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P91943 (PANG1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein pangolin, isoforms A/H/I/S
Alternative name(s):
dTCF
Gene names
Name:pan
Synonyms:TCF
ORF Names:CG34403
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length751 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Segment polarity protein. Functions together with arm to transduce the Wingless (Wg) signal in embryos and in developing adult tissues. Acts as a transcriptional activator, but in the absence of arm, it binds to gro and acts as a transcriptional repressor of wg-responsive genes. Ref.1 Ref.2 Ref.7

Subunit structure

Binds to the beta-catenin homolog arm or to gro. Ref.7

Subcellular location

Nucleus Ref.7.

Disruption phenotype

Flies exhibit a segment polarity phenotype and altered expression of the wg target genes en and Ubx. Ref.1

Sequence similarities

Belongs to the TCF/LEF family.

Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
Repressor
Segmentation polarity protein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Traceable author statement PubMed 10973066. Source: FlyBase

canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic pattern specification

Inferred from mutant phenotype PubMed 12730381. Source: FlyBase

heart development

Inferred from mutant phenotype PubMed 22398840. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 12730381. Source: FlyBase

mesodermal cell fate determination

Traceable author statement PubMed 12027431. Source: FlyBase

negative regulation of Wnt signaling pathway

Non-traceable author statement PubMed 12147138. Source: FlyBase

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.1. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 16828735. Source: FlyBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15043810. Source: FlyBase

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.1. Source: UniProtKB

regulation of Wnt signaling pathway

Inferred from mutant phenotype PubMed 17267442. Source: FlyBase

regulation of hemocyte differentiation

Inferred from mutant phenotype PubMed 15381778. Source: FlyBase

regulation of stem cell proliferation

Inferred from mutant phenotype PubMed 18633350. Source: FlyBase

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.1. Source: UniProtKB

salivary gland morphogenesis

Inferred from mutant phenotype PubMed 17507403. Source: FlyBase

segment polarity determination

Inferred from electronic annotation. Source: UniProtKB-KW

spiracle morphogenesis, open tracheal system

Inferred from mutant phenotype PubMed 15930099. Source: FlyBase

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12482712. Source: GOC

   Cellular_componentmicrotubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

nucleus

Inferred from direct assay PubMed 98454907. Source: UniProtKB

transcription factor complex

Inferred from physical interaction PubMed 20439429. Source: FlyBase

   Molecular_functionRNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12482712. Source: FlyBase

beta-catenin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

kinase binding

Inferred from physical interaction PubMed 19088090. Source: FlyBase

protein binding

Inferred from physical interaction PubMed 9751710. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction PubMed 20439429. Source: FlyBase

sequence-specific DNA binding

Inferred from direct assay PubMed 11076769. Source: FlyBase

transcription regulatory region DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P91943-3)

Also known as: C; D; E; F; G;

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 H (identifier: P91943-4)

The sequence of this isoform differs from the canonical sequence as follows:
     313-364: ELSREEQSKY...RKKDRSTTDS → ALGREEQAKY...KRKRKQDTND
Note: No experimental confirmation available.
Isoform S (identifier: P91943-6)

The sequence of this isoform differs from the canonical sequence as follows:
     713-730: Missing.
Note: No experimental confirmation available.
Isoform I (identifier: P91943-5)

The sequence of this isoform differs from the canonical sequence as follows:
     313-364: ELSREEQSKY...RKKDRSTTDS → ALGREEQAKY...KRKRKQDTND
     390-414: RKKKCIRYMEALNGNGPAEDGSCFD → YVLPLFLFTMLYILLQMDLQDSRKN
     415-751: Missing.
Note: No experimental confirmation available.
Isoform J (identifier: Q8IMA8-1)

The sequence of this isoform can be found in the external entry Q8IMA8.
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 – 751751Protein pangolin, isoforms A/H/I/S
PRO_0000048601

Regions

DNA binding273 – 34169HMG box
Region1 – 5353Beta-catenin binding site By similarity
Motif351 – 3577Nuclear localization signal Potential
Compositional bias351 – 3577Poly-Lys

Natural variations

Alternative sequence313 – 36452ELSRE…STTDS → ALGREEQAKYYELARRERQL HMQMYPDWSSRTNASRGKKR KRKQDTND in isoform H and isoform I.
VSP_021967
Alternative sequence390 – 41425RKKKC…GSCFD → YVLPLFLFTMLYILLQMDLQ DSRKN in isoform I.
VSP_021968
Alternative sequence415 – 751337Missing in isoform I.
VSP_021969
Alternative sequence713 – 73018Missing in isoform S.
VSP_047713

Sequences

Sequence LengthMass (Da)Tools
Isoform A (C) (D) (E) (F) (G) [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1C6E5A0B36017143

