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Database: UniProt
Entry: A0A3P9AVR3_9CICH
LinkDB: A0A3P9AVR3_9CICH
Original site: A0A3P9AVR3_9CICH 
ID   A0A3P9AVR3_9CICH        Unreviewed;       300 AA.
AC   A0A3P9AVR3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=General transcription factor IIH subunit 3 {ECO:0000256|RuleBase:RU368090};
DE   AltName: Full=General transcription factor IIH polypeptide 3 {ECO:0000256|RuleBase:RU368090};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005001796.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005001796.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005001796.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the general transcription and DNA repair factor
CC       IIH (TFIIH) core complex, which is involved in general and
CC       transcription-coupled nucleotide excision repair (NER) of damaged DNA
CC       and, when complexed to CAK, in RNA transcription by RNA polymerase II.
CC       In NER, TFIIH acts by opening DNA around the lesion to allow the
CC       excision of the damaged oligonucleotide and its replacement by a new
CC       DNA fragment. In transcription, TFIIH has an essential role in
CC       transcription initiation. When the pre-initiation complex (PIC) has
CC       been established, TFIIH is required for promoter opening and promoter
CC       escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC       subunit of RNA polymerase II by the kinase module CAK controls the
CC       initiation of transcription. {ECO:0000256|RuleBase:RU368090}.
CC   -!- SUBUNIT: Part of a TFIID-containing RNA polymerase II pre-initiation
CC       complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1,
CC       GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2,
CC       ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10,
CC       TAF11, TAF12 and TAF13. Component of the 7-subunit TFIIH core complex
CC       composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and
CC       GTF2H5, which is active in NER. The core complex associates with the 3-
CC       subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H,
CC       CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC       transcription. Interacts with RARA; the interaction requires prior
CC       phosphorylation of RARA on 'Ser-369' which then enhances interaction of
CC       RARA with CDK7. {ECO:0000256|RuleBase:RU368090}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368090}.
CC   -!- SIMILARITY: Belongs to the TFB4 family. {ECO:0000256|ARBA:ARBA00005273,
CC       ECO:0000256|RuleBase:RU368090}.
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DR   RefSeq; XP_004544742.1; XM_004544685.1.
DR   AlphaFoldDB; A0A3P9AVR3; -.
DR   STRING; 106582.ENSMZEP00005001796; -.
DR   Ensembl; ENSMZET00005001890.1; ENSMZEP00005001796.1; ENSMZEG00005001438.1.
DR   GeneID; 101465917; -.
DR   KEGG; mze:101465917; -.
DR   CTD; 2967; -.
DR   GeneTree; ENSGT00390000013143; -.
DR   OrthoDB; 45434at2759; -.
DR   Proteomes; UP000265160; LG12.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR004600; TFIIH_Tfb4/GTF2H3.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   NCBIfam; TIGR00627; tfb4; 1.
DR   PANTHER; PTHR12831:SF0; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 3; 1.
DR   PANTHER; PTHR12831; TRANSCRIPTION INITIATION FACTOR IIH TFIIH , POLYPEPTIDE 3-RELATED; 1.
DR   Pfam; PF03850; Tfb4; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|RuleBase:RU368090};
KW   DNA repair {ECO:0000256|RuleBase:RU368090};
KW   Metal-binding {ECO:0000256|RuleBase:RU368090};
KW   Nucleus {ECO:0000256|RuleBase:RU368090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU368090};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU368090}; Zinc {ECO:0000256|RuleBase:RU368090};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU368090}.
SQ   SEQUENCE   300 AA;  33154 MW;  E6951F26A43B84B7 CRC64;
     MASEDEINLL VIVVDVNPIW WGQQAQRDPQ FTLSKCMDAV MVMGNAHMAM ARTNKLAVIA
     SHCQGSHFLY PSKSWSGEDG GGNDVSSSGD GKYELLSAAN NLIVEEIRNI MSKIEVTGNS
     TDTLLAGSLA KALCYIHRLT KELEVGQEIK SRILVVKAAE DCALQYMNFM NVIFAAQKQN
     ILIDACVLDS DSGLLQQACD ITGGLYMKIP QKVALAQYLL WVFLPDSEQR SQLVLPPPAH
     VDYRAACFCH RNLIEIGYVC SVCLSIFCNF SPICTTCETA FKIQLPQIVK PKKKKLKQPM
//
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