ID D2HB98_AILME Unreviewed; 525 AA.
AC D2HB98;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFB14934.1};
DE Flags: Fragment;
GN ORFNames=PANDA_007781 {ECO:0000313|EMBL:EFB14934.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB14934.1};
RN [1] {ECO:0000313|EMBL:EFB14934.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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}.
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; GL192652; EFB14934.1; -; Genomic_DNA.
DR AlphaFoldDB; D2HB98; -.
DR STRING; 9646.ENSAMEP00000020107; -.
DR eggNOG; KOG3577; Eukaryota.
DR HOGENOM; CLU_007873_2_1_1; -.
DR InParanoid; D2HB98; -.
DR OMA; CPSHFAP; -.
DR TreeFam; TF317907; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl.
DR GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate 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:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; IEA:Ensembl.
DR GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0042666; P:negative regulation of ectodermal cell fate specification; IEA:Ensembl.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR CDD; cd15246; 7tmF_FZD7; 1.
DR CDD; cd07458; CRD_FZ1_like; 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:SF31; FRIZZLED-7; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 206..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 422..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 478..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..114
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 204..507
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DISULFID 8..54
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 75..99
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFB14934.1"
FT NON_TER 525
FT /evidence="ECO:0000313|EMBL:EFB14934.1"
SQ SEQUENCE 525 AA; 58858 MW; 2F42F6FBE91A3008 CRC64;
ETISIPLCTD IAYNQTILPN LLGHTNQEDA GLEVHQFYPL VKVQCSPELR FFLCSMYAPV
CTVLDQAIPP CRSLCERARQ GCEALMNKFG FQWPERLRCE NFPVHGAGEI CVGQNTSDGS
GGPGGGPTAY PTAPYMPDLP FTALPPGAAD GRGRAAFPFS CPRQLKVPPY LGYRFLGERD
CGAPCEPGRA NGLMYFKEEE RRFARLWVGV WSVLCCASTL FTVLTYLVDM RRFSYPERPI
IFLSGCYFMV AVAHVAGFLL EDRAVCVERF SDDGYRTVAQ GTKKEGCTIL FMVLYFFGMA
SSIWWVILSL TWFLAAGMKW GHEAIEANSQ YFHLAAWAVP AVKTITILAM GQVDGDLLSG
VCYVGLSSVD ALRGFVLAPL FVYLFIGTSF LLAGFVSLFR IRTIMKHDGT KTEKLEKLMV
RIGVFSVLYT VPATIVLACY FYEQAFREHW ERTWLLQTCK SYAVPCPPGH FPPMSPDFTV
FMIKYLMTMI VGITTGFWIW SGKTLQSWRR FYHRLSHSSK GETAV
//