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P38696 (ARP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centractin
Alternative name(s):
Actin-like protein
Actin-related protein 1
Gene names
Name:ARP1
Synonyms:ACT3, ACT5
Ordered Locus Names:YHR129C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding By similarity. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. Required for proper orientation of the mitotic spindle. Ref.6 Ref.8

Subunit structure

Self-associates to form an actin-like filament of 8-10 monomers. Component of the dynactin complex composed of at least ARP1, JNM1, NIP100 and ARP10. Dynactin comprises a short rod of the ARP1 filament attached to ARP10 at its pointed-end and probably associated with the capping protein at its barbed-end. The rod is implicated in dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1 filament and is implicated in motor binding By similarity.

Subcellular location

Cytoplasmcytoskeleton Probable. Membrane. Note: Membrane-associated. Ref.11

Miscellaneous

Present with 1580 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the actin family. ARP1 subfamily.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Centractin
PRO_0000089066

Experimental info

Mutagenesis21D → A: Temperature-sensitive; when associated with A-6. Ref.10
Mutagenesis61D → A: Temperature-sensitive; when associated with A-2. Ref.10
Mutagenesis461K → A: Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with 48-A-A-49. Ref.9 Ref.10
Mutagenesis48 – 492DK → AA: Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with A-46.
Mutagenesis731K → A: Reduces spindle formation; when associated with A-75. Ref.9
Mutagenesis751R → A: Reduces spindle formation; when associated with A-73. Ref.9
Mutagenesis79 – 802KH → AA: Reduces nuclear migration in mitosis.
Mutagenesis84 – 852ED → AA: Reduces spindle formation. Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with A-87.
Mutagenesis871D → A: Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with 84-A-A-85. Ref.9
Mutagenesis108 – 1092EH → AA: Reduces nuclear migration in mitosis.
Mutagenesis1331E → A: Lethal. Strongly reduces interaction with JNM1; when associated with A-136. Ref.10
Mutagenesis1361D → A: Lethal. Strongly reduces interaction with JNM1; when associated with A-133. Ref.10
Mutagenesis1621D → A: Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-165. Ref.9
Mutagenesis1651E → A: Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-162. Ref.9
Mutagenesis1851R → A: Temperature-sensitive. Strongly reduces interaction with JNM1; when associated with A-187. Ref.10
Mutagenesis1871D → A: Temperature-sensitive. Strongly reduces interaction with JNM1; when associated with A-185. Ref.10
Mutagenesis214 – 2163ERE → AAA: Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. Alters complex assembly; when associated with A-219. Ref.9 Ref.10
Mutagenesis2191R → A: Lethal; when associated with 214-A--A-216. Ref.10
Mutagenesis222 – 2243KEK → AAA: Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. Ref.9 Ref.10
Mutagenesis233 – 2386KKEEEK → AAAAAA: Temperature-sensitive. Strongly reduces interaction with JNM1. Ref.10
Mutagenesis233 – 2353KKE → AAA: Reduces spindle formation. Ref.9
Mutagenesis236 – 2383EEK → AAA: Reduces spindle formation. Ref.9
Mutagenesis2511K → A: Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis; when associated with A-254. Ref.9 Ref.10
Mutagenesis2541D → A: Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis; when associated with A-251. Ref.9 Ref.10
Mutagenesis263 – 2642DR → AA: Reduces spindle formation.
Mutagenesis2661R → A: Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-269. Ref.9 Ref.10
Mutagenesis2691E → A: Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-266. Ref.9 Ref.10
Mutagenesis2941K → A: Reduces nuclear migration in mitosis; when associated with A-296 and A-298. Ref.9
Mutagenesis2961D → A: Reduces nuclear migration in mitosis; when associated with A-294 and A-298. Ref.9
Mutagenesis2981D → A: Reduces nuclear migration in mitosis; when associated with A-294 and A-296. Ref.9
Mutagenesis321 – 3222DR → AA: Lethal. Strongly reduces interaction with JNM1.
Mutagenesis3261D → A: Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-328. Ref.9 Ref.10
Mutagenesis3281E → A: Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-326. Ref.9 Ref.10
Mutagenesis3361K → A: Strongly reduces interaction with JNM1; when associated with A-338. Ref.10
Mutagenesis3381K → A: Strongly reduces interaction with JNM1; when associated with A-336. Ref.10
Mutagenesis344 – 3463ERK → AAA: Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1. Ref.9 Ref.10
Mutagenesis368 – 3692KK → AA: Reduces nuclear migration in mitosis; when associated with A-371. Ref.10
Mutagenesis3691K → A: Lethal. Strongly reduces interaction with JNM1; when associated with A-371. Ref.10
Mutagenesis3711D → A: Lethal. Strongly reduces interaction with JNM1; when associated with A-369. Ref.9 Ref.10
Mutagenesis3711D → AA: Reduces nuclear migration in mitosis; when associated with 368-A-A-369. Ref.9 Ref.10
Mutagenesis374 – 3752ED → AA: Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-378.
Mutagenesis3781R → A: Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with 374-A-A-375. Ref.10
Sequence conflict31Q → P in AAT93103. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P38696 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 98EEA90DC9497B81

