P53632 (PAP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly(A) RNA polymerase protein 2
EC=2.7.7.-

Alternative name(s):
DNA polymerase kappa
DNA polymerase sigma
Topoisomerase 1-related protein TRF4

Gene names

Name:	PAP2
Synonyms:	TRF4
Ordered Locus Names:	YOL115W
ORF Names:	O0716, HRC584

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	584 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Polyadenylates RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. TRF4 is also required for proper nuclear division in mitosis, DNA damage repair and sister chromatid cohesion. Involved in the regulation of histone mRNA levels. May mediate mitotic chromosome condensation. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25
Catalytic activity	ATP + RNA(n) = diphosphate + RNA(n+1). Ref.25
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Component of the TRAMP complex (also called TRF4 complex) composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2. Interacts with NOP53 and POL2. Interacts directly with AIR2. Ref.13 Ref.24 Ref.25
Subcellular location	Nucleus Ref.8 Ref.14.
Miscellaneous	Present with 7550 molecules/cell in log phase SD medium. Ref.15
Sequence similarities	Belongs to the DNA polymerase type-B-like family. Contains 1 PAP-associated domain.
Caution	Was originally thought to have DNA polymerase activity.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Ligand	Magnesium Manganese Metal-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	U4 snRNA 3'-end processing Inferred from mutant phenotype Ref.21. Source: SGD base-excision repair Inferred from mutant phenotype. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW histone mRNA catabolic process Inferred from genetic interaction Ref.23. Source: SGD mitosis Inferred from electronic annotation. Source: UniProtKB-KW nuclear polyadenylation-dependent CUT catabolic process Inferred from mutant phenotype Ref.18. Source: SGD nuclear polyadenylation-dependent antisense transcript catabolic process Inferred from mutant phenotype. Source: SGD nuclear polyadenylation-dependent mRNA catabolic process Inferred from genetic interaction Ref.21. Source: SGD nuclear polyadenylation-dependent rRNA catabolic process Inferred from mutant phenotype Ref.17Ref.22. Source: SGD nuclear polyadenylation-dependent snRNA catabolic process Inferred from mutant phenotype Ref.17Ref.22. Source: SGD nuclear polyadenylation-dependent snoRNA catabolic process Inferred from mutant phenotype Ref.17. Source: SGD nuclear polyadenylation-dependent tRNA catabolic process Inferred from direct assay Ref.20Ref.17. Source: SGD polyadenylation-dependent snoRNA 3'-end processing Inferred from genetic interaction Ref.21. Source: SGD snoRNA polyadenylation Inferred from genetic interaction. Source: SGD
Cellular component	TRAMP complex Inferred from direct assay Ref.20Ref.17Ref.18. Source: SGD nucleolus Inferred from direct assay. Source: SGD
Molecular function	5'-deoxyribose-5-phosphate lyase activity Inferred from direct assay. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW polynucleotide adenylyltransferase activity Inferred from direct assay Ref.25. Source: UniProtKB protein binding Inferred from physical interaction Ref.25. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AIR1	P40507	7	EBI-19517,EBI-25083
AIR2	Q12476	13	EBI-19517,EBI-31475
MTR4	P47047	11	EBI-19517,EBI-11592

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 584

584

Poly(A) RNA polymerase protein 2

PRO_0000120314

Regions

Domain

371 – 431

61

PAP-associated

Sites

Metal binding

236

1

Magnesium or manganese; catalytic By similarity

Metal binding

238

1

Magnesium or manganese; catalytic By similarity

Experimental info

Mutagenesis

131 – 133

3

EDE → AAA in TRF4-131; slow growth.

Mutagenesis

140 – 142

3

ERE → AAA in TRF4-140; slow growth.

Mutagenesis

182 – 185

4

EIKD → AIAA in TRF4-182; lethal.

Mutagenesis

194

1

R → A in TRF4-194; lethal; when associated with A-195; A-196 and A-198.

Mutagenesis

195 – 198

4

EEIE → AIAA in TRF4-194; lethal.

Mutagenesis

217 – 219

3

DAD → AAA in TRF4-217; slow growth.

Mutagenesis

224 – 225

2

GS → AA in TRF4-224; lethal.

Mutagenesis

236 – 238

3

DID → AIA in TRF4-236; lethal. Ref.9 Ref.22

Mutagenesis

275 – 277

3

KAR → AAA in TRF4-275; temperature sensitive.

