MYBA_XENLA
ID MYBA_XENLA Reviewed; 728 AA.
AC Q05935;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Myb-related protein A;
DE Short=A-Myb;
DE Short=xAMYB;
DE AltName: Full=Myb-like protein 1;
DE AltName: Full=Myb-related protein 2;
DE AltName: Full=XMYB2;
GN Name=mybl1; Synonyms=amyb, myb2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8510936;
RA Sleeman J.P.;
RT "Xenopus A-myb is expressed during early spermatogenesis.";
RL Oncogene 8:1931-1941(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-181, AND DEVELOPMENTAL STAGE.
RX PubMed=1606020; DOI=10.1016/0925-4773(92)90015-c;
RA Bouwmeester T., Guehmann S., El-Baradi T., Kalkbrenner F., van Wijk I.,
RA Moelling K., Pieler T.;
RT "Molecular cloning, expression and in vitro functional characterization of
RT Myb-related proteins in Xenopus.";
RL Mech. Dev. 37:57-68(1992).
CC -!- FUNCTION: Transcription factor that specifically recognizes the
CC sequence 5'-YAAC[GT]G-3'. Acts as a master regulator of male meiosis by
CC promoting expression of piRNAs. The piRNA metabolic process mediates
CC the repression of transposable elements during meiosis by forming
CC complexes composed of piRNAs and Piwi proteins and governs the
CC methylation and subsequent repression of transposons, which is
CC essential for the germline integrity. {ECO:0000250|UniProtKB:P51960}.
CC -!- SUBUNIT: Component of the DREAM complex.
CC {ECO:0000250|UniProtKB:P10243}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51960}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early spermatogenesis.
CC {ECO:0000269|PubMed:1606020}.
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DR EMBL; X72620; CAA51196.1; -; mRNA.
DR EMBL; M75871; AAA49904.1; -; mRNA.
DR PIR; S36095; S36095.
DR RefSeq; NP_001081179.1; NM_001087710.1.
DR AlphaFoldDB; Q05935; -.
DR SMR; Q05935; -.
DR GeneID; 397697; -.
DR KEGG; xla:397697; -.
DR CTD; 397697; -.
DR Xenbase; XB-GENE-986561; mybl1.L.
DR OrthoDB; 219341at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397697; Expressed in testis and 13 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR015395; C-myb_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR012642; Tscrpt_reg_Wos2-domain.
DR Pfam; PF09316; Cmyb_C; 1.
DR Pfam; PF07988; LMSTEN; 1.
DR Pfam; PF00249; Myb_DNA-binding; 3.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 3.
PE 2: Evidence at transcript level;
KW Activator; Differentiation; DNA-binding; Nucleus; Reference proteome;
KW Repeat; Spermatogenesis; Transcription; Transcription regulation.
FT CHAIN 1..728
FT /note="Myb-related protein A"
FT /id="PRO_0000197057"
FT DOMAIN 30..80
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 81..136
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 137..187
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 57..80
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 109..132
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 160..183
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..293
FT /note="Transcriptional activation domain"
FT /evidence="ECO:0000250"
FT REGION 296..534
FT /note="Negative regulatory domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 83577 MW; 7A360CBA51AC0797 CRC64;
MAGRARSEDE EEDGQFTEHD YDVSLQKGPK KPWSKLRWTK DEDDKVKKLV EKHGEDWGVV
ARHFINRSEV QCQHRWHKVL SPELVKGPWT KEEDQRVIEL VHKYGPKKWS IIAKHLKGRI
GKQCRERWHN HLNPDVKKSS WTEEEDRIIY SAHKRMGNRW AEIAKLLPGR TDNSIKNHWN
STMKRKVEQE GYLQDLMNCD RPSKLQAKSC AAPNHLQAQN QFYIPVQTQI PRYSSLSHDD
NCIEIQNSFS FIQQPFVDAD DPEKEKRIKE LELLLMSAEN EVRRKRVPSG SSLTWSESYH
MGESMSNTMS HLEEQTHDFY SLDEIPNTSG QQSVEDKILA PEANIVLQPL ETIPEFSETL
ELIDVDTVDW NNIESFELPF TASPAKHTPM KWIHEISPEC ALNSCLVQAD GRGSASRVLS
SSPAMPKFYS PPTILRKKKI HPDLSLTPEV RDASNVVLKG TPVKTRQYSP LQLFRSGNVQ
NHLNLDNLPL TSTPVCGQKI SATPLQRQIT PKKDKENAGF RTPTIRRSLM AVTPRTPTPF
KNALAAQEKK YGPLRTVMQP LIFVEEDIME VLKKETEKDV FIKEEKESDC KPMKQEHVST
VRKVRKSLIL DSCDKEELGA DFLAPDEVSQ SQNGNTLPTS FLMIPLGERQ DQKCDENTDT
RKGSVMQRKN YIPATRNVKL QSSVQPLCEW EAVVYGKTED QLIMTEQARR YLDTYKPTSS
SGLRHLIL
