ID A0A3B4UG46_SERDU Unreviewed; 367 AA.
AC A0A3B4UG46;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Vacuolar protein sorting-associated protein 72 homolog {ECO:0000256|ARBA:ARBA00020000};
DE AltName: Full=Transcription factor-like 1 {ECO:0000256|ARBA:ARBA00032814};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000016675.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000016675.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00002050}.
CC -!- SIMILARITY: Belongs to the VPS72/YL1 family.
CC {ECO:0000256|ARBA:ARBA00006832}.
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DR AlphaFoldDB; A0A3B4UG46; -.
DR STRING; 41447.ENSSDUP00000016675; -.
DR Ensembl; ENSSDUT00000016983.1; ENSSDUP00000016675.1; ENSSDUG00000012188.1.
DR GeneTree; ENSGT00390000017503; -.
DR OMA; TGPTIRY; -.
DR OrthoDB; 12606at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0140849; F:ATP-dependent H2AZ histone chaperone activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR InterPro; IPR008895; Vps72/YL1.
DR InterPro; IPR013272; Vps72/YL1_C.
DR InterPro; IPR046757; YL1_N.
DR PANTHER; PTHR13275:SF4; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 72 HOMOLOG; 1.
DR PANTHER; PTHR13275; YL-1 PROTEIN TRANSCRIPTION FACTOR-LIKE 1; 1.
DR Pfam; PF05764; YL1; 1.
DR Pfam; PF08265; YL1_C; 1.
DR SMART; SM00993; YL1_C; 1.
PE 3: Inferred from homology;
FT DOMAIN 294..323
FT /note="Vps72/YL1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00993"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 41740 MW; 2604A859E6F42D9E CRC64;
MSLAVGREPR KTAGNRMSKL LDAEEEDEFY KTTYGGFNDE SGDDEYHGEH SDTEDEVDSD
FDIDEGDEPD SDQEEDAPRR KSRVVTKAYK EPIKVAKPKP KRPSEEQKKT EKTKVELKRR
IPQEFQDFNE TRKSVRQSTS EHTRKTNLRL QERQDAPRRR RGAHRDRPLT QEELLAEAKI
TAEINIRSLE NYERLEADKK KQVHKKRRFE GPTIRYHSVL MPLVSHSVLK EENVDVEGLD
QDVPQTAPQN PTTPSQQPAG GLCSRTYITF SDDEAFEAAF PRSAQSSPQL PVQEVCPVTH
KAALYRDPVT DIPYANTRAF RIIREAYRKY VAAHGFPNTS GGVTGHDSSA TKGARQKMVV
KQSAVST
//
