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FZD9_HUMAN
ID   FZD9_HUMAN              Reviewed;         591 AA.
AC   O00144;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Frizzled-9;
DE            Short=Fz-9;
DE            Short=hFz9;
DE   AltName: Full=FzE6;
DE   AltName: CD_antigen=CD349;
DE   Flags: Precursor;
GN   Name=FZD9; Synonyms=FZD3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=9147651; DOI=10.1093/hmg/6.3.465;
RA   Wang Y.-K., Samos H.C., Peoples R., Perez-Jurado L.A., Nusse R.,
RA   Francke U.;
RT   "A novel human homologue of the Drosophila frizzled wnt receptor gene binds
RT   wingless protein and is in the Williams syndrome deletion at 7q11.23.";
RL   Hum. Mol. Genet. 6:465-472(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 269-329.
RC   TISSUE=Esophageal carcinoma;
RX   PubMed=9707618; DOI=10.1073/pnas.95.17.10164;
RA   Tanaka S., Akiyoshi T., Mori M., Wands J.R., Sugimachi K.;
RT   "A novel frizzled gene identified in human esophageal carcinoma mediates
RT   APC/beta-catenin signals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=27509850; DOI=10.1038/nature19067;
RA   Chailangkarn T., Trujillo C.A., Freitas B.C., Hrvoj-Mihic B., Herai R.H.,
RA   Yu D.X., Brown T.T., Marchetto M.C., Bardy C., McHenry L., Stefanacci L.,
RA   Jaervinen A., Searcy Y.M., DeWitt M., Wong W., Lai P., Ard M.C.,
RA   Hanson K.L., Romero S., Jacobs B., Dale A.M., Dai L., Korenberg J.R.,
RA   Gage F.H., Bellugi U., Halgren E., Semendeferi K., Muotri A.R.;
RT   "A human neurodevelopmental model for Williams syndrome.";
RL   Nature 536:338-343(2016).
CC   -!- FUNCTION: Receptor for WNT2 that is coupled to the beta-catenin
CC       canonical signaling pathway, which leads to the activation of
CC       disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation
CC       of beta-catenin and activation of Wnt target genes (By similarity).
CC       Plays a role in neuromuscular junction (NMJ) assembly by negatively
CC       regulating the clustering of acetylcholine receptors (AChR) through the
CC       beta-catenin canonical signaling pathway (By similarity). May play a
CC       role in neural progenitor cells (NPCs) viability through the beta-
CC       catenin canonical signaling pathway by negatively regulating cell cycle
CC       arrest leading to inhibition of neuron apoptotic process
CC       (PubMed:27509850). During hippocampal development, regulates neuroblast
CC       proliferation and apoptotic cell death. Controls bone formation through
CC       non canonical Wnt signaling mediated via ISG15. Positively regulates
CC       bone regeneration through non canonical Wnt signaling (By similarity).
CC       {ECO:0000250|UniProtKB:Q8K4C8, ECO:0000250|UniProtKB:Q9R216,
CC       ECO:0000269|PubMed:27509850}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9R216};
CC       Multi-pass membrane protein {ECO:0000255}. Note=Relocalizes DVL1 to the
CC       cell membrane leading to phosphorylation of DVL1 and AXIN1
CC       relocalization to the cell membrane. {ECO:0000250|UniProtKB:Q8K4C8}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in adult and fetal brain,
CC       testis, eye, skeletal muscle and kidney. Moderately expressed in
CC       pancreas, thyroid, adrenal cortex, small intestine and stomach.
CC       Detected in fetal liver and kidney. Expressed in neural progenitor
CC       cells (PubMed:27509850). {ECO:0000269|PubMed:27509850}.
CC   -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl
CC       (Disheveled) family members and is involved in the activation of the
CC       Wnt/beta-catenin signaling pathway. {ECO:0000250}.
CC   -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by ZNRF3, leading to its degradation by the
CC       proteasome. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Authors show that FZD9 is responsible for the cellular
CC       phenotype found in neural progenitor cells (NPCs) derived from Williams
CC       syndrome patients namely increased apoptosis of neural progenitor cells
CC       (NPCs). {ECO:0000269|PubMed:27509850}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Has been first described as FZD3 in literature. {ECO:0000305}.
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DR   EMBL; U82169; AAC51174.1; -; mRNA.
DR   EMBL; AC005049; AAQ93359.1; -; Genomic_DNA.
DR   CCDS; CCDS5548.1; -.
DR   RefSeq; NP_003499.1; NM_003508.2.
DR   AlphaFoldDB; O00144; -.
DR   SMR; O00144; -.
DR   BioGRID; 113922; 4.
DR   IntAct; O00144; 1.
DR   STRING; 9606.ENSP00000345785; -.
DR   ChEMBL; CHEMBL4523116; -.
DR   GlyGen; O00144; 2 sites.
DR   iPTMnet; O00144; -.
DR   PhosphoSitePlus; O00144; -.
DR   BioMuta; FZD9; -.
DR   jPOST; O00144; -.
DR   MassIVE; O00144; -.
DR   PaxDb; O00144; -.
