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Database: UniProt
Entry: A0A3B4C6E3_PYGNA
LinkDB: A0A3B4C6E3_PYGNA
Original site: A0A3B4C6E3_PYGNA 
ID   A0A3B4C6E3_PYGNA        Unreviewed;       378 AA.
AC   A0A3B4C6E3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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:ENSPNAP00000006129.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000006129.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000006129.1}
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   RefSeq; XP_017577188.1; XM_017721699.1.
DR   AlphaFoldDB; A0A3B4C6E3; -.
DR   STRING; 42514.ENSPNAP00000006129; -.
DR   Ensembl; ENSPNAT00000004093.1; ENSPNAP00000006129.1; ENSPNAG00000012209.1.
DR   GeneTree; ENSGT00390000017503; -.
DR   OMA; YRNTYGG; -.
DR   OrthoDB; 12606at2759; -.
DR   Proteomes; UP000261440; 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          310..339
FT                   /note="Vps72/YL1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00993"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..72
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  42523 MW;  B1BFAFEA41DAAAE0 CRC64;
     MSLAFCRAPR KNAGSRMSKL LDAEEEDEFY KTTYGGFNDE SGDDEYKGDL SDTEDEVDSD
     FDIDEGEEPD SEQEEDGPRR KSRVVTKAYK EPIKAVKPKP KPKKLSELPR RVDKIKTEKH
     KTLELQDDIN RKSVRQSTTE HTRLTYLRLQ ERQVAPRRKK GTRHERPLTQ AELLAEAKVT
     AEINLRSLEN YERLEADKKK QVHKKRQCVG PVIRYHSVLM PLVSDPSFKE ENVDVEGLDQ
     DPQQSLPGSG SGAAVMSQSE ATLSGQPVSI SAPPPPGGGR CSRTYITFSD EDTFQSYFPK
     TSAPRVPVKE VCPVTHKPAL YRDPITDIPY ANVRAFKIIR EAYKKYVAAH GLPCPGTTLP
     AEPTAKSLRQ KIVIKQGI
//
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