UVSSA_DANRE
ID UVSSA_DANRE Reviewed; 721 AA.
AC E7EXT2; F1QTE8; Q6PGZ1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=UV-stimulated scaffold protein A;
GN Name=uvssa; ORFNames=si:dkey-18h19.2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-666.
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Factor involved in transcription-coupled nucleotide excision
CC repair (TC-NER) in response to UV damage. TC-NER allows RNA polymerase
CC II-blocking lesions to be rapidly removed from the transcribed strand
CC of active genes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250}. Note=Accumulates at UV
CC DNA damage sites. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UVSSA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56778.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BX119314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR382342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056778; AAH56778.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001333081.1; NM_001346152.1.
DR RefSeq; XP_017214592.1; XM_017359103.1.
DR AlphaFoldDB; E7EXT2; -.
DR SMR; E7EXT2; -.
DR STRING; 7955.ENSDARP00000109630; -.
DR PaxDb; E7EXT2; -.
DR PeptideAtlas; E7EXT2; -.
DR Ensembl; ENSDART00000160677; ENSDARP00000133113; ENSDARG00000100916.
DR Ensembl; ENSDART00000172666; ENSDARP00000132945; ENSDARG00000100916.
DR GeneID; 402864; -.
DR KEGG; dre:402864; -.
DR CTD; 57654; -.
DR ZFIN; ZDB-GENE-091204-111; uvssa.
DR eggNOG; KOG2374; Eukaryota.
DR GeneTree; ENSGT00940000164256; -.
DR HOGENOM; CLU_023577_0_0_1; -.
DR InParanoid; E7EXT2; -.
DR OMA; TSEHRFW; -.
DR OrthoDB; 996127at2759; -.
DR PhylomeDB; E7EXT2; -.
DR TreeFam; TF321660; -.
DR Reactome; R-DRE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DRE-6782135; Dual incision in TC-NER.
DR Reactome; R-DRE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR PRO; PR:E7EXT2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000100916; Expressed in mature ovarian follicle and 19 other tissues.
DR ExpressionAtlas; E7EXT2; baseline and differential.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
DR InterPro; IPR018610; UVSSA.
DR PANTHER; PTHR28670; PTHR28670; 1.
DR Pfam; PF09740; DUF2043; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; DNA damage; DNA repair; Reference proteome.
FT CHAIN 1..721
FT /note="UV-stimulated scaffold protein A"
FT /id="PRO_0000417996"
FT REGION 6..149
FT /note="VHS-like"
FT REGION 223..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..203
FT /evidence="ECO:0000255"
FT COMPBIAS 223..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 220
FT /note="A -> AV (in Ref. 2; AAH56778)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="T -> G (in Ref. 2; AAH56778)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="V -> A (in Ref. 2; AAH56778)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="R -> L (in Ref. 2; AAH56778)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="P -> L (in Ref. 2; AAH56778)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="S -> F (in Ref. 2; AAH56778)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="N -> K (in Ref. 2; AAH56778)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="I -> V (in Ref. 2; AAH56778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 83342 MW; D3AC124B91A1B71D CRC64;
MDQTMRDKLS QLVEELTTSG EPQLNQDKMK EVKKICRVSD SYIDHFYHLI MTQLNQEHAE
IRLSAFQMVN EVFSRSHHFR VLLITNFQEF LELTVETDAE QPLPPPKEVA RKLRTLAIQT
VQSWHATYGE AYKKLSLGYH FLKQIKKVDF QDVEARTLAE RKRQEEKQKR LERIYKEKLD
KAKQEMEEMT SGIEETLTEM NNCIRLLATD DFNLFDEDSA ASISTTAEDQ SDQPCCSKDL
SNEHNGKMME KKTDKEQTDE SSDESDMEEV PDEDAFLRST GLMSYRYQLE LDVSADLKVR
ETEENEALVN TVRDLHRLVT TRHLPLVQSW VQVFTKVGVE EELMRRATEL KKSLEHVLRK
HEYLHIDYKD RERLVMRAPE DGEDDDDDFV DVPEKEGYEP HIPEHLRTEY GLDETPSTST
SGTKAKPSRP VVKCAVPPVS SSLSRLKRRM CDEEQDPTCA AATLRVLKQK LHPAPSTSVP
DGSSESAVSS SDQSNMTKNK ASFKAPVIPF GMDLYYWGEE QPTAGKIIKQ TSQHQFWVPH
EVEEEVENKE LSAQMKSRCI TYAGKFKPVE HKCKAPMPNG SLCERQDRVK CPFHGHIIPR
DELGRPVNPE DALRLEREKR KREEEQPDWR DPELMREIEA ATGEDLGSSK TYGKGKKGNK
GKSKKKYPNL TDLKQKANTS RSRLEKKVFN KSSMRRVTEV MNKMDKRKHE KFANQFNYAL
N