FASTA38442,995
        10         20         30         40         50         60 
MDQLSDSYAL YNQPVVIDNG SGIIKAGFSG EERPKALEYC LVGNTKYDKV MLEGLQGDTF 

        70         80         90        100        110        120 
IGNNAQKLRG LLKLRYPIKH GVVEDWDSME LIWSYVLNEV LQLQNIGEHP LLITEAPMNP 

       130        140        150        160        170        180 
LKNREQMAQV LFETFDVSAL YVSNPAVLSL YASGRTTGCV VDCGEGYCST VPIYDGFALP 

       190        200        210        220        230        240 
ASMMRMDIGG ADITEQLQFQ LRKSAGVSLF SSSEREIVRT MKEKVCYLAK NIKKEEEKYL 

       250        260        270        280        290        300 
QGTQDLISTF KLPDGRCIEV GNDRYRAPEI LFSPQIIGLG YDGLSDMCMQ SIWKVDLDLR 

       310        320        330        340        350        360 
KPLLSSIILS GGTTTLKGFG DRMLWDLEAL TKGTSKIKII APSERKYTTW IGGSILTGLS 

       370        380 
TFQRLWTKKS DWLEDSTRVY SNLM 

« Hide

References

« Hide 'large scale' references
[1]"ACT3: a putative centractin homologue in S. cerevisiae is required for proper orientation of the mitotic spindle."
Clark S.W., Meyer D.I.
J. Cell Biol. 127:129-138(1994) [PubMed: 7929558] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26109 / X2180.
[2]"A yeast actin-related protein homologous to that in vertebrate dynactin complex is important for spindle orientation and nuclear migration."
Muhua L., Karpova T.S., Cooper J.A.
Cell 78:669-679(1994) [PubMed: 8069915] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[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. expand/collapse author list , 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 [LARGE SCALE GENOMIC DNA].
[6]"The yeast dynactin complex is involved in partitioning the mitotic spindle between mother and daughter cells during anaphase B."
Kahana J.A., Schlenstedt G., Evanchuk D.M., Geiser J.R., Hoyt M.A., Silver P.A.
Mol. Biol. Cell 9:1741-1756(1998) [PubMed: 9658168] [Abstract]
Cited for: IDENTIFICATION IN THE DYNACTIN COMPLEX, FUNCTION OF THE DYNACTIN COMPLEX.
[7]"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].
[8]"Dynactin is involved in a checkpoint to monitor cell wall synthesis in Saccharomyces cerevisiae."
Suzuki M., Igarashi R., Sekiya M., Utsugi T., Morishita S., Yukawa M., Ohya Y.
Nat. Cell Biol. 6:861-871(2004) [PubMed: 15311283] [Abstract]
Cited for: FUNCTION OF THE DYNACTIN COMPLEX.
[9]"Molecular dissection of ARP1 regions required for nuclear migration and cell wall integrity checkpoint functions in Saccharomyces cerevisiae."
Igarashi R., Suzuki M., Nogami S., Ohya Y.
Cell Struct. Funct. 30:57-67(2005) [PubMed: 16415535] [Abstract]
