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WDR11_DANRE
ID   WDR11_DANRE             Reviewed;        1239 AA.
AC   F1QEB7; F1QHQ4;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=WD repeat-containing protein 11 {ECO:0000305};
GN   Name=wdr11;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=20887964; DOI=10.1016/j.ajhg.2010.08.018;
RA   Kim H.G., Ahn J.W., Kurth I., Ullmann R., Kim H.T., Kulharya A., Ha K.S.,
RA   Itokawa Y., Meliciani I., Wenzel W., Lee D., Rosenberger G., Ozata M.,
RA   Bick D.P., Sherins R.J., Nagase T., Tekin M., Kim S.H., Kim C.H.,
RA   Ropers H.H., Gusella J.F., Kalscheuer V., Choi C.Y., Layman L.C.;
RT   "WDR11, a WD protein that interacts with transcription factor EMX1, is
RT   mutated in idiopathic hypogonadotropic hypogonadism and Kallmann
RT   syndrome.";
RL   Am. J. Hum. Genet. 87:465-479(2010).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=29263200; DOI=10.15252/embr.201744632;
RA   Kim Y.J., Osborn D.P., Lee J.Y., Araki M., Araki K., Mohun T.,
RA   Kaensaekoski J., Brandstack N., Kim H.T., Miralles F., Kim C.H.,
RA   Brown N.A., Kim H.G., Martinez-Barbera J.P., Ataliotis P., Raivio T.,
RA   Layman L.C., Kim S.H.;
RT   "WDR11-mediated Hedgehog signalling defects underlie a new ciliopathy
RT   related to Kallmann syndrome.";
RL   EMBO Rep. 19:269-289(2018).
CC   -!- FUNCTION: Involved in the Hedgehog (Hh) signaling pathway, is essential
CC       for normal ciliogenesis (PubMed:29263200). Regulates the proteolytic
CC       processing of gli3 and cooperates with the transcription factor emx1 in
CC       the induction of downstream Hh pathway gene expression and
CC       gonadotropin-releasing hormone production. WDR11 complex facilitates
CC       the tethering of Adaptor protein-1 complex (AP-1)-derived vesicles.
CC       {ECO:0000250|UniProtKB:Q9BZH6, ECO:0000269|PubMed:29263200}.
CC   -!- SUBUNIT: Component of the complex WDR11.
CC       {ECO:0000250|UniProtKB:Q9BZH6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250|UniProtKB:Q9BZH6}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9BZH6}. Nucleus {ECO:0000250|UniProtKB:Q9BZH6}.
CC       Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29263200}.
CC       Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9BZH6}. Golgi apparatus,
CC       trans-Golgi network {ECO:0000250|UniProtKB:Q9BZH6}. Note=Shuttles from
CC       the cilium to the nucleus in response to Hh signaling. Might be
CC       shuttling between the nucleus and the cytoplasm.
CC       {ECO:0000250|UniProtKB:Q9BZH6}.
CC   -!- DEVELOPMENTAL STAGE: Expressed ubiquitously at 24 hpf.
CC       {ECO:0000269|PubMed:20887964}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown causes microphtalmia,
CC       microcephaly, melanocyte disorganization, curved body axis, motility
CC       defects and narrow trunk. Morphants also exhibit aberrant head
CC       cartilage formation and cranial-facial dysmorphology.
CC       {ECO:0000269|PubMed:29263200}.
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DR   EMBL; BX571701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_687231.3; XM_682139.7.
DR   AlphaFoldDB; F1QEB7; -.
DR   STRING; 7955.ENSDARP00000102548; -.
DR   PaxDb; F1QEB7; -.
DR   PRIDE; F1QEB7; -.
DR   Ensembl; ENSDART00000114328; ENSDARP00000102548; ENSDARG00000075245.
DR   Ensembl; ENSDART00000136977; ENSDARP00000123378; ENSDARG00000075245.
DR   GeneID; 558865; -.
DR   KEGG; dre:558865; -.
DR   CTD; 55717; -.
DR   ZFIN; ZDB-GENE-081107-28; wdr11.
DR   eggNOG; KOG1912; Eukaryota.
DR   GeneTree; ENSGT00390000004068; -.
DR   InParanoid; F1QEB7; -.
DR   OMA; NAIDWND; -.
DR   OrthoDB; 617629at2759; -.