Mutagenesis

282

1

K → A in TRF4-282; lethal; when associated with A-285.

Mutagenesis

285

1

E → A in TRF4-282; lethal; when associated with A-282.

Mutagenesis

309 – 310

2

RE → AA in TRF4-309; lethal.

Mutagenesis

332 – 333

2

RR → AA in TRF4-332; temperature sensitive.

Mutagenesis

378

1

E → A in TRF4-378; lethal; when associated with A-381.

Mutagenesis

381

1

E → A in TRF4-378; lethal; when associated with A-378.

Mutagenesis

425

1

D → A in TRF4-425; lethal; when associated with A-428 and A-429.

Mutagenesis

428 – 429

2

DE → AA in TRF4-425; lethal; when associated with A-425.

Mutagenesis

444 – 445

2

KK → AA in TRF4-444; lethal.

Mutagenesis

467 – 469

3

KDR → AAA in TRF4-467; temperature sensitive.

Mutagenesis

486 – 487

2

RD → AA in TRF4-486; lethal.

Mutagenesis

490 – 492

3

DER → AAA in TRF4-486; lethal.

Mutagenesis

502

1

E → A in TRF4-502; lethal; when associated with A-504.

Mutagenesis

504

1

E → A in TRF4-502; lethal; when associated with A-502.

Mutagenesis

508 – 510

3

KKR → AAA in TRF4-508; lethal.

Mutagenesis

559 – 560

2

KR → AA in TRF4-559; slow growth.

Mutagenesis

560

1

R → A in TRF4-559; slow growth; when associated with A-559.

Mutagenesis

572 – 574

3

EDD → AAA in TRF4-572; slow growth. Ref.12

Secondary structure

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584

Helix Strand Turn

Details...

