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Database: UniProt
Entry: A0A670K9W6_PODMU
LinkDB: A0A670K9W6_PODMU
Original site: A0A670K9W6_PODMU 
ID   A0A670K9W6_PODMU        Unreviewed;       487 AA.
AC   A0A670K9W6;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Doublesex and mab-3 related transcription factor 3 {ECO:0000313|Ensembl:ENSPMRP00000033140.1};
GN   Name=DMRT3 {ECO:0000313|Ensembl:ENSPMRP00000033140.1};
OS   Podarcis muralis (Wall lizard) (Lacerta muralis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC   Lacertibaenia; Lacertidae; Podarcis.
OX   NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000033140.1, ECO:0000313|Proteomes:UP000472272};
RN   [1] {ECO:0000313|Ensembl:ENSPMRP00000033140.1, ECO:0000313|Proteomes:UP000472272}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA   Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA   Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA   Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA   Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA   Andersson L., Carneiro M.;
RT   "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT   polymorphisms in the wall lizard.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN   [2] {ECO:0000313|Ensembl:ENSPMRP00000033140.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A670K9W6; -.
DR   Ensembl; ENSPMRT00000035158.1; ENSPMRP00000033140.1; ENSPMRG00000021491.1.
DR   GeneTree; ENSGT00940000160420; -.
DR   OMA; RWASEPQ; -.
DR   OrthoDB; 2915919at2759; -.
DR   Proteomes; UP000472272; Chromosome 17.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd14419; CUE_DMA_DMRTA3; 1.
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; IPR005173; DMA.
DR   InterPro; IPR026607; DMRT.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR12322; DOUBLESEX AND MAB-3 RELATED TRANSCRIPTION FACTOR DMRT; 1.
DR   PANTHER; PTHR12322:SF120; DOUBLESEX- AND MAB-3-RELATED TRANSCRIPTION FACTOR 3; 1.
DR   Pfam; PF00751; DM; 1.
DR   Pfam; PF03474; DMA; 1.
DR   SMART; SM00301; DM; 1.
DR   SUPFAM; SSF82927; Cysteine-rich DNA binding domain, (DM domain); 1.
DR   SUPFAM; SSF46934; UBA-like; 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:UP000472272};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00070}.
FT   DOMAIN          29..76
FT                   /note="DM"
FT                   /evidence="ECO:0000259|PROSITE:PS50809"
FT   DNA_BIND        29..76
FT                   /note="DM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00070"
FT   REGION          152..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  52107 MW;  66C5CEC4C814582C CRC64;
     MNGYGSPYLY MGGPVAPPAR APLQRTPKCA RCRNHGVLSW LKGHKRYCRF KDCTCEKCIL
     IIERQRVMAA QVALRRQQAN ESLESLIPDA LRALPAAAAA APGSAGATTT GHPGVGAAAG
     AAAAAVAPSE GPPGTPHRPP MELAAAALRW ASEQPAAVQP PQLPKADMTE DRLGDASGVD
     SAETYSDKDA DQRSTPDLTK AKSGFAPESP EIVSVDEGGY AIQKNSGSTD SRPESPKYQP
     EPNHLLIEGP SGTVSLPFGL KANRPPLEVL KKIFPNQKPT VLELILKGCG GDLVSAVEVL
     LSSRSSIAGG DRTSAESEGL VLPSNGHLFE HTLGSYPISS SKWSVGSAFR VPDTLRFSAD
     ASNVVPNPLA VPLQHPFPQP PRYPLMLRNT LARNQSSPFL PNDVTLWNTM TLQQQYQLRS
     QYVSPFSTNT TSVFRSSPVL PTRPSEDPRI SIPDDGCPIV SKQPIYTEDD YDERSDSSDS
     RILNTSS
//
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