ID   MYSM1_CHICK             Reviewed;         832 AA.
AC   Q5F3F2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Histone H2A deubiquitinase MYSM1;
DE            Short=2A-DUB;
DE            EC=3.4.19.-;
DE   AltName: Full=Myb-like, SWIRM and MPN domain-containing protein 1;
GN   Name=MYSM1; ORFNames=RCJMB04_19a21;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Metalloprotease that specifically deubiquitinates
CC       monoubiquitinated histone H2A, a specific tag for epigenetic
CC       transcriptional repression, thereby acting as a coactivator.
CC       Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated
CC       nucleosomes. Deubiquitination of histone H2A leads to facilitate the
CC       phosphorylation and dissociation of histone H1 from the nucleosome.
CC       Acts as a coactivator by participating in the initiation and elongation
CC       steps of androgen receptor (AR)-induced gene activation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DOMAIN: Binds double-stranded DNA via the SANT domain. The SWIRM domain
CC       does not bind double-stranded DNA (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. MYSM1 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ851698; CAH65332.1; -; mRNA.
DR   RefSeq; NP_001012945.1; NM_001012927.1.
DR   AlphaFoldDB; Q5F3F2; -.
DR   SMR; Q5F3F2; -.
DR   STRING; 9031.ENSGALP00000037248; -.
DR   MEROPS; M67.005; -.
DR   PaxDb; Q5F3F2; -.
DR   GeneID; 424671; -.
DR   KEGG; gga:424671; -.
DR   CTD; 114803; -.
DR   VEuPathDB; HostDB:geneid_424671; -.
DR   eggNOG; KOG1279; Eukaryota.
DR   eggNOG; KOG1555; Eukaryota.
DR   InParanoid; Q5F3F2; -.
DR   OrthoDB; 590811at2759; -.
DR   PhylomeDB; Q5F3F2; -.
DR   PRO; PR:Q5F3F2; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   CDD; cd00167; SANT; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR033497; MYSM1.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR12802:SF67; PTHR12802:SF67; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS51293; SANT; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   2: Evidence at transcript level;
KW   Activator; Chromatin regulator; DNA-binding; Hydrolase; Metal-binding;
KW   Metalloprotease; Nucleus; Protease; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation pathway; Zinc.
FT   CHAIN           1..832
FT                   /note="Histone H2A deubiquitinase MYSM1"
FT                   /id="PRO_0000234075"
FT   DOMAIN          117..168
FT                   /note="SANT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   DOMAIN          374..472
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT   DOMAIN          579..711
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           658..671
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           776..780
FT                   /note="LXXLL motif"
FT   COMPBIAS        167..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         658
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         660
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         671
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   832 AA;  94556 MW;  757AE9CA3C19DC57 CRC64;
     MAAEEPEVDV EGDLAAAPGE AASEGHENTA SSLLQDHYLD SSWRTDNSLP WTLDSSISEE
     NRAVIEKMLL EEEYYLSNKS LSEKIWLSQK EAEKRSVKSP HKKTGKVMVR SPTKPGSYSL
     KWTSEEKELF EQGLVKYGRR WTKIAKLIGS RTVLQVKSYA RQYFKNKAKN DGSEREEQSQ
     HGGTLPTEDG VRVEAWSAGN LRGRADPNLN AVKIEKLSDD EEVDITDDMD ELFSPAFQQG
     VGKSELSIIS ESPAEETKGT EHPFPHVGHS SAVSLLKEDP QNTKQPTVDA LLFQDGAATC
     SQHVNGDKSV NLEYQQCNDF IEKAEQGRTG MSHGARQITD QELNEEQRDL ADNGLLFHPP
     CQVDEDHQEE AEALKPPDQE VEIDRSIILE EEKQAIPEFF EGRQAKTPER YLKIRNYILD
     QWERCKPKYL NKTSVRPGLK NCGDVNCIGR IHTYLELIGA INFGCEQAVY NRPQPADKTR
     SKEGKDTVEA YQLAQRLQSM RTRRRRVRDP WGNWCDAKDL EGQTFEHLSA EELARRREEE
     KLKPSKSSKG SRQIKSSFDP FQLIPCCLFT EEKQEPFQVK VSSEALLIMD LHSHVSMAEV
     IGLLGGRYSE ADKVVEVCAA EPCNSLSTGL QCEMDPVSQT QASETLAARG YSVIGWYHSH
     PAFDPNPSIR DIDTQAKYQS YFSRGGAMFI GMIVSPYNRN NPLPYSQITC LVISDEISSD
     GSYRLPYKFE IQQMLEEPQW ELIFEKTRWI IEKYRFCHSS VPMDKIFHRD SDLTCLQKLL
     ECMRKTLGKV TNCFIAEEFL TQIENLFVSM YKSEKKSNAE ENKNEHSSEL ES