P36006 (MYO3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myosin-3

Alternative name(s):
Actin-dependent myosin-I MYO3
Class I unconventional myosin MYO3
Type I myosin MYO3

Gene names

Name:	MYO3
Ordered Locus Names:	YKL129C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1272 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12
Subunit structure	Interacts (via myosin head-like domain) with SHE4; this interaction is important for proper localization and may regulate the interaction of the motor domain with actin. Interacts (via SH3 domain) with VRP1; this interaction is required for localization to sites of polarized growth and may regulate the interaction of the tail domain with actin. Interacts (via SH3 domain) with PAN1; this interaction is important for late stages of endocytopsis. Interacts (via SH3 domain) with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits. Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.17
Subcellular location	Cytoplasm › cytoskeleton › actin patch. Note: Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth. Ref.17
Domain	The myosin head-like domain displays actin-stimulated ATPase activity and constitutes the motor domain by generating a mechanochemical force. The tail domain participates in molecular interactions that specify the role of the motor domain. It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding domain (TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).
Post-translational modification	Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase By similarity. Ser-357 is phosphorylated by CLA4 and STE20 in vitro. Ref.6
Miscellaneous	Present with 155 molecules/cell in log phase SD medium.
Sequence similarities	Contains 2 IQ domains. Contains 1 myosin head-like domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Repeat SH3 domain
Ligand	ATP-binding Actin-binding Nucleotide-binding
Molecular function	Hydrolase Motor protein Myosin
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cortical patch localization Inferred from genetic interaction PubMed 18177206. Source: SGD bipolar cellular bud site selection Traceable author statement PubMed 10652251. Source: SGD endocytosis Traceable author statement PubMed 10652251. Source: SGD exocytosis Traceable author statement PubMed 10652251. Source: SGD fungal-type cell wall organization Traceable author statement PubMed 10652251. Source: SGD response to osmotic stress Traceable author statement PubMed 10652251. Source: SGD
Cellular_component	actin cortical patch Traceable author statement PubMed 10652251. Source: SGD myosin complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microfilament motor activity Traceable author statement PubMed 9153752. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BBC1	P47068	3	EBI-11670,EBI-3437
BNI1	P41832	3	EBI-11670,EBI-3692
BNR1	P40450	4	EBI-11670,EBI-3711
LAS17	Q12446	3	EBI-11670,EBI-10022
VRP1	P37370	3	EBI-11670,EBI-20502

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1272

1272

Myosin-3

PRO_0000123490

Regions

Domain

38 – 701

664

Myosin head-like

Domain

719 – 739

21

IQ 1

Domain

740 – 765

26

IQ 2

Domain

1120 – 1182

63

SH3

Nucleotide binding

129 – 136

8

ATP Potential

Region

404 – 486

83

Actin-binding By similarity

Region

759 – 961

203

Basic, putative membrane-binding region

Compositional bias

1003 – 1123

121

Ala/Pro-rich

Compositional bias

1109 – 1116

8

Poly-Pro

Compositional bias

1259 – 1271

13

Asp-rich (acidic)

Amino acid modifications

Modified residue

357

1

Phosphoserine Ref.6 Ref.14 Ref.16 Ref.18 Ref.19

Modified residue

359

1

Phosphotyrosine Ref.19

Modified residue

777

1

Phosphoserine Ref.10 Ref.15 Ref.16 Ref.18 Ref.19

Modified residue

932

1

Phosphothreonine Ref.19

Modified residue

935

1

Phosphoserine Ref.19

Modified residue

1136

1

Phosphoserine Ref.19

Modified residue

1137

1

Phosphoserine Ref.19

Modified residue

1138

1

Phosphoserine Ref.19

Experimental info

Mutagenesis

132

1

G → R: Loss of function. Ref.8

Mutagenesis

357

1

S → A: Loss of function. Ref.6 Ref.8

Mutagenesis

357

1

S → D: Has a constitutive higher activity in actin assembly. Ref.6 Ref.8

Mutagenesis

1158

1

W → S: Abolishes interaction with LAS17 and causes severe mislocalization of the protein.

Mutagenesis

1272

1

Missing: Abolishes interaction with ARC40.