DR   PhylomeDB; F1QEB7; -.
DR   TreeFam; TF314830; -.
DR   Reactome; R-DRE-9013407; RHOH GTPase cycle.
DR   PRO; PR:F1QEB7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000075245; Expressed in brain and 24 other tissues.
DR   GO; GO:0005930; C:axoneme; IDA:ZFIN.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR   GO; GO:0060322; P:head development; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0035264; P:multicellular organism growth; ISS:UniProtKB.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:ZFIN.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0099041; P:vesicle tethering to Golgi; ISS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR039694; WDR11.
DR   PANTHER; PTHR14593; PTHR14593; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
PE   2: Evidence at transcript level;
KW   Cell projection; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Golgi apparatus; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   WD repeat.
FT   CHAIN           1..1239
FT                   /note="WD repeat-containing protein 11"
FT                   /id="PRO_0000445435"
FT   REPEAT          63..112
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          115..158
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          358..398
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          476..515
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          571..610
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          713..750
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          752..792
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          798..836
FT                   /note="WD 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          898..944
FT                   /note="WD 9"
FT                   /evidence="ECO:0000255"
FT   REGION          1213..1239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1214..1239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1239 AA;  137139 MW;  3D1799770FB056ED CRC64;
     MASTMIPYTV NIKLAARTLT GTLNLQNKTA VDWGWQGLIA QGCHSSILII DPNTAQTIQV
     LERHKANVVK VKWSRENYHH SLSSPYSLRL ASADAAGKII VWDVVSGMAH CEIQEHSKPI
     QDMDWLWAQD ASRDLLLAVH PPNYIVLWNG DTGTKLWKKS YAENILSFSF DPFEPSNLAL
     LTSEGIVFIT DFSHSKPPGS GGKKVYIASP HSSPAHSKPA AAQPTGAKKA LNKVKVLITN
     EKPTAEAVTL NDCLQLSYLP SKRNHMLLLY PREILILDLE LSQTVGVVAI ERSGVPFIQV
     IPCAQRDALY CLHENGCITL RVCRSTTPSP NETVTDPEQN SQELVYDLRS QCDAIRVTKT
     VRPYRVVICP VNENKAVLVV SDGRVMLWEL KAHASKSSSN LSSGLPPLYS AVNFCGTPLR
     QNQKCIPDLS LNSMIGHSLI PGVDSPRPLA DQKEVHLKFL LTGLLSGLPL PPFSLRMCPP
     LTTKNINHYQ PLLAVGTSNG SVLVYNLTSG LLHKELSVHS CEVRGIEWIS LTSFLSFATS
     VPNNLGLVRN ELQHVDLRTG RCFAFRGERG NDEPAIEMIK VSHLKQYLVV VFRDKPLELW
     DVRTGTLLRE MAKNFPTVTA LEWSPSHNLK SLKKKQLAAR EAMARQTTLA DAEQSSVESS
     VISLLQDAES KSESSQGISA REHFVFTDTD GQVYHITVEG NTVKDGARIP PDGSMGSIAC
     IAWKGDTLVL GDVDGNLNFW DLKARLSRGV PTHRGWVKKI RFAPGKGNQK LLVMYTDGAE
     VWDTKEVQMV SSIRVGRNVN YRILDIDWCT SDKVVLASDD GCVRVLEMAM KSASYRMDEQ
     DLTDPVWCPY LLLPRAALTL KAFLLLQPWM DTFTMDITQV DYKEKDEIKG LIQEQLNSLS
     NDIKSVLQDP NLSLLQRCLL VSRLFGDESD LQFWTVASHY IQAFAQSAQS NESVPEGQAA
     ASHLDICHDI LCESSFFQGF QLERVRLQEV KRSSYEHTKK CADQLLLLGQ TDRAVQLLLE
     TSADNSSYYC DSLKACLVTT ITSSGPSQST IKLVATNMIA NGKLAEGVQL LCLIDKAADA
     CRYLQTYGEW TRAAWLAKVR LNAAEGSDVL KRWAEHLCSP QVNQKSKAML VLLSLGCFQK
     VGEMLHSMRY FDRAALFIEA CLKYGVMETN DDINKLVGAA FVDYAKLLRS IGLKQGAVHW
     ASRAGEAGKQ LLEDLSQTEG TGTESSPADD TDNSLVNIE
 
 
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