P31369 (PDM2A_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Homeobox
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	central nervous system development Inferred from mutant phenotype Ref.3. Source: UniProtKB ectoderm development Inferred from mutant phenotype Ref.3. Source: UniProtKB neuroblast development Inferred from mutant phenotype. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred by curator Ref.3. Source: UniProtKB
Molecular function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 498	498	POU domain protein 2, isoform A		PRO_0000100778
Regions
	Domain	286 – 360	75	POU-specific
	DNA binding	391 – 450	60	Homeobox
	Compositional bias	5 – 10	6	Poly-Gln
	Compositional bias	74 – 79	6	Poly-Glu
Amino acid modifications
	Modified residue	72	1	Phosphoserine Ref.8
	Modified residue	211	1	Phosphoserine Ref.8
	Modified residue	215	1	Phosphoserine Ref.8
	Modified residue	217	1	Phosphoserine Ref.8
	Modified residue	219	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	221 – 224	4	VPRH → GAPAR in AAA28481. Ref.2
	Sequence conflict	248	1	M → S in AAA28732. Ref.4
	Sequence conflict	447	1	K → N in AAA28732. Ref.4
	Sequence conflict	472 – 474	3	PQA → RRL in AAA28481. Ref.2
	Sequence conflict	475 – 498	24	Missing in AAA28481. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 60F17AF776603974	FASTA	498	55,463
	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
	Isoform B [UniParc]. See Q9VK71.		–	–

References

	« Hide 'large scale' referencesShow '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: 1685891] [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: 1881906] [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: 1496003] [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. , 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: 10731132] [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. , 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: 12537572] [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. , 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: 1680380] [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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-211; SER-215; SER-217 AND SER-219, 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.
PIR	A56564.
RefSeq	NP_523558.2. NM_078834.2.
UniGene	Dm.4704.
3D structure databases
ProteinModelPortal	P31369.
SMR	P31369. Positions 289-451.
ModBase	Search...
Protein-protein interaction databases
STRING	P31369.
Proteomic databases
PRIDE	P31369.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0080393; FBpp0079974; FBgn0004394.
GeneID	34673.
KEGG	dme:Dmel_CG12287.
NMPDR	fig|7227.3.peg.2155.
Organism-specific databases
CTD	34673.
FlyBase	FBgn0004394. pdm2.
Phylogenomic databases
eggNOG	meNOG09020.
GeneTree	EMGT00050000001591.
InParanoid	P31369.
OrthoDB	EOG4KWH7V.
Gene expression databases
ArrayExpress	P31369.
Bgee	P31369.
GermOnline	CG12287. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001356. Homeobox. IPR017970. Homeobox_CS. IPR009057. Homeodomain-like. IPR012287. Homeodomain-rel. IPR010982. Lambda_DNA-bd. IPR013847. POU. IPR000327. POU_specific. [Graphical view]
Gene3D	G3DSA:1.10.260.40. G3DSA:1.10.260.40. 1 hit. G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
KO	K09364.
Pfam	PF00046. Homeobox. 1 hit. PF00157. Pou. 1 hit. [Graphical view]
PRINTS	PR00028. POUDOMAIN.
SMART	SM00389. HOX. 1 hit. SM00352. POU. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit. SSF47413. Lambda_like_DNA. 1 hit.
PROSITE	PS00027. 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]
ProtoNet	Search...
Other
NextBio	789620.

Entry information

Entry name

PDM2A_DROME

Accession

Primary (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:	January 25, 2012
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project