Sequence conflict

95

1

G → RK in AAB34124. Ref.1

Sequence conflict

168 – 169

2

NP → T in AAB34124. Ref.1

Sequence conflict

263 – 270

8

TADTIDDV → SADQLMR in CAA81970. Ref.2

Sequence conflict

917 – 918

2

VG → RLV in AAB34124. Ref.1

Sequence conflict

1021

1

A → R in CAA81970. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

1272

Helix Strand Turn

Details...

Beta strand

1123 – 1129

7

Beta strand

1137 – 1139

3

Beta strand

1147 – 1153

7

Beta strand

1157 – 1163

7

Beta strand

1169 – 1173

5

Helix

1174 – 1176

3

Beta strand

1177 – 1179

3

Sequences

	Sequence		Length	Mass (Da)
	P36006 [UniParc]. Last modified September 21, 2011. Version 4. Checksum: 6CB13AD3CD669600	FASTA	1,272	142,451
	10 20 30 40 50 60 MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGISD LTLLSKISDE SINENLKKRF 70 80 90 100 110 120 KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE VPPHVFAIAE SMYYNLKSYN 130 140 150 160 170 180 ENQCVIISGE SGAGKTEAAK RIMQYIAAAS NSHSESIGKI KDMVLATNPL LESFGCAKTL 190 200 210 220 230 240 RNNNSSRHGK YLEIKFNSQF EPCAGNITNY LLEKQRVVGQ IKNERNFHIF YQFTKGASDT 250 260 270 280 290 300 YKQMFGVQMP EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI 310 320 330 340 350 360 LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS HGMKRGSVYH 370 380 390 400 410 420 VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG ADKSIGILDI YGFEIFEHNS 430 440 450 460 470 480 FEQICINYVN EKLQQIFIQL TLKAEQETYE REKIKWTPIK YFDNKVVCDL IEAKNPPGIL 490 500 510 520 530 540 AAMNDSIATA HADSNAADQA FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK 550 560 570 580 590 600 NKDQLQKDLI ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP 610 620 630 640 650 660 SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK FVERFYLLSP 670 680 690 700 710 720 DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF IKTPESLFAL EDMRDKYWYN 730 740 750 760 770 780 MAARIQRAWR RFLQRRIDAA IKIQRTIREK KGGNKYVKLR DYGTKLLAGK KERRSMSLLG 790 800 810 820 830 840 YRAFMGDYLS CNESKTKGSY IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK 850 860 870 880 890 900 TFYIIGQTRE QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQS DPLINTPFKT 910 920 930 940 950 960 ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS STIYVRRGHP 970 980 990 1000 1010 1020 ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH RDAAKKQPLP SQKPVNPLSL 1030 1040 1050 1060 1070 1080 AATAAQAAYN PKPDKTVPIK SSAIPAAKVS SKHSSKPSSK EKVAVKKASS SHKSSSAKQN 1090 1100 1110 1120 1130 1140 QVSMPPSKGV EKNKEPLKET TATATANIPI PPPPPPMGQP KDPKFEAAYD FPGSGSSSEL 1150 1160 1170 1180 1190 1200 PLKKGDIVFI SRDEPSGWSL AKLLDGSKEG WVPTAYMTPY KDTRNTVPVA ATGAVNDVTN 1210 1220 1230 1240 1250 1260 QKSSQIDNTI SSAQEGVQFG SATVGPTSDN QSNPVGTFSD GLASALAARA NKMRAESADD 1270 DDNDDGDDDD DW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and molecular characterization of a yeast myosin I." Goodson H.V., Spudich J.A. Cell Motil. Cytoskeleton 30:73-84(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CRY3.
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 263-270 AND 1021. Strain: ATCC 204508 / S288c.
[4]	"Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton." Goodson H.V., Anderson B.L., Warrick H.M., Pon L.A., Spudich J.A. J. Cell Biol. 133:1277-1291(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIN CYTOSKELETON ORGANIZATION.
[5]	"Role of type I myosins in receptor-mediated endocytosis in yeast." Geli M.I., Riezman H. Science 272:533-535(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN RECEPTOR ENDOCYTOSIS.
[6]	"The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast." Wu C., Lytvyn V., Thomas D.Y., Leberer E. J. Biol. Chem. 272:30623-30626(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 BY CLA4 AND STE20, MUTAGENESIS OF SER-357.
[7]	"A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex." Evangelista M., Klebl B.M., Tong A.H.Y., Webb B.A., Leeuw T., Leberer E., Whiteway M., Thomas D.Y., Boone C. J. Cell Biol. 148:353-362(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARC19; ARC40; LAS17 AND VRP1.
[8]	"Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization." Lechler T., Shevchenko A., Li R. J. Cell Biol. 148:363-373(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARP2 AND LAS17, MUTAGENESIS OF GLY-132 AND SER-357.
[9]	"The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae." Mochida J., Yamamoto T., Fujimura-Kamada K., Tanaka K. Genetics 160:923-934(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BBC1.
[10]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777, MASS SPECTROMETRY. Strain: 2124.
[11]	"The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function." Wesche S., Arnold M., Jansen R.-P. Curr. Biol. 13:715-724(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SHE4.
[12]	"She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae." Toi H., Fujimura-Kamada K., Irie K., Takai Y., Todo S., Tanaka K. Mol. Biol. Cell 14:2237-2249(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SHE4.
[13]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, MASS SPECTROMETRY. Strain: SUB592.
[15]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777, MASS SPECTROMETRY. Strain: YAL6B.
[16]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-777, MASS SPECTROMETRY. Strain: ADR376.
[17]	"Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis." Barker S.L., Lee L., Pierce B.D., Maldonado-Baez L., Drubin D.G., Wendland B. Mol. Biol. Cell 18:2893-2903(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAN1, SUBCELLULAR LOCATION.
[18]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-777, MASS SPECTROMETRY.
[19]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; TYR-359; SER-777; THR-932; SER-935; SER-1136; SER-1137 AND SER-1138, MASS SPECTROMETRY.
[20]	"New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S.cerevisiae." Musi V., Birdsall B., Fernandez-Ballester G., Guerrini R., Salvatori S., Serrano L., Pastore A. Protein Sci. 15:795-807(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1123-1191.
[21]	"Crystal structure of the SH3 domain from S.cerevisiae Myo3." Kursula P., Kursula I., Lehmann F., Song Y.H., Wilmanns M. Submitted (MAR-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1123-1191.
[22]	"High-throughput structural genomics of yeast SH3 domains." Kursula P., Lehmann F., Song Y.H., Wilmanns M. Submitted (JUN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1123-1191.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S76960 Genomic DNA. Translation: AAB34124.1.
Z28129 Genomic DNA. Translation: CAA81970.1.
BK006944 Genomic DNA. Translation: DAA09032.2.