FASTA75181,892
        10         20         30         40         50         60 
MPHTHSRHGS SGDDLCSTDE VKIFKDEGDR EDEKISSENL LVEEKSSLID LTESEEKGHK 

        70         80         90        100        110        120 
ISRPDHSPVF NKLDTHAPSF NMGYLVSPYS YANGSPSGLP VTMANKIGLP PFFCHNADPL 

       130        140        150        160        170        180 
STPPPAHCGI PPYQLDPKMG LTRPALYPFA GGQYPYPMLS SDMSQVASWH TPSVYSASSF 

       190        200        210        220        230        240 
RTPYPSSLPI NTTLASDFPF RFSPSLLPSV HATSHHVINA HSAIVGVSSK QECGVQDPTT 

       250        260        270        280        290        300 
NNRYPRNLEA KHTSNAQSNE SKETTNDKKK PHIKKPLNAF MLYMKEMRAK VVAECTLKES 

       310        320        330        340        350        360 
AAINQILGRR WHELSREEQS KYYEKARQER QLHMELYPGW SARDNYGYVS KKKKRKKDRS 

       370        380        390        400        410        420 
TTDSGGNNMK KCRARFGLDQ QSQWCKPCRR KKKCIRYMEA LNGNGPAEDG SCFDEHGSQL 

       430        440        450        460        470        480 
SDDDEDDYDD DKLGGSCGSA DETNKIEDED SESLNQSMPS PGCLSGLSSL QSPSTTMSLA 

       490        500        510        520        530        540 
SPLNMNANSA TNVIFPASSN ALLIVGADQP TAQQRPTLVS TSGSSSGSTS SISTTPNTSS 

       550        560        570        580        590        600 
TVSPVTCMTG PCLGSSQERA MMLGNRFSHL GMGLSPPVVS TSTSKSEPFF KPHPTVCNNP 

       610        620        630        640        650        660 
IFALPSIGNC SLNISSMPNT SRNPIGANPR DINNPLSINQ LTKRREYKNV ELIEASESKT 

       670        680        690        700        710        720 
IVAHAATSII QHVAVNGYHA NHSLLNSNLG HLHHQLNNRT ENPNRSEQTM LSVSNHSVNS 

       730        740        750 
SECHKESDSQ AIVSSNPPNA GSSDNGVISV S 

« Hide

Isoform H [UniParc].

Checksum: 227A1983477B38C8
Show »

FASTA74781,391
Isoform S [UniParc].

Checksum: 2B90BC91E37D8FB1
Show »

FASTA73379,936
Isoform I [UniParc].

Checksum: D80032389302FA84
Show »

FASTA41046,291
Isoform J [UniParc].

See Q8IMA8.

