VPS72_BOVIN
ID VPS72_BOVIN Reviewed; 364 AA.
AC Q5E9F6; Q2TBU7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Vacuolar protein sorting-associated protein 72 homolog;
DE AltName: Full=Transcription factor-like 1;
GN Name=VPS72; Synonyms=TCFL1;
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 MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deposition-and-exchange histone chaperone specific for H2AZ1,
CC specifically chaperones H2AZ1 and deposits it into nucleosomes. As
CC component of the SRCAP complex, mediates the ATP-dependent exchange of
CC histone H2AZ1/H2B dimers for nucleosomal H2A/H2B, leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC {ECO:0000250|UniProtKB:Q15906}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41 and VPS72/YL1. Component of a NuA4-related complex which
CC contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41.
CC Also part of a multiprotein complex which contains SRCAP and which
CC binds to H2AZ1/H2AZ. Interacts (via N-terminal domain) with H2AZ1.
CC {ECO:0000250|UniProtKB:Q15906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15906}.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family. {ECO:0000305}.
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DR EMBL; BT020964; AAX08981.1; -; mRNA.
DR EMBL; BC109639; AAI09640.1; -; mRNA.
DR RefSeq; NP_001015658.1; NM_001015658.1.
DR AlphaFoldDB; Q5E9F6; -.
DR SMR; Q5E9F6; -.
DR STRING; 9913.ENSBTAP00000024063; -.
DR PaxDb; Q5E9F6; -.
DR PRIDE; Q5E9F6; -.
DR Ensembl; ENSBTAT00000024063; ENSBTAP00000024063; ENSBTAG00000018074.
DR GeneID; 534883; -.
DR KEGG; bta:534883; -.
DR CTD; 6944; -.
DR VEuPathDB; HostDB:ENSBTAG00000018074; -.
DR VGNC; VGNC:36831; VPS72.
DR eggNOG; KOG2897; Eukaryota.
DR GeneTree; ENSGT00390000017503; -.
DR HOGENOM; CLU_040862_0_0_1; -.
DR InParanoid; Q5E9F6; -.
DR OMA; VNTKAYK; -.
DR OrthoDB; 1468037at2759; -.
DR TreeFam; TF314532; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000018074; Expressed in oocyte and 105 other tissues.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IEA:Ensembl.
DR GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR InterPro; IPR008895; Vps72/YL1.
DR InterPro; IPR013272; Vps72/YL1_C.
DR PANTHER; PTHR13275; PTHR13275; 1.
DR Pfam; PF05764; YL1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR SMART; SM00993; YL1_C; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..364
FT /note="Vacuolar protein sorting-associated protein 72
FT homolog"
FT /id="PRO_0000239003"
FT DNA_BIND 156..206
FT /evidence="ECO:0000255"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15906"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15906"
FT CONFLICT 254
FT /note="P -> T (in Ref. 2; AAI09640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 40651 MW; BFECD775B198F928 CRC64;
MSLAGGRAPR KTAGNRLSGL LEKEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD
FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK VSTPAGSSQK TREEKALLPL
ELQDDGTDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE ELLREAKITE
ELNLRSLETY ERLEADKKKQ VHKKRKCPGP IITYHSVTVP LVGEPGPKEE NVDVEGLDPA
PMASALAARA GTGPVIPPAR CSRTFITFSD DATFEEWFPQ GRTPKIPVRE VCPVTHRPAL
YRDPVTDIPY ATARAFKIIR EAYKKYITAH GLPPTASALG PGPPPPEPLP GSGPRALRQK
IVIK
