD; cd15038; 7tmF_FZD4; 1.
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; IPR026551; FZD4_7TM.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR PANTHER; PTHR11309; FRIZZLED; 1.
DR PANTHER; PTHR11309:SF23; FRIZZLED-4; 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 Reference proteome {ECO:0000313|Proteomes:UP000007646};
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..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..536
FT /note="Frizzled-4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003456494"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..160
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 218..502
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DISULFID 44..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 52..98
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 89..127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 116..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 120..144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 536 AA; 59911 MW; 5A2744C55E181A9D CRC64;
MGRRGAGPRV PGEPGGVGLS LRLLLLLLLL GPARGFGDEE ERRCDPIRIT MCQNLGYNVT
KMPNLVGHEL QTDAELQLTT FTPLIQYGCS SQLQFFLCSV YVPMCTEKIN IPIGPCGGMC
LSVKRRCEPV LKEFGFAWPE SLNCSKFPPQ NDHNHMCMEG PGDEEVPLPH KTPIQPGEEC
HSVGTNSDQY IWVKRSLNCV LKCGYDAGLY SRSAKEFTDI WMAVWASLCF ISTAFTVLTF
LIDSSRFSYP ERPIIFLSMC YNIYSIAYIV RLTVGRERIS CDFEEAAEPV LIQEGLKNTG
CAIIFLLMYF FGMASSIWWV ILTLTWFLAA GLKWGHEAIE MHSSYFHIAA WAIPAVKTIV
ILIMRLVDAD GLTGLCYVGN QNLDALTGFV VAPLFTYLVI GTLFIAAGLV ALFKIRSNLQ
KDGTKTDKLE RLMVKIGVFS VLYTVPATCV IACYFYEISN WALFRYSADD SNMAVEMLKI
FMSLLVGITS GMWIWSAKTF HTWQKCSNRL VNSGKVKREK RGSGWVKPGK GNETVV
//
