ID A0A2Y9E9Q8_TRIMA Unreviewed; 374 AA.
AC A0A2Y9E9Q8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LOC101345256 {ECO:0000313|RefSeq:XP_004389608.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004389608.1};
RN [1] {ECO:0000313|RefSeq:XP_004389608.1}
RP IDENTIFICATION.
RG RefSeq;
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_004389608.1; XM_004389551.2.
DR AlphaFoldDB; A0A2Y9E9Q8; -.
DR STRING; 127582.A0A2Y9E9Q8; -.
DR GeneID; 101345256; -.
DR KEGG; tmu:101345256; -.
DR InParanoid; A0A2Y9E9Q8; -.
DR OrthoDB; 12606at2759; -.
DR Proteomes; UP000248480; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT DOMAIN 301..330
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 42..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 114..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 41492 MW; 8C3B29BDA00D79A4 CRC64;
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD
FDIDEGDGPS SDGEAEEPRR KRRIVTKAYK EPLKSLRPRK VSNPAGSSQK TREEKALLPL
ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHYERPLTQE ELLREAKITE
ELNLRSLETY ERLEADKKKQ VHKKRKCSGP IITYHSVTVP LVGEPGPKEE NVDVEGCVSV
SLSFALRLDP APAASALTPH AGTGAVVPPA RCSRTFITFS DDATFEEWFP PGRPPKVPVR
EVCPVTHRPA LYRDPVTDIP YATARAFKII REAYKKYITA HGLPAASALG PGPPPPEPLA
GPGPRALRQK IVIK
//
