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Database: UniProt
Entry: D2HB98_AILME
LinkDB: D2HB98_AILME
Original site: D2HB98_AILME 
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}.
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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
//
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