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P31369 (PDM2A_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
POU domain protein 2, isoform A
Alternative name(s):
Miti-mere
Pdm-2
Protein didymous
dOct2
dPOU-28
Gene names
Name:pdm2
Synonyms:dim, OCT2, pdm-2, POU-28
ORF Names:CG12287
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-binding regulatory protein implicated in early development. Involved in neuronal cell fate decision. May act as an octamer-dependent activator of transcription. Could also play an early role in specific ectodermal cells, and a subsequent role in the embryonic nervous system. Ref.1 Ref.2 Ref.3 Ref.7

Subcellular location

Nucleus.

Tissue specificity

Initial expression in cellular blastoderm stage, then in ectodermal stripes during germband extension. Broad expression in the neuroectoderm followed by limitation to discrete subsets of CNS cells, and expression in specific PNS neurons and support cells. Ref.1 Ref.2 Ref.3 Ref.7

Developmental stage

Expressed primarily during the first half of embryogenesis. Ref.1 Ref.7

Sequence similarities

Belongs to the POU transcription factor family. Class-2 subfamily.

Contains 1 homeobox DNA-binding domain.

Contains 1 POU-specific domain.

Sequence caution

The sequence AAQ23557.1 differs from that shown. Reason: Frameshift at position 95.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P31369-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q9VK71-1)

The sequence of this isoform can be found in the external entry Q9VK71.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498POU domain protein 2, isoform A
PRO_0000100778

Regions

Domain286 – 36075POU-specific
DNA binding391 – 45060Homeobox
Compositional bias5 – 106Poly-Gln
Compositional bias74 – 796Poly-Glu

Amino acid modifications

Modified residue721Phosphoserine Ref.8
Modified residue2111Phosphoserine Ref.8
Modified residue2151Phosphoserine Ref.8
Modified residue2171Phosphoserine Ref.8
Modified residue2191Phosphoserine Ref.8

Experimental info

Sequence conflict221 – 2244VPRH → GAPAR in AAA28481. Ref.2
Sequence conflict2481M → S in AAA28732. Ref.4
Sequence conflict4471K → N in AAA28732. Ref.4
Sequence conflict472 – 4743PQA → RRL in AAA28481. Ref.2
Sequence conflict475 – 49824Missing in AAA28481. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 60F17AF776603974

FASTA49855,463
        10         20         30         40         50         60 
MMVLQQQQQQ RLWDATTTSN TNTQTQQSAN VESTPTKVCH QENAATHTFM RHMSNSPTPP 

        70         80         90        100        110        120 
SPLRSLSDCG KSFEEEELEL GENCEMPQNL SSKRQARELD SELENEVLDL APPPKRLAEE 

       130        140        150        160        170        180 
QEEEKVASVN PPQPVAFAPE EMHQALQLQL HSYIEMVRQL APEAFPNPNL ATQFLLQNSL 

       190        200        210        220        230        240 
QALAQFQALQ QMKQQQREDP LPSYSTPLAK SPLRSPSLSP VPRHSKSQQR TPPNSMTANS 

       250        260        270        280        290        300 
LGMSSAVMTP NTPSMQQQPQ LQQSTPKPTS GLTVASAMAK LEQSPEETTD LEELEQFAKT 

       310        320        330        340        350        360 
FKQRRIKLGF TQGDVGLAMG KLYGNDFSQT TISRFEALNL SFKNMCKLKP LLQKWLEDAD 

       370        380        390        400        410        420 
STVAKSGGGV FNINTMTSTL SSTPESILGR RRKKRTSIET TVRTTLEKAF LMNCKPTSEE 

       430        440        450        460        470        480 
ISQLSERLNM DKEVIRVWFC NRRQKEKRIN PSLDLDSPTG TPLSSHAFGY PPQALNMSHM 

       490 
QMEGGSGSFC GSSISSGE 

« Hide

Isoform B [UniParc].

See Q9VK71.

References

« Hide 'large scale' references
[1]"Characterization of two Drosophila POU domain genes, related to oct-1 and oct-2, and the regulation of their expression patterns."
Lloyd A., Sakonju S.
Mech. Dev. 36:87-102(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]"Two closely linked Drosophila POU domain genes are expressed in neuroblasts and sensory elements."
Dick T., Yang X., Yeo S., Chia W.
Proc. Natl. Acad. Sci. U.S.A. 88:7645-7649(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Embryo.
[3]"dOct2, a Drosophila Oct transcription factor that functions in yeast."
Prakash K., Fang X.D., Engelberg D., Behal A., Parker C.S.
Proc. Natl. Acad. Sci. U.S.A. 89:7080-7084(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Embryo.
[4]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[5]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[6]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[7]"Isolation of a family of Drosophila POU domain genes expressed in early development."
Billin A.N., Cockerill K.A., Poole S.J.
Mech. Dev. 34:75-84(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-498, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Oregon-R.
Tissue: Embryo.
[8]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-211; SER-215; SER-217 AND SER-219, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S80559 mRNA. Translation: AAB21408.1.
M65016 mRNA. Translation: AAA28481.1.
M93149 mRNA. Translation: AAA28732.1.
AE014134 Genomic DNA. Translation: AAF53209.1.
BT010239 mRNA. Translation: AAQ23557.1. Frameshift.
M81958 Transcribed RNA. Translation: AAA28830.2.
PIRA56564.
RefSeqNP_523558.2. NM_078834.2.
UniGeneDm.4704.

3D structure databases

ProteinModelPortalP31369.
SMRP31369. Positions 289-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60717. 1 interaction.

Proteomic databases

PaxDbP31369.
PRIDEP31369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080393; FBpp0079974; FBgn0004394. [P31369-1]
GeneID34673.
KEGGdme:Dmel_CG12287.

Organism-specific databases

CTD34673.
FlyBaseFBgn0004394. pdm2.

Phylogenomic databases

eggNOGNOG267922.
GeneTreeENSGT00750000117373.
InParanoidP31369.
KOK09364.
OrthoDBEOG7DJSMG.

Gene expression databases

BgeeP31369.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
1.10.260.40. 1 hit.
InterProIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
IPR013847. POU.
IPR000327. POU_specific.
[Graphical view]
PfamPF00046. Homeobox. 1 hit.
PF00157. Pou. 1 hit.
[Graphical view]
PRINTSPR00028. POUDOMAIN.
SMARTSM00389. HOX. 1 hit.
SM00352. POU. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 1 hit.
PROSITEPS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
PS00035. POU_1. 1 hit.
PS00465. POU_2. 1 hit.
PS51179. POU_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi34673.
NextBio789620.

Entry information

Entry namePDM2A_DROME
AccessionPrimary (citable) accession number: P31369
Secondary accession number(s): Q24430, Q6NR41, Q9VK70
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase