ID F6YWN9_CIOIN Unreviewed; 625 AA.
AC F6YWN9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DM domain-containing protein {ECO:0000259|PROSITE:PS50809};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000024566.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000024566.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00070}.
CC -!- SIMILARITY: Belongs to the DMRT family.
CC {ECO:0000256|ARBA:ARBA00006834}.
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DR EMBL; EAAA01002575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6YWN9; -.
DR STRING; 7719.ENSCINP00000024566; -.
DR Ensembl; ENSCINT00000024812.2; ENSCINP00000024566.2; ENSCING00000013359.2.
DR GeneTree; ENSGT00940000156282; -.
DR HOGENOM; CLU_437393_0_0_1; -.
DR InParanoid; F6YWN9; -.
DR TreeFam; TF317837; -.
DR Proteomes; UP000008144; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; IBA:GO_Central.
DR Gene3D; 4.10.1040.10; DM DNA-binding domain; 1.
DR InterPro; IPR001275; DM_DNA-bd.
DR InterPro; IPR036407; DM_DNA-bd_sf.
DR InterPro; IPR026607; DMRT.
DR PANTHER; PTHR12322; DOUBLESEX AND MAB-3 RELATED TRANSCRIPTION FACTOR DMRT; 1.
DR PANTHER; PTHR12322:SF116; DOUBLESEX- AND MAB-3-RELATED TRANSCRIPTION FACTOR 1; 1.
DR Pfam; PF00751; DM; 1.
DR SMART; SM00301; DM; 1.
DR SUPFAM; SSF82927; Cysteine-rich DNA binding domain, (DM domain); 1.
DR PROSITE; PS40000; DM_1; 1.
DR PROSITE; PS50809; DM_2; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00070};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00070}; Reference proteome {ECO:0000313|Proteomes:UP000008144};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00070}.
FT DOMAIN 42..90
FT /note="DM"
FT /evidence="ECO:0000259|PROSITE:PS50809"
FT DNA_BIND 42..90
FT /note="DM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00070"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 69562 MW; 34847D3A2CC16C91 CRC64;
MKPVADSSPV GADTSSDFPS SIPNEFQQVA GASRKPLRTP KCARCRNHGV VSTLKGHKRH
CRWRDCQCSN CLLVVERQRI MAAQQAADVK KSGRSDSETS SPVGEKEDAA VDVGLMEDAA
ASLRIRNKKQ AAPHESIARH ILPPISERMR KRRAFADKEL DDAMMRREMN SRCGIFPHNP
TNIASVLNVN SDISPYAALL RASHNPYVLN TEATELSDGL TSPDITVDHL VDHQTSGKLK
LDVESGPRNK RPRHSSRQNV YKSKLSNESE VRDAAVNKNT GETNKDTPMG NNPYQADTAE
GRTRKQRINF LSIMFPTCDP ATLERALGIY ENPYSPANSL DSAAFDAGGK ARTEGSFSFC
NDPMCNSIYP KFLSSMPHLN ASCPSSRHNK GIIGATYDSV HAENIKPYIY PYHALPTPMF
AQKIHFDESC NSDRIFPNFR RMDDAARHNE EFRACMLQQY TAAINNSLPF APVFATSRHF
PVDADCPVSK DIGRFRSEIA SKLHSRKEIL TLPNKSVTLA GCEEINKLTA KQRNDAVTPR
PQFTVAKYQD EKINGLDSVK QEKRCNLEQN GDDPDLPRAV VCSTDHTTES RYKWNSASQR
RICKNQRSNK LTSFTVQSIM GNASS
//