Cited for: MUTAGENESIS OF LYS-46; 48-ASP-LYS-49; LYS-73; ARG-75; 79-LYS-HIS-80; 84-GLU-ASP-85; ASP-87; 108-GLU-HIS-109; ASP-162; GLU-165; 214-GLU--GLU-216; 222-LYS--LYS-224; 233-LYS--GLU-235; 236-GLU--LYS-238; LYS-251; ASP-254; 263-ASP-ARG-264; ARG-266; GLU-269; LYS-294; ASP-296; ASP-298; ASP-326; GLU-328; 344-GLU--LYS-346; 368-LYS-LYS-369 AND ASP-371.
[10]"Alanine scanning of Arp1 delineates a putative binding site for Jnm1/dynamitin and Nip100/p150Glued."
Clark S.W., Rose M.D.
Mol. Biol. Cell 16:3999-4012(2005) [PubMed: 15975903] [Abstract]
Cited for: INTERACTION WITH JNM1, MUTAGENESIS OF ASP-2; ASP-6; LYS-46; 48-ASP-LYS-49; 84-GLU-ASP-85; GLU-133; ASP-136; ARG-185; ASP-187; 214-GLU--GLU-216; ARG-219; 222-LYS--LYS-224; 233-LYS--LYS-238; LYS-251; ASP-254; ARG-266; GLU-269; 321-ASP-ARG-322; ASP-326; GLU-328; LYS-336; LYS-338; 344-GLU--LYS-346; LYS-369; ASP-371; 374-GLU-ASP-375 AND ARG-378.
[11]"Arp10p is a pointed-end-associated component of yeast dynactin."
Clark S.W., Rose M.D.
Mol. Biol. Cell 17:738-748(2006) [PubMed: 16291862] [Abstract]
Cited for: SUBCELLULAR LOCATION, SELF-ASSOCIATION, INTERACTION WITH ARP10 AND JNM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79811 Genomic DNA. Translation: CAA56206.1.
U10398 Genomic DNA. Translation: AAB68412.1.
AY693084 Genomic DNA. Translation: AAT93103.1.
BK006934 Genomic DNA. Translation: DAA06822.1.
PIRS48973.
RefSeqNP_011997.1. NM_001179259.1.

3D structure databases

ProteinModelPortalP38696.
SMRP38696. Positions 12-383.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1205N.
IntActP38696. 15 interactions.
MINTMINT-389717.
STRINGP38696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR129C; YHR129C; YHR129C.
GeneID856530.
KEGGsce:YHR129C.
NMPDRfig|4932.3.peg.3158.

Organism-specific databases

CYGDYHR129c.
SGDS000001171. ARP1.

Phylogenomic databases

eggNOGfuNOG07557.
GeneTreeEFGT00050000001097.
HOGENOMHBG559892.
OMAMCELLFE.
OrthoDBEOG4X3M8S.

Gene expression databases

ArrayExpressP38696.
GenevestigatorP38696.
GermOnlineYHR129C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004000. Actin-like.
IPR020902. Actin/actin-like_CS.
[Graphical view]
PANTHERPTHR11937. Actin_like. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982304.

Entry information

Entry nameARP1_YEAST
AccessionPrimary (citable) accession number: P38696
Secondary accession number(s): D3DL78, Q6B1J6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 14, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

SIMILARITY comments

Index of protein domains and families