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Database: UniProt
Entry: D3ZAT1_RAT
LinkDB: D3ZAT1_RAT
Original site: D3ZAT1_RAT 
ID   D3ZAT1_RAT              Unreviewed;       514 AA.
AC   D3ZAT1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 2.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Histone H4 transcription factor {ECO:0000313|Ensembl:ENSRNOP00000012868.6};
GN   Name=Hinfp {ECO:0000313|Ensembl:ENSRNOP00000012868.6,
GN   ECO:0000313|RGD:1311492};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000012868.6, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000012868.6, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000012868.6,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000012868.6}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000012868.6};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_002727096.1; XM_002727050.5.
DR   RefSeq; XP_002729961.1; XM_002729915.5.
DR   AlphaFoldDB; D3ZAT1; -.
DR   SMR; D3ZAT1; -.
DR   STRING; 10116.ENSRNOP00000012868; -.
DR   PaxDb; 10116-ENSRNOP00000012868; -.
DR   Ensembl; ENSRNOT00000012868.7; ENSRNOP00000012868.6; ENSRNOG00000009499.7.
DR   GeneID; 300665; -.
DR   KEGG; rno:300665; -.
DR   UCSC; RGD:1311492; rat.
DR   AGR; RGD:1311492; -.
DR   CTD; 25988; -.
DR   RGD; 1311492; Hinfp.
DR   eggNOG; KOG3608; Eukaryota.
DR   GeneTree; ENSGT00870000136508; -.
DR   HOGENOM; CLU_026599_0_0_1; -.
DR   InParanoid; D3ZAT1; -.
DR   OMA; QDHIVQH; -.
DR   OrthoDB; 2915296at2759; -.
DR   TreeFam; TF350923; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000009499; Expressed in spleen and 19 other cell types or tissues.
DR   GO; GO:0015030; C:Cajal body; ISO:RGD.
DR   GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0042393; F:histone binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0044843; P:cell cycle G1/S phase transition; ISO:RGD.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:RGD.
DR   GO; GO:0006281; P:DNA repair; ISO:RGD.
DR   GO; GO:0006351; P:DNA-templated transcription; ISO:RGD.
DR   GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0045445; P:myoblast differentiation; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24391:SF26; HISTONE H4 TRANSCRIPTION FACTOR; 1.
DR   PANTHER; PTHR24391; HISTONE H4 TRANSCRIPTION FACTOR-RELATED; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   Pfam; PF13894; zf-C2H2_4; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          166..195
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          226..253
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          252..280
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          281..308
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          309..339
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          342..370
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          483..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  59329 MW;  FC914EF304411B0C CRC64;
     MSPPGKVPRK ENLGLQCEWG SCSFVCSAME EFFDHVTQHL QQHIHGSKEE EEEEDLLEEE
     FSCLWQECGF CSLDSSADLI RHVYFHCYHT KLKQWGLQAL QSQADLSPCI LDFQSRNVIP
     DTPDHFLCLW EHCESVFDNP EWFYRHVDAH SLCCEYQAVS KDNHVVLCGW KGCTCTFKDR
     CKLREHLRSH TQEKVVACPT CGGMFANNTK FLDHIRRQTS LDQQRFQCSH CSKRFATERL
     LRDHMRNHVN HYKCPLCDMT CPLPSSLRNH MRFRHSEDRP FKCDCCDYSC KNLIDLRKHL
     DTHSKESAYR CDFENCSFSA RSLSSVKSHH RKVHEGDSEP RYKCHVCDKC FTRGNNLTVH
     LRKKHQFKWP SGHPRFRYKE HEDGYMRLQL VRYESVELTQ QLLQQLQEGS DPGLALNESS
     LQGIVLETVL GGPGPEEETE EEGRVVEGTA LSASQDNPSS ALHMVSQTDA QGQRDLVYYV
     LSEAPGEPPP VSEAPSREME KLQGIPEEPD VQMG
//
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