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Database: UniProt
Entry: A0A3B1K883_ASTMX
LinkDB: A0A3B1K883_ASTMX
Original site: A0A3B1K883_ASTMX 
ID   A0A3B1K883_ASTMX        Unreviewed;       380 AA.
AC   A0A3B1K883;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ENSAMXP00000049854.1};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000049854.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000049854.1}
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   RefSeq; XP_015461407.1; XM_015605921.1.
DR   AlphaFoldDB; A0A3B1K883; -.
DR   Ensembl; ENSAMXT00000038153.1; ENSAMXP00000049854.1; ENSAMXG00000018817.2.
DR   GeneID; 103047377; -.
DR   KEGG; amex:103047377; -.
DR   CTD; 795272; -.
DR   GeneTree; ENSGT00390000017503; -.
DR   OrthoDB; 12606at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000018817; Expressed in brain and 7 other cell types or tissues.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467}.
FT   DOMAIN          312..341
FT                   /note="Vps72/YL1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00993"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..280
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..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   380 AA;  42813 MW;  1464F06866806B94 CRC64;
     MSLAFSRAPR KNAGSRMSKL LDAEEEDEFY KTTYGGFNDE SGDDEYKGDL SDTEDEVDSD
     FDIDEGEEPD SEQEEDGPRR KTRVVTKAYK EPIKAVKPKP KPKKLSELPR RADKTKTDKH
     KTFELQEDIS KNRKSVRQST TEHTRLTYLR LQERQVAPRR RKGTRHERPL TQAELLAEAK
     VTAEINLRSL ENYERLEADK KKQVHKKRQC VGPVIRYHSV LMPLVSNPSL KEENVDVEGL
     DQDPQQSHPG PAAGAAMSSQ SETPLSGQQP STSASLPPGG ARCSRTYITF SDEDTFQSFF
     PKTPAPRVPA REVCPVTHKP ALYRDPITDI PYANLRAFKI IREAYKKYVA AHGLPCPGAT
     LPAEPTAKNP RQKIVIKQGM
//
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