ID H0VHC8_CAVPO Unreviewed; 1529 AA.
AC H0VHC8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN Name=KDM5B {ECO:0000313|Ensembl:ENSCPOP00000009555.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000009555.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
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:ENSCPOP00000009555.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000009555.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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DR EMBL; AAKN02017933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02017934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02017935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02017936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02017937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 10141.ENSCPOP00000009555; -.
DR Ensembl; ENSCPOT00000010741.3; ENSCPOP00000009555.3; ENSCPOG00000010644.4.
DR VEuPathDB; HostDB:ENSCPOG00000010644; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000157076; -.
DR HOGENOM; CLU_000991_2_2_1; -.
DR InParanoid; H0VHC8; -.
DR OMA; TMMNPGR; -.
DR TreeFam; TF106476; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000010644; Expressed in testis and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:2000864; P:regulation of estradiol secretion; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0061038; P:uterus morphogenesis; IEA:Ensembl.
DR CDD; cd16874; ARID_KDM5B; 1.
DR CDD; cd15603; PHD1_KDM5B; 1.
DR CDD; cd15607; PHD2_KDM5B; 1.
DR CDD; cd15687; PHD3_KDM5B; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR047981; KDM5B_ARID.
DR InterPro; IPR047978; KDM5B_PHD1.
DR InterPro; IPR047979; KDM5B_PHD3.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF3; LYSINE-SPECIFIC DEMETHYLASE 5B; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 82..172
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 294..344
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 438..604
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1161..1209
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1469..1523
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1529 AA; 174117 MW; F82FF8F3FE1C5FB9 CRC64;
MDPATALPPG PRPAMPLGGP GPLGEFLPPP ECPVFELSWE VVRAPLRFHP QDPDWQPPFA
CDVDKLHFTP RIQRLNELEA QTRVKLNFLD QIAKYWELQG STLKIPHVER KILDLFQLNK
LVAEEGGFAV VCKDRKWTKI ATKMGFAPGK AVGSHIRGHY ERILNPYNLF LSGDSLRCLQ
KPNLTTDTKD KEYKPHDIPQ RQSVQPSETC PPARRAKRMR AETMNIKVEP EETTEARTHN
LRRRMGCPTL KCENEKEMKS NIKQEPLEKK DYIVESEKEK PKSRSKKTTN AVDLYVCLLC
GSGNDEDRLL LCDGCDDSYH TFCLIPPLHD VPKGDWRCPK CLAQECSKPQ EAFGFEQAAR
DYTLRTFGEM ADAFKSDYFN MPVHMVPTEL VEKEFWRLVS TIEEDVTVEY GADIASKEFG
SGFPVRDGKI KLSPEEEEYL DSGWNLNNMP VMEQSVLAHI TADICGMKLP WLYVGMCFSS
FCWHIEDHWS YSINYLHWGE PKTWYGVPGY AAEQLENVMK KLAPELFVSQ PDLLHQLVTI
MNPNTLMTHE VPVYRTNQCA GEFVITFPRA YHSGFNQGFN FAEAVNFCTV DWLPLGRQCV
EHYRLLHRYC VFSHDEMICK MASKADVLDV VVASTVQKDM AIMIEDEKAL REVVHKLGVI
DSERMDFELL PDDERQCIKC KTTCFMSAIS CSCKPGLLVC LHHVKELCSC PPYKYKLQYR
YTLDDLYPMM NALKLRAESY NEWALNVNEA LEAKINKKKS LINFKALIEE SEMKKFPDND
LLRHLRLVTQ DAEKCASVAQ QLLNGKRQTR YRSGGGKSQN QLTVNELRQF VTQLYALPCV
LSQTPLLKDL LNRVEDFQQH SQKLLSEEMP SAAELQDLLD ISFEFDVELP QLAEMRTRLE
QARWLEEVQQ ACLDPSSLTL DDMRRLIDLG VGLAPYSAVE KAMARLQELL TVSEHWDDKA
KSLLRARPRL SLSSLATAVK EIEEIPAYLP NGAALKDSVQ RARDWLQDVE TLQAGGRVPV
LDTLIELVTR GRSIPVHLNS LPRLESLVAE VQAWKECAAN TFLTENSPYS LLEVLCPRCD
IGLLGLKRKQ RKLKEPLPSG KKKNTKLENL SDLERALTES KETASAMATL GEARLREMEA
LQSLRVANEG KLLSPVQDVE LKVCLCQKAP ATPMIQCELC RDAFHTNCVA VPSTLQNPRI
WLCPHCRRSE KPPLEKILPL LASLQRIRVR LPEGDALRYM IERTVNWQHR AQQLLSSGNL
KFVQDRVSSG LLSSRWQTSG RQVSETSKVS QPPGTTSFSL PDDWDNRTSY LHSPFSTGQS
CIPLHGISPE VNELLMEAQL LQVSLPEIQE LYQTLLAKPS PVSQTDRSSP VRPSSEKNDC
CRGKRDGINS LERKLKRRLD REGLSNERWD RVKKMRTPKK KKIKLSHPKD INNFKLERER
SYELVRSAET HSLPSDTSYS EQEDSEDEDA ICPAVSCLQP EGDEVDWVQC DGSCNQWFHQ
VCVGVSPEMA EKEDYICVRC TGKDAPSRK
//
