ID L5MCY9_MYODS Unreviewed; 402 AA.
AC L5MCY9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=MDA_GLEAN10009683 {ECO:0000313|EMBL:ELK36256.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36256.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB101680; ELK36256.1; -; Genomic_DNA.
DR AlphaFoldDB; L5MCY9; -.
DR eggNOG; KOG2897; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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:UP000010556}.
FT DOMAIN 328..357
FT /note="Vps72/YL1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00993"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 44284 MW; E68B0F88CBD51293 CRC64;
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEA RPGPRKREGE SGDDEYQGDQ
SDTEDEVDSD FDIDEGDEPS SDGEAEEPRR KRRIVTKAYK EPLKSLRPRK VSTPAGSSQK
TREEKTLLPL ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE
ELLREAKITE ELNLRSLETY ERLEADKKKQ VHKKRKCPGP VITYHSVTVP LLGEPGPKEE
NVDVEGLDPA PTASALTPQA GTGTETGTGT GTETGTGTGT GTGTGTGTTT RTVVPPPRCS
RTFITFSDDA TFEEWFPQVR PPKVPVREVC PVTHRPALYR DPVTDIPYAT ARAFKIIREA
YKKYITAHGL PPTASALGPG PLPPEPLPGS GPRALRQKIV IK
//