PIR

S37958.

RefSeq

NP_012793.2. NM_001179695.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RUW	X-ray	1.80	A	1122-1189	[»]
1VA7	X-ray	2.90	A/B/C/D	1122-1189	[»]
2BTT	NMR	-	A	1121-1189	[»]

ProteinModelPortal

P36006.

SMR

P36006. Positions 37-745, 1121-1189.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2221N.

IntAct

P36006. 28 interactions.

MINT

MINT-382399.

STRING

4932.YKL129C.

Proteomic databases

PaxDb

P36006.

PeptideAtlas

P36006.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YKL129C; YKL129C; YKL129C.

GeneID

853729.

KEGG

sce:YKL129C.

Organism-specific databases

SGD

S000001612. MYO3.

Phylogenomic databases

eggNOG

COG5022.

GeneTree

ENSGT00690000101741.

HOGENOM

HOG000260265.

OMA

PAGAPMM.

OrthoDB

EOG4M950J.

Gene expression databases

Genevestigator

P36006.

GermOnline

YKL129C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00193. MYOSINHEAVY.

SMART

SM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50096. IQ. False negative.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P36006.

NextBio

974764.

Entry information

Entry name

MYO3_YEAST

Accession

Primary (citable) accession number: P36006
Secondary accession number(s): D6VX66

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	September 21, 2011
Last modified:	May 1, 2013
This is version 124 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program