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PDM2A_DROME
ID   PDM2A_DROME             Reviewed;         498 AA.
AC   P31369; Q24430; Q6NR41; Q9VK70;
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=POU domain protein 2, isoform A;
DE   AltName: Full=Miti-mere;
DE   AltName: Full=Pdm-2;
DE   AltName: Full=Protein didymous;
DE   AltName: Full=dOct2;
DE   AltName: Full=dPOU-28;
GN   Name=pdm2; Synonyms=dim, OCT2, pdm-2, POU-28; ORFNames=CG12287;
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, 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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=1496003; DOI=10.1073/pnas.89.15.7080;
RA   Prakash K., Fang X.D., Engelberg D., Behal A., Parker C.S.;
RT   "dOct2, a Drosophila Oct transcription factor that functions in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7080-7084(1992).
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, AND ALTERNATIVE SPLICING.
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;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 68-498, FUNCTION, TISSUE SPECIFICITY, AND
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-211; SER-215; SER-217
RP   AND SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: DNA-binding regulatory protein implicated in early
CC       development. Involved in neuronal cell fate decision. May act as an
CC       octamer-dependent activator of transcription. Could also play an early
CC       role in specific ectodermal cells, and a subsequent role in the
CC       embryonic nervous system. {ECO:0000269|PubMed:1496003,
CC       ECO:0000269|PubMed:1680380, ECO:0000269|PubMed:1685891,
CC       ECO:0000269|PubMed:1881906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P31369-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q9VK71-1; Sequence=External;
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:1496003, ECO:0000269|PubMed:1680380,
CC       ECO:0000269|PubMed:1685891, ECO:0000269|PubMed:1881906}.
CC   -!- DEVELOPMENTAL STAGE: Expressed primarily during the first half of
CC       embryogenesis. {ECO:0000269|PubMed:1680380,
CC       ECO:0000269|PubMed:1685891}.
CC   -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ23557.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; S80559; AAB21408.1; -; mRNA.
DR   EMBL; M65016; AAA28481.1; -; mRNA.
DR   EMBL; M93149; AAA28732.1; -; mRNA.
DR   EMBL; AE014134; AAF53209.1; -; Genomic_DNA.
DR   EMBL; BT010239; AAQ23557.1; ALT_FRAME; mRNA.
DR   EMBL; M81958; AAA28830.2; -; Transcribed_RNA.
DR   PIR; A56564; A56564.
DR   RefSeq; NP_523558.2; NM_078834.3. [P31369-1]
DR   AlphaFoldDB; P31369; -.
DR   SMR; P31369; -.
DR   BioGRID; 60717; 13.
DR   IntAct; P31369; 7.
DR   iPTMnet; P31369; -.
DR   DNASU; 34673; -.
DR   EnsemblMetazoa; FBtr0080393; FBpp0079974; FBgn0004394. [P31369-1]
DR   GeneID; 34673; -.
DR   CTD; 34673; -.
DR   FlyBase; FBgn0004394; pdm2.
DR   VEuPathDB; VectorBase:FBgn0004394; -.
DR   GeneTree; ENSGT00940000168873; -.
DR   HOGENOM; CLU_013065_7_2_1; -.
DR   BioGRID-ORCS; 34673; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 34673; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0004394; Expressed in presumptive embryonic/larval nervous system and 99 other tissues.
DR   ExpressionAtlas; P31369; baseline and differential.
DR   Genevisible; P31369; DM.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
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:0007417; P:central nervous system development; IMP:UniProtKB.
DR   GO; GO:0007398; P:ectoderm development; IMP:UniProtKB.
DR   GO; GO:0048699; P:generation of neurons; IMP:FlyBase.
DR   GO; GO:0014019; P:neuroblast development; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   Activator; Alternative splicing; Developmental protein; DNA-binding;
KW   Homeobox; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..498
FT                   /note="POU domain protein 2, isoform A"
FT                   /id="PRO_0000100778"
FT   DOMAIN          286..360
FT                   /note="POU-specific"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT   DNA_BIND        391..450
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        221..224
FT                   /note="VPRH -> GAPAR (in Ref. 2; AAA28481)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="M -> S (in Ref. 4; AAA28732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        447
FT                   /note="K -> N (in Ref. 4; AAA28732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        472..474
FT                   /note="PQA -> RRL (in Ref. 2; AAA28481)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        475..498
FT                   /note="Missing (in Ref. 2; AAA28481)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   498 AA;  55463 MW;  60F17AF776603974 CRC64;
     MMVLQQQQQQ RLWDATTTSN TNTQTQQSAN VESTPTKVCH QENAATHTFM RHMSNSPTPP
     SPLRSLSDCG KSFEEEELEL GENCEMPQNL SSKRQARELD SELENEVLDL APPPKRLAEE
     QEEEKVASVN PPQPVAFAPE EMHQALQLQL HSYIEMVRQL APEAFPNPNL ATQFLLQNSL
     QALAQFQALQ QMKQQQREDP LPSYSTPLAK SPLRSPSLSP VPRHSKSQQR TPPNSMTANS
     LGMSSAVMTP NTPSMQQQPQ LQQSTPKPTS GLTVASAMAK LEQSPEETTD LEELEQFAKT
     FKQRRIKLGF TQGDVGLAMG KLYGNDFSQT TISRFEALNL SFKNMCKLKP LLQKWLEDAD
     STVAKSGGGV FNINTMTSTL SSTPESILGR RRKKRTSIET TVRTTLEKAF LMNCKPTSEE
     ISQLSERLNM DKEVIRVWFC NRRQKEKRIN PSLDLDSPTG TPLSSHAFGY PPQALNMSHM
     QMEGGSGSFC GSSISSGE
 
 
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