Helix

162 – 164

3

Helix

175 – 189

15

Helix

194 – 212

19

Beta strand

220 – 223

4

Turn

226 – 229

4

Beta strand

237 – 241

5

Helix

250 – 263

14

Beta strand

271 – 277

7

Beta strand

279 – 284

6

Beta strand

291 – 297

7

Helix

303 – 313

11

Helix

319 – 331

13

Helix

346 – 356

11

Helix

359 – 362

4

Helix

368 – 370

3

Helix

375 – 382

8

Beta strand

391 – 394

4

Helix

406 – 408

3

Helix

410 – 412

3

Beta strand

418 – 420

3

Helix

440 – 447

8

Helix

451 – 462

12

Helix

466 – 469

4

Sequences

	Sequence		Length	Mass (Da)
	P53632 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8A58B29E4BFDC022	FASTA	584	66,031
	10 20 30 40 50 60 MGAKSVTASS SKKIKNRHNG KVKKSKKIKK VRKPQKSISL NDENEVEILP SRNEQETNKL 70 80 90 100 110 120 PKDHVTADGI LVLEHKSDDD EGFDVYDGHF DNPTDIPSTT EESKTPSLAV HGDEKDLANN 130 140 150 160 170 180 DDFISLSASS EDEQAEQEEE REKQELEIKK EKQKEILNTD YPWILNHDHS KQKEISDWLT 190 200 210 220 230 240 FEIKDFVAYI SPSREEIEIR NQTISTIREA VKQLWPDADL HVFGSYSTDL YLPGSDIDCV 250 260 270 280 290 300 VTSELGGKES RNNLYSLASH LKKKNLATEV EVVAKARVPI IKFVEPHSGI HIDVSFERTN 310 320 330 340 350 360 GIEAAKLIRE WLDDTPGLRE LVLIVKQFLH ARRLNNVHTG GLGGFSIICL VFSFLHMHPR 370 380 390 400 410 420 IITNEIDPKD NLGVLLIEFF ELYGKNFGYD DVALGSSDGY PVYFPKSTWS AIQPIKNPFS 430 440 450 460 470 480 LAIQDPGDES NNISRGSFNI RDIKKAFAGA FDLLTNRCFE LHSATFKDRL GKSILGNVIK 490 500 510 520 530 540 YRGKARDFKD ERGLVLNKAI IENENYHKKR SRIIHDEDFA EDTVTSTATA TTTDDDYEIT 550 560 570 580 NPPAKKAKIE EKPESEPAKR NSGETYITVS SEDDDEDGYN PYTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of mutants of Saccharomyces cerevisiae requiring DNA topoisomerase I." Sadoff B.U., Heath-Pagliuso S., Castano I.B., Zhu Y., Kieff F.S., Christman M.F. Genetics 141:465-479(1995) [PubMed: 8647385] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element." Vandenbol M., Durand P., Portetelle D., Hilger F. Yeast 11:1069-1075(1995) [PubMed: 7502582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Mitotic chromosome condensation in the rDNA requires TRF4 and DNA topoisomerase I in Saccharomyces cerevisiae." Castano I.B., Brzoska P.M., Sadoff B.U., Chen H., Christman M.F. Genes Dev. 10:2564-2576(1996) [PubMed: 8895658] [Abstract] Cited for: FUNCTION.
[7]	"A novel family of TRF (DNA topoisomerase I-related function) genes required for proper nuclear segregation." Castano I.B., Heath-Pagliuso S., Sadoff B.U., Fitzhugh D.J., Christman M.F. Nucleic Acids Res. 24:2404-2410(1996) [PubMed: 8710513] [Abstract] Cited for: FUNCTION.
[8]	"The topoisomerase-related function gene TRF4 affects cellular sensitivity to the antitumor agent camptothecin." Walowsky C., Fitzhugh D.J., Castano I.B., Ju J.Y., Levin N.A., Christman M.F. J. Biol. Chem. 274:7302-7308(1999) [PubMed: 10066793] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"Pol kappa: a DNA polymerase required for sister chromatid cohesion." Wang Z., Castano I.B., De Las Penas A., Adams C., Christman M.F. Science 289:774-779(2000) [PubMed: 10926539] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 236-ASP--ASP-238.
[10]	"Eukaryotic DNA polymerases: proposal for a revised nomenclature." Burgers P.M.J., Koonin E.V., Bruford E., Blanco L., Burtis K.C., Christman M.F., Copeland W.C., Friedberg E.C., Hanaoka F., Hinkle D.C., Lawrence C.W., Nakanishi M., Ohmori H., Prakash L., Prakash S., Reynaud C.-A., Sugino A., Todo T. , Wang Z., Weill J.-C., Woodgate R. J. Biol. Chem. 276:43487-43490(2001) [PubMed: 11579108] [Abstract] Cited for: NOMENCLATURE.
[11]	"Cid13 is a cytoplasmic poly(A) polymerase that regulates ribonucleotide reductase mRNA." Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III, Russell P. Cell 109:563-573(2002) [PubMed: 12062100] [Abstract] Cited for: FUNCTION.
[12]	"Structure/function analysis of the Saccharomyces cerevisiae Trf4/Pol sigma DNA polymerase." Wang Z., Castano I.B., Adams C., Vu C., Fitzhugh D.J., Christman M.F. Genetics 160:381-391(2002) [PubMed: 11861546] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 131-GLU--GLU-133; 140-GLU--GLU-142; 182-GLU--ASP-185; 194-ARG--GLU-198; 217-ASP--ASP-219; 224-GLU-SER-225; 236-ASP--ASP-238; 275-LYS--ARG-277; 282-LYS--GLU-285; 309-ARG-GLU-310; 332-ARG-ARG-333; 378-GLU--GLU-381; 425-ASP--GLU-429; 444-LYS-LYS-445; 467-LYS--ARG-469; 486-ARG--ASP-490; 491-GLU-ARG-492; 502-GLU--GLU-504; 508-LYS--ARG-510; 559-LYS-ARG-560 AND 572-GLU--ASP-574.
[13]	"Saccharomyces cerevisiae DNA polymerase epsilon and polymerase sigma interact physically and functionally, suggesting a role for polymerase epsilon in sister chromatid cohesion." Edwards S., Li C.M., Levy D.L., Brown J., Snow P.M., Campbell J.L. Mol. Cell. Biol. 23:2733-2748(2003) [PubMed: 12665575] [Abstract] Cited for: FUNCTION, INTERACTION WITH POL2.
