PDM1_DROME
ID PDM1_DROME Reviewed; 601 AA.
AC P31368; Q9VK74;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Protein nubbin;
DE AltName: Full=POU domain protein 1;
DE Short=PDM-1;
DE AltName: Full=Protein twain;
DE AltName: Full=dOCT1;
DE AltName: Full=dPOU-19;
GN Name=nub; Synonyms=OCT1, pdm-1, POU-19, TWN; ORFNames=CG34395;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=1680380; DOI=10.1016/0925-4773(91)90045-8;
RA Billin A.N., Cockerill K.A., Poole S.J.;
RT "Isolation of a family of Drosophila POU domain genes expressed in early
RT development.";
RL Mech. Dev. 34:75-84(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=1685891; DOI=10.1016/0925-4773(91)90075-h;
RA Lloyd A., Sakonju S.;
RT "Characterization of two Drosophila POU domain genes, related to oct-1 and
RT oct-2, and the regulation of their expression patterns.";
RL Mech. Dev. 36:87-102(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1881906; DOI=10.1073/pnas.88.17.7645;
RA Dick T., Yang X., Yeo S., Chia W.;
RT "Two closely linked Drosophila POU domain genes are expressed in
RT neuroblasts and sensory elements.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7645-7649(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: DNA-binding regulatory protein implicated in early
CC development. Involved in neuronal cell fate decision. Repressed
CC directly or indirectly by the BX-C homeotic proteins.
CC {ECO:0000269|PubMed:1680380, ECO:0000269|PubMed:1685891,
CC ECO:0000269|PubMed:1881906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:1881906}.
CC -!- TISSUE SPECIFICITY: Initial expression in cellular blastoderm stage,
CC then in ectodermal stripes during germband extension. Broad expression
CC in the neuroectoderm followed by limitation to discrete subsets of CNS
CC cells, and expression in specific PNS neurons and support cells.
CC {ECO:0000269|PubMed:1685891, ECO:0000269|PubMed:1881906}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:1680380, ECO:0000269|PubMed:1685891,
CC ECO:0000269|PubMed:1881906}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC subfamily. {ECO:0000305}.
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DR EMBL; M81957; AAA28829.1; -; mRNA.
DR EMBL; S80561; AAB21409.1; -; mRNA.
DR EMBL; M65015; AAA28480.1; -; mRNA.
DR EMBL; AE014134; AAF53205.2; -; Genomic_DNA.
DR EMBL; AY118387; AAM48416.1; -; mRNA.
DR PIR; B56564; B56564.
DR RefSeq; NP_001285876.1; NM_001298947.1.
DR RefSeq; NP_476659.1; NM_057311.5.
DR AlphaFoldDB; P31368; -.
DR SMR; P31368; -.
DR BioGRID; 60715; 34.
DR IntAct; P31368; 5.
DR STRING; 7227.FBpp0111554; -.
DR PaxDb; P31368; -.
DR PRIDE; P31368; -.
DR DNASU; 34669; -.
DR EnsemblMetazoa; FBtr0112643; FBpp0111555; FBgn0085424.
DR EnsemblMetazoa; FBtr0342628; FBpp0309559; FBgn0085424.
DR GeneID; 34669; -.
DR KEGG; dme:Dmel_CG34395; -.
DR CTD; 34669; -.
DR FlyBase; FBgn0085424; nub.
DR VEuPathDB; VectorBase:FBgn0085424; -.
DR eggNOG; KOG3802; Eukaryota.
DR HOGENOM; CLU_013065_7_1_1; -.
DR InParanoid; P31368; -.
DR OMA; MMQNRYI; -.
DR PhylomeDB; P31368; -.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR SignaLink; P31368; -.
DR BioGRID-ORCS; 34669; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34669; -.
DR PRO; PR:P31368; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0085424; Expressed in presumptive embryonic/larval nervous system and 90 other tissues.
DR ExpressionAtlas; P31368; baseline and differential.
DR Genevisible; P31368; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0035107; P:appendage morphogenesis; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0002809; P:negative regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IGI:FlyBase.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..601
FT /note="Protein nubbin"
FT /id="PRO_0000100777"
FT DOMAIN 421..495
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 523..582
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 420
FT /note="P -> R (in Ref. 2; AAB21409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 65202 MW; 8FFCD7B3C162D2B2 CRC64;
MVMSELRWHT ASPEDNKNSL KRDLLKSTPT SAREAAVHIM QNRYISRLSR SPSPLQSNAS
DCDDNNSSVG TSSDRCRSPL SPALSLSHQQ AKRQLMSLQP HPAHHHHNPH HLNHLNHHQY
KQEEDYDDAN GGALNLTSDN SRHSTQSPSN SVKSATASPV PVISVPSPVP PMISPVLAPS
GCGSTTPNSM AAAAAAAAAV ASTMGSGISP LLALPGMSSP QAQLAAAGLG MNNPLLTGSL
SPQDFAQFHQ LLQQRQVALT QQFNSYMELL RSGSLGLAQD DPALTAQVAA AQFLMQSQLQ
ALSQASQQLQ ALQKQQQRQV DEPLQLNHKM TQQPRSSTPH SIRSPIAIRS PASSPQQLHH
HHHHPLQITP PSSAASLKLS GMLTPSTPTS GTQMSQGTTT PQPKTVASAA AARAAGEPSP
EETTDLEELE QFAKTFKQRR IKLGFTQGDV GLAMGKLYGN DFSQTTISRF EALNLSFKNM
CKLKPLLQKW LDDADRTIQA TGGVFDPAAL QATVSTPEII GRRRKKRTSI ETTIRGALEK
AFLANQKPTS EEITQLADRL SMEKEVVRVW FCNRRQKEKR INPSLDSPTG ADDDESSYMM
H
