MSL1_DANRE
ID MSL1_DANRE Reviewed; 489 AA.
AC A9JRX0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Male-specific lethal 1-like 1;
DE Short=MSL1-like 1;
DE AltName: Full=Male-specific lethal-1 homolog 1;
DE Short=MSL-1;
GN Name=msl1l1; ORFNames=zgc:175094;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of histone acetyltransferase complex. Within MSL
CC complex, promotes ubiquitination of histone H2B.
CC {ECO:0000250|UniProtKB:Q68DK7}.
CC -!- SUBUNIT: Component of a multisubunit histone acetyltransferase complex
CC (MSL). {ECO:0000250|UniProtKB:Q68DK7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q68DK7}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q6PDM1}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q6PDM1}.
CC -!- SIMILARITY: Belongs to the msl-1 family. {ECO:0000305}.
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DR EMBL; BC155827; AAI55828.1; -; mRNA.
DR RefSeq; NP_001107940.1; NM_001114468.1.
DR AlphaFoldDB; A9JRX0; -.
DR SMR; A9JRX0; -.
DR STRING; 7955.ENSDARP00000101527; -.
DR PaxDb; A9JRX0; -.
DR PRIDE; A9JRX0; -.
DR GeneID; 100000715; -.
DR KEGG; dre:100000715; -.
DR CTD; 100000715; -.
DR ZFIN; ZDB-GENE-030131-8168; msl1a.
DR eggNOG; ENOG502QQ0S; Eukaryota.
DR InParanoid; A9JRX0; -.
DR OrthoDB; 560559at2759; -.
DR PhylomeDB; A9JRX0; -.
DR PRO; PR:A9JRX0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0072487; C:MSL complex; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR InterPro; IPR026711; Msl-1.
DR InterPro; IPR031840; MSL1_dimer.
DR InterPro; IPR029332; PEHE_dom.
DR PANTHER; PTHR21656; PTHR21656; 2.
DR Pfam; PF16801; MSL1_dimer; 1.
DR Pfam; PF15275; PEHE; 1.
DR SMART; SM01300; PEHE; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Coiled coil; Nucleus; Reference proteome.
FT CHAIN 1..489
FT /note="Male-specific lethal 1-like 1"
FT /id="PRO_0000349238"
FT REGION 126..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..227
FT /evidence="ECO:0000255"
FT MOTIF 380..394
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q6PDM1"
FT COMPBIAS 249..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 55880 MW; 611877E522585310 CRC64;
MTLRSIVIKS GGHRLDTSLI KKPAEINEYL ASLKKETCDF ATYVLCSICN SIIQKHQVQS
KAKISCRKVL SCPDQSSAGG LGHKNWEPSG ALILPSTKQM GAEGSPVKSR SLFCQTNHNH
LVNMDPMVSN DNNQQREGEQ VGAMVGDSSP EDSPSGKHWN VRKGSGLVDP QTSCIRQILL
LQLELIEQQQ KHLHNKNKEI EDLKAEKEML MARIERMEHR LQMVKKDGVV SRPSQTTCHK
EPEAETTTSD DVQHSGGRVQ TPKQTQRGRG VKGSKGKFLL QDSPTGRSRR GQPRSPPTSQ
QESPALKEDM QCHSKEVPYL TTTEMYLSHW QTPPSPQRDP STVHENTVEV PSWRESILEP
LGQKEASDIL ECLDDSVFLK RHSKLELDEK RRKRWDIQRI REQRMFQRLQ QRMNRRKVIQ
ESEPELLSFH AEPEDVEYIM VTPFLPVVAF GSPLPNLKQQ DFDLPWLDER SRCQPEVTKK
RTPRRRCRK