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Database: UniProt
Entry: W5LJQ3_ASTMX
LinkDB: W5LJQ3_ASTMX
Original site: W5LJQ3_ASTMX 
ID   W5LJQ3_ASTMX            Unreviewed;       351 AA.
AC   W5LJQ3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 37.
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   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:ENSAMXP00000020065.2, 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:ENSAMXP00000020065.2}
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   AlphaFoldDB; W5LJQ3; -.
DR   STRING; 7994.ENSAMXP00000020065; -.
DR   Ensembl; ENSAMXT00000020065.2; ENSAMXP00000020065.2; ENSAMXG00000019484.2.
DR   eggNOG; KOG2897; Eukaryota.
DR   GeneTree; ENSGT00390000017503; -.
DR   HOGENOM; CLU_149415_0_0_1; -.
DR   InParanoid; W5LJQ3; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000019484; Expressed in camera-type eye and 14 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          276..305
FT                   /note="Vps72/YL1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00993"
FT   REGION          1..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..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..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  39787 MW;  8DAAE7EA96FEA7AB CRC64;
     MSLAQGREQR CTAGNRMGKL LDAEEEDDFY KTTYGGFNDE SGDDEYRGDH SDTEDEVDSD
     FDIDEGDEPD SNEEDDAPRR KSRVVTKAYK EPVKAVKPKV KRPSEEPKRT ERLKPEKRSH
     QDLQEYGELR KSVRKSTSEH TRKTFERLQE RQQEAPRRRK ANTEPVLSQE ELLKEAQITA
     QSNLQSLENY ERLEADKKKH VHKKRRFEGP TVRYHSEENV DVEGLDQDTP QSSSSSGAVG
     TRSLCSRTFI TFSDDEAFRT AFPQVSSPDP ALPVQEVCPV THKPALYRDP VTDIPYSDSR
     AFRIIREAYR KYISAHGFPG NSDSTQSAGG SSAPAKTLKP KTLIKQGLVT A
//
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