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SART3_DANRE
ID   SART3_DANRE             Reviewed;         951 AA.
AC   B3DJT0;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Squamous cell carcinoma antigen recognized by T-cells 3 {ECO:0000305};
DE            Short=SART-3;
GN   Name=sart3 {ECO:0000312|ZFIN:ZDB-GENE-040724-10}; Synonyms=egy;
GN   ORFNames=si:ch211-191d15.4, wu:fc51h03;
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 {ECO:0000312|EMBL:AAI63594.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17416673; DOI=10.1073/pnas.0701919104;
RA   Trede N.S., Medenbach J., Damianov A., Hung L.H., Weber G.J., Paw B.H.,
RA   Zhou Y., Hersey C., Zapata A., Keefe M., Barut B.A., Stuart A.B., Katz T.,
RA   Amemiya C.T., Zon L.I., Bindereif A.;
RT   "Network of coregulated spliceosome components revealed by zebrafish mutant
RT   in recycling factor p110.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:6608-6613(2007).
CC   -!- FUNCTION: U6 snRNP-binding protein that functions as a recycling factor
CC       of the splicing machinery. Promotes the initial reassembly of U4 and U6
CC       snRNPs following their ejection from the spliceosome during its
CC       maturation (PubMed:17416673). May also function as a substrate
CC       targeting factor for deubiquitinases and mediate the deubiquitination
CC       of components of the spliceosome and histones (By similarity).
CC       {ECO:0000250|UniProtKB:Q15020, ECO:0000269|PubMed:17416673}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q15020}. Nucleus, Cajal body
CC       {ECO:0000250|UniProtKB:Q15020}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q15020}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q15020}.
CC   -!- DISRUPTION PHENOTYPE: The egy mutant embryos that lack detectable sart3
CC       expression display microcephaly, microphthalmia and die by 7 to 8 dpf.
CC       Pharyngeal arch formation is defective resulting in a thymus devoid of
CC       lymphocytes and exocrine pancreas development is also impaired.
CC       {ECO:0000269|PubMed:17416673}.
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DR   EMBL; AL845326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC163594; AAI63594.1; -; mRNA.
DR   RefSeq; XP_005165211.1; XM_005165154.3.
DR   RefSeq; XP_017211593.1; XM_017356104.1.
DR   RefSeq; XP_017211594.1; XM_017356105.1.
DR   AlphaFoldDB; B3DJT0; -.
DR   SMR; B3DJT0; -.
DR   STRING; 7955.ENSDARP00000004923; -.
DR   PaxDb; B3DJT0; -.
DR   PeptideAtlas; B3DJT0; -.
DR   Ensembl; ENSDART00000124545; ENSDARP00000106223; ENSDARG00000008032.
DR   GeneID; 558581; -.
DR   CTD; 9733; -.
DR   ZFIN; ZDB-GENE-040724-10; sart3.
DR   eggNOG; KOG0128; Eukaryota.
DR   GeneTree; ENSGT00900000141107; -.
DR   HOGENOM; CLU_007172_0_0_1; -.
DR   InParanoid; B3DJT0; -.
DR   PhylomeDB; B3DJT0; -.
DR   TreeFam; TF317554; -.
DR   ChiTaRS; sart3; zebrafish.
DR   PRO; PR:B3DJT0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000008032; Expressed in presomitic mesoderm and 28 other tissues.
DR   ExpressionAtlas; B3DJT0; baseline.
DR   GO; GO:0061574; C:ASAP complex; IBA:GO_Central.
DR   GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR   GO; GO:0031017; P:exocrine pancreas development; IMP:ZFIN.
DR   GO; GO:0030098; P:lymphocyte differentiation; IMP:ZFIN.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR   GO; GO:1903586; P:positive regulation of histone deubiquitination; ISS:UniProtKB.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IMP:ZFIN.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; IMP:UniProtKB.
DR   GO; GO:0048538; P:thymus development; IMP:ZFIN.
DR   CDD; cd12391; RRM1_SART3; 1.
DR   CDD; cd12392; RRM2_SART3; 1.
DR   Gene3D; 1.25.40.10; -; 2.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034217; SART3_RRM1.
DR   InterPro; IPR034218; SART3_RRM2.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00386; HAT; 7.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..951
FT                   /note="Squamous cell carcinoma antigen recognized by T-
FT                   cells 3"
FT                   /id="PRO_0000431579"
FT   REPEAT          88..120
FT                   /note="HAT 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          126..157
FT                   /note="HAT 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          163..199
FT                   /note="HAT 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          222..255
FT                   /note="HAT 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          304..336
FT                   /note="HAT 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          339..371
FT                   /note="HAT 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          374..410
FT                   /note="HAT 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          467..500
FT                   /note="HAT 8"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          688..766
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          785..862
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..941
FT                   /note="Necessary and sufficient for U6 snRNA binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q15020"
FT   REGION          567..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          905..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          533..593
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..54
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   951 AA;  109735 MW;  DFBD6B293A95B156 CRC64;
     MAATGNEEQT LLPDIEEEAE GMEREMESED DEEEGMGVEH SEEEDEEDTS EDERENEAEI
     QRLEEQLSIN AFDYNCHVDL IKLLRQEGKL HRLRKARQKM SELFPLTEEI WLDWLKDEIR
     ITEDESDREK VYELFERAIK DYVCPEIWLE YVQYSIGGMG AQGGIERVRS IFERALTAVG
     LHMTKGASIW EAYREFEIVI LSTVQPPPGT VPSQEQQELL SAQLERIHTL FRRQLAVPLM
     DMEGTYAEYS DWADDGVPET VTHQYRRALQ QMEKGKPYEE ALLVSEPPKL AEYQSYIDFE
     IKEGDPARVQ IIFERALAEN CLVPDLWIKY TTYLDRQLKI KDLVLSAHER AVRNCPWTMG
     LWKSYLLALE RHGADHQTVK DVFEKALNAG FIQATDYVEI WQSYLDYLRR RVDFSKEWSR
     ELDELRAAFS RSLEYLKQDV EERFSESGDL SCTLMQIWAR IEALHCKNMQ KARELWDSIM
     TKGNAKYANM WLEYYNLERS YGDAAHCRKA LHRAVQCTSD YPEHVCDVLL NFERVEGSLE
     DWDAAVQKTE TKLNRVCEQR ARVAEKEALH ARQEEEKAEQ RRKVKADKKA QKKGQKANRT
     GDKRKAEDDD EEEWGEEAEL PSKRLRGEDD FDSTVTEELM ETESGLFGRR APPARKTEPP
     GFRKNQQGAP EPQRQPHDMP KEQRKDENCV FVSNLTFNME DPEGKLRTLF QGCGTIQQVR
     PVFTAKGTFR GYCYVQFEDR LAVPEALKMD RQEVDGRPMY VSPCVDKNKN PDFKVFKYKT
     SMEKHKIFIS GLPYSATKET LEDLCKEHGT IRAIRIVTNR SGKSKGLAYV EFEDEAQASQ
     AVLKMDGTML ENFTLSVAIS NPPGRRMKDE AAPSRFLGAA MPRQLQGARG KGRTQISLLP
     RSLYRQSTPD AKAENGTISA PHATVTDGET SLDTQTKSLS NEDFARMLLK K
 
 
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