ID A7MB15_BOVIN Unreviewed; 645 AA.
AC A7MB15;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Frizzled-1 {ECO:0000256|ARBA:ARBA00018150};
GN Name=FZD1 {ECO:0000313|EMBL:AAI51284.1,
GN ECO:0000313|Ensembl:ENSBTAP00000002720.4,
GN ECO:0000313|VGNC:VGNC:29165};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI51284.1};
RN [1] {ECO:0000313|EMBL:AAI51284.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI51284.1};
RC TISSUE=Fetal skin {ECO:0000313|EMBL:AAI51284.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000002720.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000002720.4,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000002720.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000002720.4};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR EMBL; BC151283; AAI51284.1; -; mRNA.
DR RefSeq; NP_001094518.1; NM_001101048.1.
DR STRING; 9913.ENSBTAP00000002720; -.
DR PaxDb; 9913-ENSBTAP00000002720; -.
DR Ensembl; ENSBTAT00000002720.5; ENSBTAP00000002720.4; ENSBTAG00000002107.5.
DR GeneID; 445417; -.
DR KEGG; bta:445417; -.
DR CTD; 8321; -.
DR VEuPathDB; HostDB:ENSBTAG00000002107; -.
DR VGNC; VGNC:29165; FZD1.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000162584; -.
DR HOGENOM; CLU_007873_2_1_1; -.
DR OMA; GQENCGA; -.
DR OrthoDB; 5483535at2759; -.
DR TreeFam; TF317907; -.
DR Reactome; R-BTA-4086400; PCP/CE pathway.
DR Reactome; R-BTA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-BTA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000002107; Expressed in uterine cervix and 100 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0035425; P:autocrine signaling; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0044338; P:canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation; IEA:Ensembl.
DR GO; GO:0044339; P:canonical Wnt signaling pathway involved in osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR CDD; cd15247; 7tmF_FZD1; 1.
DR CDD; cd07465; CRD_FZ1; 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; IPR017981; GPCR_2-like_7TM.
DR PANTHER; PTHR11309; FRIZZLED; 1.
DR PANTHER; PTHR11309:SF81; FRIZZLED-1; 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 2: Evidence at transcript level;
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 G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 109..228
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 316..627
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 114..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 122..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 189..213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 645 AA; 70855 MW; BB6AF0246F4C88B9 CRC64;
MAEEEAPKKS RAAGGGGGGG SWELCAGALR TVPAAEGSGD AGSRRRPPAD SRRLARRLLL
LLWLLEAPLL LGVRAQAAGQ GPGPGQQPPP PQQQQSGQQY NGERGISIPD HGYCQPISIP
LCTDIAYNQT IMPNLLGHTN QEDAGLEVHQ FYPLVKVQCS AELKFFLCSM YAPVCTVLEQ
ALPPCRSLCE RARQGCEALM NKFGFQWPDT LKCEKFPVHG AGELCVGQNT SDKGTPTPSL
LPEFWTSNPQ HGGGGHRGGG FAGGAGASER GKFSCPRALK VPSYLNYHFL GEKDCGAPCE
PTKVYGLMYF GPEELRFSRT WIGIWSVLCC ASTLFTVLTY LVDMRRFSYP ERPIIFLSGC
YTAVAVAYIA GFLLEDRVVC NDKFAEDGAR TVAQGTKKEG CTILFMMLYF FSMASSIWWV
ILSLTWFLAA GMKWGHEAIE ANSQYFHLAA WAVPAIKTIT ILALGQVDGD VLSGVCFVGL
NNVDALRGFV LAPLFVYLFI GTSFLLAGFV SLFRIRTIMK HDGTKTEKLE KLMVRIGVFS
VLYTVPATIV IACYFYEQAF RDQWERSWVA QSCKSYAIPC PHLQAGGAPP HPPMSPDFTV
FMIKYLMTLI VGITSGFWIW SGKTLNSWRK FYTRLTNSKQ GETTV
//