[14]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[15]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[16]	"Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae." Kadaba S., Krueger A., Trice T., Krecic A.M., Hinnebusch A.G., Anderson J.T. Genes Dev. 18:1227-1240(2004) [PubMed: 15145828] [Abstract] Cited for: FUNCTION.
[17]	"RNA degradation by the exosome is promoted by a nuclear polyadenylation complex." LaCava J., Houseley J., Saveanu C., Petfalski E., Thompson E., Jacquier A., Tollervey D. Cell 121:713-724(2005) [PubMed: 15935758] [Abstract] Cited for: IDENTIFICATION IN TRAMP COMPLEX, FUNCTION OF THE TRAMP COMPLEX.
[18]	"Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase." Wyers F., Rougemaille M., Badis G., Rousselle J.-C., Dufour M.-E., Boulay J., Regnault B., Devaux F., Namane A., Seraphin B., Libri D., Jacquier A. Cell 121:725-737(2005) [PubMed: 15935759] [Abstract] Cited for: IDENTIFICATION IN THE TRF4 COMPLEX, MASS SPECTROMETRY, FUNCTION OF THE TRF4 COMPLEX.
[19]	"Trf4 and Trf5 proteins of Saccharomyces cerevisiae exhibit poly(A) RNA polymerase activity but no DNA polymerase activity." Haracska L., Johnson R.E., Prakash L., Prakash S. Mol. Cell. Biol. 25:10183-10189(2005) [PubMed: 16260630] [Abstract] Cited for: FUNCTION.
[20]	"A new yeast poly(A) polymerase complex involved in RNA quality control." Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A., Langen H., Keith G., Keller W. PLoS Biol. 3:986-997(2005) [PubMed: 15828860] [Abstract] Cited for: IDENTIFICATION IN THE TRF4 COMPLEX, MASS SPECTROMETRY, FUNCTION OF THE TRF4 COMPLEX.
[21]	"Contributions of Trf4p- and Trf5p-dependent polyadenylation to the processing and degradative functions of the yeast nuclear exosome." Egecioglu D.E., Henras A.K., Chanfreau G.F. RNA 12:26-32(2006) [PubMed: 16373491] [Abstract] Cited for: FUNCTION.
[22]	"Nuclear RNA surveillance in Saccharomyces cerevisiae: Trf4p-dependent polyadenylation of nascent hypomethylated tRNA and an aberrant form of 5S rRNA." Kadaba S., Wang X., Anderson J.T. RNA 12:508-521(2006) [PubMed: 16431988] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 236-ASP--ASP-238.
[23]	"Contribution of Trf4/5 and the nuclear exosome to genome stability through regulation of histone mRNA levels in Saccharomyces cerevisiae." Reis C.C., Campbell J.L. Genetics 175:993-1010(2007) [PubMed: 17179095] [Abstract] Cited for: FUNCTION.
[24]	"Nop53p interacts with 5.8S rRNA co-transcriptionally, and regulates processing of pre-rRNA by the exosome." Granato D.C., Machado-Santelli G.M., Oliveira C.C. FEBS J. 275:4164-4178(2008) [PubMed: 18631361] [Abstract] Cited for: INTERACTION WITH NOP53.
[25]	"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex." Hamill S., Wolin S.L., Reinisch K.M. Proc. Natl. Acad. Sci. U.S.A. 107:15045-15050(2010) [PubMed: 20696927] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 161-481 IN COMPLEX WITH AIR2, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH AIR2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U31355 Genomic DNA. Translation: AAC49091.1.
Z48149 Genomic DNA. Translation: CAA88145.1.
Z74857 Genomic DNA. Translation: CAA99134.1.
AY723865 Genomic DNA. Translation: AAU09782.1.
BK006948 Genomic DNA. Translation: DAA10668.1.

PIR

S51882.

RefSeq

NP_014526.1. NM_001183369.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NYB	X-ray	2.70	A	161-481	[»]

ProteinModelPortal

P53632.

SMR

P53632. Positions 161-481.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4214N.

IntAct

P53632. 17 interactions.

MINT

MINT-500696.

STRING

P53632.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOL115W; YOL115W; YOL115W.

GeneID

854034.

KEGG

sce:YOL115W.

NMPDR

fig|4932.3.peg.5612.

Organism-specific databases

CYGD

YOL115w.

SGD

S000005475. PAP2.

Phylogenomic databases

eggNOG

fuNOG05608.

GeneTree

EFGT00050000004816.

HOGENOM

HBG395964.

OMA

LHVFGSY.

OrthoDB

EOG43BQXK.

Gene expression databases

ArrayExpress

P53632.

Genevestigator

P53632.

GermOnline

YOL115W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002934. Nucleotidyltransferase.
IPR002058. PAP_assoc.
[Graphical view]

KO

K03514.

Pfam

PF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

975589.

Entry information

Entry name

PAP2_YEAST

Accession

Primary (citable) accession number: P53632
Secondary accession number(s): D6W1V2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program