ID G1TAP3_RABIT Unreviewed; 942 AA.
AC G1TAP3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000013755.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000013755.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000013755.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000013755.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738}.
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DR AlphaFoldDB; G1TAP3; -.
DR SMR; G1TAP3; -.
DR STRING; 9986.ENSOCUP00000013755; -.
DR Ensembl; ENSOCUT00000016007.4; ENSOCUP00000013755.3; ENSOCUG00000015998.4.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000157440; -.
DR HOGENOM; CLU_006530_2_1_1; -.
DR InParanoid; G1TAP3; -.
DR TreeFam; TF106174; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000015998; Expressed in ovary and 16 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR CDD; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1.
DR Gene3D; 6.10.250.1550; -; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF11; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT DOMAIN 68..156
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..166
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 248..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 103409 MW; FD22D59650B0E6C8 CRC64;
LSTQGHPGRL PVDLGAGGGP GQPCRLSDRP LCCALSAVDV ATALPLQVAP SAVPMDLRLD
HPFALPVAEP ALREQRLQQE LLALKQQQQL QRQVLIAEFQ RQHEQLSRQH EAQLQEHIKQ
QQEMLAMKHQ QELLEHQRKL ERFIYFKELE ERQRERERKR EREREVFHPM VHYPDGAVAS
TEVKMKLQEF VLNKKKALAH RNLNHCISSD PRYWYGKTQH SSLDQSSPPQ SGTSASYAHP
VLGMYDTKDD FPLRKTASEP NLKLRSRLKQ KVAERRSSPL LRRKDGPVVT ALKKRPLDVT
DSACSSAPGS GPSSPNNNSS GNVSTENGGV PAAPSIPTEA SLAPRLVTRE GSVAPLPLYT
SPSLPNITLG LPATGPSAGA AAQQDTERLA LPALQQRISL FPGSHLAPYL STSPLERDGG
AAHSPLLQHM VLLEQPPVTD WYLSGLGALP LHTQPLVGAD RVSPSIHKLR QHRPLGRTQS
APLPQNAQAL QHLVIQQQHQ QFLEKHKQQF QQQLHLNKII SKPSEPPRQP ESHPEETEEE
LREHQALLDQ PYLERLSGQK EAQVAGVQVK QEPIESDEEE AEPREAEPGQ RPPTEQELLF
RQVSVGTGRP PACSAAAGPP VFHRSPPTCR SAPASAPADP LQCGPCSPRL VYDTLMLKHQ
CACGNTNSHP EHAGRIQSIW SRLQETGLRS QCECIRGRKA TLEELQTVHS ESHTLLYGTN
PLNRQKLDSK KLLGICSAPF PPRQGCGIPS EPSSIHWFAS LMAALARAGP GHSQEPGTPS
GSPTWAAGPK HLSRLHCLPR SSQDLNQHSS QHGYNVLRGS PASPQGSCTE VGASPAPWAQ
TTDLGPADGC EDSLLFPPWP SAAPHQFLSP SSLPLSPRGE ASSHSSLHKP QEAREELPAP
RTSSQGQGST AVRGPGTLHT RPDRLLHPCV HWLSSFRARF YF
//
