ID K7GHX0_PELSI Unreviewed; 358 AA.
AC K7GHX0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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};
GN Name=VPS72 {ECO:0000313|Ensembl:ENSPSIP00000019881.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000019881.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000019881.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AGCU01025301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01025302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7GHX0; -.
DR STRING; 13735.ENSPSIP00000019881; -.
DR Ensembl; ENSPSIT00000019975.1; ENSPSIP00000019881.1; ENSPSIG00000017615.1.
DR eggNOG; KOG2897; Eukaryota.
DR GeneTree; ENSGT00390000017503; -.
DR HOGENOM; CLU_040862_0_0_1; -.
DR OMA; TGPTIRY; -.
DR TreeFam; TF314532; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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:0140849; F:ATP-dependent H2AZ histone chaperone activity; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; 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 DNA-templated transcription; IEA:InterPro.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000007267}.
FT DOMAIN 286..315
FT /note="Vps72/YL1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00993"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 40354 MW; 0E5498706434AEA6 CRC64;
MSLAGGRAPR RTAGNRLAGL LEAEEDEFYQ TTYGGFTEGS GDDEYKGDQS DSDDEVDSDF
DIDEGDEPAS DQDDDEPKRK RRVVTKAYKE PIKSLRPKKP DTAASSSQKA REEKSAPLEL
QDEVGDSRKY MRQSTTEHTR QTFLRVQERQ VQSKRKKGGP NYDRPLTQDE LLREAKITEE
INLRSLENYE RLEADKKKQV QKKRKCVGPM IRYYSGTMPL ITDLGLKEEN VDVEGLDQDM
QQTAEAPQNA ASPVGKCSRT FITFTDDETF ERFFPKAKQP KLPVKEICPV THKLAVYRDP
ITDIPYSNIR AFKIIREAYK KYITAHGLPN AAASAALGAG PPAADPNVRA TRQKIIIK
//
