ID   UVSSA_BOVIN             Reviewed;         685 AA.
AC   F1MX48;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=UV-stimulated scaffold protein A;
GN   Name=UVSSA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
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. Acts by promoting stabilization of ERCC6 by recruiting
CC       deubiquitinating enzyme USP7 to TC-NER complexes, preventing UV-induced
CC       degradation of ERCC6 by the proteasome. Interacts with the elongating
CC       form of RNA polymerase II (RNA pol IIo) and facilitates its
CC       ubiquitination at UV damage sites, leading to promote RNA pol IIo
CC       backtracking to allow access to the nucleotide excision repair
CC       machinery. Not involved in processing oxidative damage (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the elongating form of RNA polymerase II (RNA
CC       pol IIo). Interacts with ERCC6, ERCC8 and USP7 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250}. Note=Accumulates at UV
CC       DNA damage sites. {ECO:0000250}.
CC   -!- PTM: Monoubiquitinated: ubiquitination does not increase in response to
CC       UV. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UVSSA family. {ECO:0000305}.
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DR   EMBL; DAAA02018546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1MX48; -.
DR   SMR; F1MX48; -.
DR   STRING; 9913.ENSBTAP00000016697; -.
DR   PaxDb; F1MX48; -.
DR   PRIDE; F1MX48; -.
DR   eggNOG; KOG2374; Eukaryota.
DR   HOGENOM; CLU_023577_0_0_1; -.
DR   InParanoid; F1MX48; -.
DR   OrthoDB; 996127at2759; -.
DR   TreeFam; TF321660; -.
DR   Proteomes; UP000009136; Unplaced.
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   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR018610; UVSSA.
DR   PANTHER; PTHR28670; PTHR28670; 1.
DR   Pfam; PF09740; DUF2043; 1.
PE   3: Inferred from homology;
KW   Chromosome; Coiled coil; DNA damage; DNA repair; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..685
FT                   /note="UV-stimulated scaffold protein A"
FT                   /id="PRO_0000417993"
FT   REGION          2..145
FT                   /note="VHS-like"
FT   REGION          243..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          153..198
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        251..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..381
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..459
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YD98"
SQ   SEQUENCE   685 AA;  76862 MW;  0CCDE2670E87BD37 CRC64;
     MDQKLSELVE ELTTSGEPQL NPEKMKQLKK ICKSSEEQLG HAYHLLMAQL SQEHAEIRLS
     AFQVLDQLFA RSHQFRTLVV SNFQEFLELT LGTDHERPLP PPREVAQRLR QAATQAIRGW
     NEKYGAAYKK LALGFHFLKH SKQVDFQDVD ARTVAERKRA EERQKRLDRI YKERSEWAAR
     EMEEMSTEIR GCLTELESCF RLLLPFDLDL APGAAWCPVP EKGDRDEEQP CCSKSLAACA
     HHPGAMDAGG PPSEDEDRDP DGFVRRHGLG SRQYTLDVEL SSDSLRVREN EDNSAVIRAA
     RDALRLIQNK LLPAACSWVQ LFTRAGTYGG HLEGAIHLKA ELEAALKRSR ELDIVPEEGR
     SGETAAPGDE DEDEDDFVEV PEKEGYEACV PEHLRPECGE QRHGPGRGLE EGLAAPGSQA
     RKRPGSDMEA FDPTSAAAQQ QWPRPHGPPA SPPSPRAPLA PEQAAWRAAE QARAPVVPFG
     VDLCYWGQEE LMAGKILKCD SEHRFWKPCE VDAEVESASV SEALRSRRIT FAGQFEPVQH
     RCRAPRPDGQ LCARQDRLKC PFHGKIIPRD DAGRPLNAED RAREQRQQLQ RPAGRPDWQD
     PEFLRDVEAA TGVDLGSSRP GGKGKGKRRK HSGLTDLKRQ ADTARARIAK KVFAKAAVQR
     VVTAMNQMDE KKHEKFANQF NYALN