References

« Hide 'large scale' references
[1]"Armadillo coactivates transcription driven by the product of the Drosophila segment polarity gene dTCF."
van de Wetering M., Cavallo R.A., Dooijes D., van Beest M., van Es J., Loureiro J., Ypma A., Hursh D., Jones T., Bejsovec A., Peifer M., Mortin M., Clevers H.
Cell 88:789-799(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DISRUPTION PHENOTYPE.
[2]"Pangolin encodes a Lef-1 homologue that acts downstream of Armadillo to transduce the Wingless signal in Drosophila."
Brunner E., Peter O., Schweizer L., Basler K.
Nature 385:829-833(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION.
[3]"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.
[4]"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.
[5]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 363-751 (ISOFORM J).
Strain: Berkeley.
Tissue: Head.
[6]"Recombination, dominance and selection on amino acid polymorphism in the Drosophila genome: contrasting patterns on the X and fourth chromosomes."
Sheldahl L.A., Weinreich D.M., Rand D.M.
Genetics 165:1195-1208(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 390-751.
Strain: Crete24, Crete26, Crete30, Crete31, Crete35, Crete40, Crete42, Crete43, Crete44, Crete8, FTF1, FTF105, FTF14, FTF2, FTF20, FTF23, FTF26, FTF28, FTF5, FTF6, Zim11, Zim2, Zim30 and Zim53.
[7]"Drosophila Tcf and Groucho interact to repress Wingless signalling activity."
Cavallo R.A., Cox R.T., Moline M.M., Roose J., Polevoy G.A., Clevers H., Peifer M., Bejsovec A.
Nature 395:604-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARM AND GRO, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09125 mRNA. Translation: CAA70343.1.
U88538 mRNA. Translation: AAC47464.1.
AE014135 Genomic DNA. Translation: AAF59371.2.
AE014135 Genomic DNA. Translation: AAN06545.1.
AE014135 Genomic DNA. Translation: AAN06548.2.
AE014135 Genomic DNA. Translation: AFH06766.1.
AE014135 Genomic DNA. Translation: AAX52517.1.
AE014135 Genomic DNA. Translation: ABC65830.1.
BT021431 mRNA. Translation: AAX33579.1.
BT029282 mRNA. Translation: ABK30919.1.
BT044547 mRNA. Translation: ACI03583.1.
BT053747 mRNA. Translation: ACK77665.1.
AY312729 Genomic DNA. Translation: AAQ67543.1.
AY312730 Genomic DNA. Translation: AAQ67544.1.
AY312731 Genomic DNA. Translation: AAQ67545.1.
AY312732 Genomic DNA. Translation: AAQ67546.1.
AY312733 Genomic DNA. Translation: AAQ67547.1.
AY312734 Genomic DNA. Translation: AAQ67548.1.
AY312735 Genomic DNA. Translation: AAQ67549.1.
AY312736 Genomic DNA. Translation: AAQ67550.1.
AY312737 Genomic DNA. Translation: AAQ67551.1.
AY312738 Genomic DNA. Translation: AAQ67552.1.
AY312739 Genomic DNA. Translation: AAQ67553.1.
AY312740 Genomic DNA. Translation: AAQ67554.1.
AY312741 Genomic DNA. Translation: AAQ67555.1.
AY312742 Genomic DNA. Translation: AAQ67556.1.
AY312743 Genomic DNA. Translation: AAQ67557.1.
AY312744 Genomic DNA. Translation: AAQ67558.1.
AY312745 Genomic DNA. Translation: AAQ67559.1.
AY312746 Genomic DNA. Translation: AAQ67560.1.
AY312747 Genomic DNA. Translation: AAQ67561.1.
AY312748 Genomic DNA. Translation: AAQ67562.1.
AY312749 Genomic DNA. Translation: AAQ67563.1.
AY312750 Genomic DNA. Translation: AAQ67564.1.
AY312751 Genomic DNA. Translation: AAQ67565.1.
AY312752 Genomic DNA. Translation: AAQ67566.1.
RefSeqNP_001014685.1. NM_001014685.3. [P91943-4]
NP_001033798.1. NM_001038709.3. [P91943-5]
NP_001245406.1. NM_001258477.2. [P91943-3]
NP_524619.3. NM_079880.6. [P91943-3]
NP_726522.1. NM_166718.3. [P91943-3]
NP_726524.1. NM_166720.3. [P91943-3]
NP_726527.2. NM_166723.3. [P91943-6]
UniGeneDm.17803.

3D structure databases

ProteinModelPortalP91943.
SMRP91943. Positions 272-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68607. 35 interactions.
DIPDIP-19970N.
IntActP91943. 24 interactions.
MINTMINT-994044.

Proteomic databases

PaxDbP91943.
PRIDEP91943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089156; FBpp0088223; FBgn0085432. [P91943-3]
FBtr0089157; FBpp0088224; FBgn0085432. [P91943-3]
FBtr0089158; FBpp0088225; FBgn0085432. [P91943-3]
FBtr0089159; FBpp0088226; FBgn0085432. [P91943-3]
FBtr0089160; FBpp0088227; FBgn0085432. [P91943-3]
FBtr0089161; FBpp0088228; FBgn0085432. [P91943-3]
FBtr0089162; FBpp0088229; FBgn0085432. [P91943-3]
FBtr0309803; FBpp0301556; FBgn0085432. [P91943-3]
GeneID43769.
KEGGdme:Dmel_CG34403.

Organism-specific databases

CTD43769.
FlyBaseFBgn0085432. pan.

Phylogenomic databases

eggNOGNOG252916.
GeneTreeENSGT00390000009964.
InParanoidP91943.
OMAKCIRYKE.
OrthoDBEOG72VH6Z.

Enzyme and pathway databases

SignaLinkP91943.

Gene expression databases

BgeeP91943.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
4.10.900.10. 1 hit.
InterProIPR027397. Catenin_binding_dom.
IPR013558. CTNNB1-bd_N.
IPR009071. HMG_box_dom.
IPR028782. Pangolin.
IPR024940. TCF/LEF.
[Graphical view]
PANTHERPTHR10373. PTHR10373. 1 hit.
PTHR10373:SF36. PTHR10373:SF36. 1 hit.
PfamPF08347. CTNNB1_binding. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
PROSITEPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSpan. drosophila.
GenomeRNAi43769.
NextBio835691.

Entry information

Entry namePANG1_DROME
AccessionPrimary (citable) accession number: P91943
Secondary accession number(s): A0AVW4 expand/collapse secondary AC list , A4V148, B5RJS3, O02548, Q0KIE9, Q59DP5, Q5BHZ3, Q6W492, Q6W493, Q6W494, Q6W495, Q6W4A6, Q6W4B4, Q9V4B0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 133 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