DR   PeptideAtlas; O00144; -.
DR   PRIDE; O00144; -.
DR   ABCD; O00144; 1 sequenced antibody.
DR   Antibodypedia; 14305; 546 antibodies from 39 providers.
DR   DNASU; 8326; -.
DR   Ensembl; ENST00000344575.5; ENSP00000345785.3; ENSG00000188763.5.
DR   GeneID; 8326; -.
DR   KEGG; hsa:8326; -.
DR   MANE-Select; ENST00000344575.5; ENSP00000345785.3; NM_003508.3; NP_003499.1.
DR   UCSC; uc003tyb.4; human.
DR   CTD; 8326; -.
DR   DisGeNET; 8326; -.
DR   GeneCards; FZD9; -.
DR   HGNC; HGNC:4047; FZD9.
DR   HPA; ENSG00000188763; Tissue enhanced (brain, skeletal muscle, testis).
DR   MIM; 601766; gene.
DR   neXtProt; NX_O00144; -.
DR   OpenTargets; ENSG00000188763; -.
DR   PharmGKB; PA28464; -.
DR   VEuPathDB; HostDB:ENSG00000188763; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   GeneTree; ENSGT00940000161226; -.
DR   HOGENOM; CLU_007873_2_1_1; -.
DR   InParanoid; O00144; -.
DR   OMA; CEGIGYN; -.
DR   OrthoDB; 509772at2759; -.
DR   PhylomeDB; O00144; -.
DR   TreeFam; TF317907; -.
DR   PathwayCommons; O00144; -.
DR   Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR   SignaLink; O00144; -.
DR   SIGNOR; O00144; -.
DR   BioGRID-ORCS; 8326; 10 hits in 1072 CRISPR screens.
DR   GeneWiki; FZD9; -.
DR   GenomeRNAi; 8326; -.
DR   Pharos; O00144; Tbio.
DR   PRO; PR:O00144; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; O00144; protein.
DR   Bgee; ENSG00000188763; Expressed in cartilage tissue and 94 other tissues.
DR   Genevisible; O00144; HS.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0031527; C:filopodium membrane; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0042813; F:Wnt receptor activity; ISS:UniProtKB.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR   GO; GO:1990523; P:bone regeneration; ISS:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0051902; P:negative regulation of mitochondrial depolarization; ISS:UniProtKB.
DR   GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060546; P:negative regulation of necroptotic process; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR   GO; GO:1904394; P:negative regulation of skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0001503; P:ossification; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:UniProtKB.
DR   GO; GO:0099173; P:postsynapse organization; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:UniProtKB.
DR   Gene3D; 1.10.2000.10; -; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like.
DR   PANTHER; PTHR11309; PTHR11309; 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; SSF63501; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Developmental protein; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW   Ubl conjugation; Wnt signaling pathway.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..591
FT                   /note="Frizzled-9"
FT                   /id="PRO_0000013003"
FT   TOPO_DOM        23..229
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..266
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..315
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..400
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..447
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        469..508
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        509..529
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        530..591
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          34..155
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   REGION          58..172
FT                   /note="Required for Wnt-activated receptor activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K4C8"
FT   REGION          554..591
FT                   /note="Required for CTNNB1 accumulation and TCF
FT                   transcription factor activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K4C8"
FT   MOTIF           532..537
FT                   /note="Lys-Thr-X-X-X-Trp motif, mediates interaction with
FT                   the PDZ domain of Dvl family members"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        47..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        84..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        111..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        115..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   591 AA;  64466 MW;  0D3784A78DF0B2E5 CRC64;
     MAVAPLRGAL LLWQLLAAGG AALEIGRFDP ERGRGAAPCQ AVEIPMCRGI GYNLTRMPNL
     LGHTSQGEAA AELAEFAPLV QYGCHSHLRF FLCSLYAPMC TDQVSTPIPA CRPMCEQARL
     RCAPIMEQFN FGWPDSLDCA RLPTRNDPHA LCMEAPENAT AGPAEPHKGL GMLPVAPRPA
     RPPGDLGPGA GGSGTCENPE KFQYVEKSRS CAPRCGPGVE VFWSRRDKDF ALVWMAVWSA
     LCFFSTAFTV LTFLLEPHRF QYPERPIIFL SMCYNVYSLA FLIRAVAGAQ SVACDQEAGA
     LYVIQEGLEN TGCTLVFLLL YYFGMASSLW WVVLTLTWFL AAGKKWGHEA IEAHGSYFHM
     AAWGLPALKT IVILTLRKVA GDELTGLCYV ASTDAAALTG FVLVPLSGYL VLGSSFLLTG
     FVALFHIRKI MKTGGTNTEK LEKLMVKIGV FSILYTVPAT CVIVCYVYER LNMDFWRLRA
     TEQPCAAAAG PGGRRDCSLP GGSVPTVAVF MLKIFMSLVV GITSGVWVWS SKTFQTWQSL
     CYRKIAAGRA RAKACRAPGS YGRGTHCHYK APTVVLHMTK TDPSLENPTH L
 
 
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