ARP1_YEAST
ID ARP1_YEAST Reviewed; 384 AA.
AC P38696; D3DL78; Q6B1J6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Centractin;
DE AltName: Full=Actin-like protein;
DE AltName: Full=Actin-related protein 1;
GN Name=ARP1; Synonyms=ACT3, ACT5; OrderedLocusNames=YHR129C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=7929558; DOI=10.1083/jcb.127.1.129;
RA Clark S.W., Meyer D.I.;
RT "ACT3: a putative centractin homologue in S. cerevisiae is required for
RT proper orientation of the mitotic spindle.";
RL J. Cell Biol. 127:129-138(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8069915; DOI=10.1016/0092-8674(94)90531-2;
RA Muhua L., Karpova T.S., Cooper J.A.;
RT "A yeast actin-related protein homologous to that in vertebrate dynactin
RT complex is important for spindle orientation and nuclear migration.";
RL Cell 78:669-679(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP IDENTIFICATION IN THE DYNACTIN COMPLEX, AND FUNCTION OF THE DYNACTIN
RP COMPLEX.
RX PubMed=9658168; DOI=10.1091/mbc.9.7.1741;
RA Kahana J.A., Schlenstedt G., Evanchuk D.M., Geiser J.R., Hoyt M.A.,
RA Silver P.A.;
RT "The yeast dynactin complex is involved in partitioning the mitotic spindle
RT between mother and daughter cells during anaphase B.";
RL Mol. Biol. Cell 9:1741-1756(1998).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION OF THE DYNACTIN COMPLEX.
RX PubMed=15311283; DOI=10.1038/ncb1162;
RA Suzuki M., Igarashi R., Sekiya M., Utsugi T., Morishita S., Yukawa M.,
RA Ohya Y.;
RT "Dynactin is involved in a checkpoint to monitor cell wall synthesis in
RT Saccharomyces cerevisiae.";
RL Nat. Cell Biol. 6:861-871(2004).
RN [9]
RP MUTAGENESIS OF LYS-46; 48-ASP-LYS-49; LYS-73; ARG-75; 79-LYS-HIS-80;
RP 84-GLU-ASP-85; ASP-87; 108-GLU-HIS-109; ASP-162; GLU-165; 214-GLU--GLU-216;
RP 222-LYS--LYS-224; 233-LYS--GLU-235; 236-GLU--LYS-238; LYS-251; ASP-254;
RP 263-ASP-ARG-264; ARG-266; GLU-269; LYS-294; ASP-296; ASP-298; ASP-326;
RP GLU-328; 344-GLU--LYS-346; 368-LYS-LYS-369 AND ASP-371.
RX PubMed=16415535; DOI=10.1247/csf.30.57;
RA Igarashi R., Suzuki M., Nogami S., Ohya Y.;
RT "Molecular dissection of ARP1 regions required for nuclear migration and
RT cell wall integrity checkpoint functions in Saccharomyces cerevisiae.";
RL Cell Struct. Funct. 30:57-67(2005).
RN [10]
RP INTERACTION WITH JNM1, AND MUTAGENESIS OF ASP-2; ASP-6; LYS-46;
RP 48-ASP-LYS-49; 84-GLU-ASP-85; GLU-133; ASP-136; ARG-185; ASP-187;
RP 214-GLU--GLU-216; ARG-219; 222-LYS--LYS-224; 233-LYS--LYS-238; LYS-251;
RP ASP-254; ARG-266; GLU-269; 321-ASP-ARG-322; ASP-326; GLU-328; LYS-336;
RP LYS-338; 344-GLU--LYS-346; LYS-369; ASP-371; 374-GLU-ASP-375 AND ARG-378.
RX PubMed=15975903; DOI=10.1091/mbc.e05-02-0093;
RA Clark S.W., Rose M.D.;
RT "Alanine scanning of Arp1 delineates a putative binding site for
RT Jnm1/dynamitin and Nip100/p150Glued.";
RL Mol. Biol. Cell 16:3999-4012(2005).
RN [11]
RP SUBCELLULAR LOCATION, SELF-ASSOCIATION, AND INTERACTION WITH ARP10 AND
RP JNM1.
RX PubMed=16291862; DOI=10.1091/mbc.e05-05-0449;
RA Clark S.W., Rose M.D.;
RT "Arp10p is a pointed-end-associated component of yeast dynactin.";
RL Mol. Biol. Cell 17:738-748(2006).
CC -!- FUNCTION: Core component of the dynactin complex which assists
CC cytoplasmic dynein by increasing its processivity and by regulation of
CC its cargo binding (By similarity). The dynactin complex is required for
CC the spindle translocation late in anaphase and is involved in a cell
CC wall synthesis checkpoint. ARP1 forms the backbone filament of the
CC dynactin rod structure and serves as the scaffold for the remaining
CC subunits. Required for proper orientation of the mitotic spindle.
CC {ECO:0000250, ECO:0000269|PubMed:15311283, ECO:0000269|PubMed:9658168}.
CC -!- SUBUNIT: Self-associates to form an actin-like filament of 8-10
CC monomers. Component of the dynactin complex composed of at least ARP1,
CC JNM1, NIP100 and ARP10. Dynactin comprises a short rod of the ARP1
CC filament attached to ARP10 at its pointed-end and probably associated
CC with the capping protein at its barbed-end. The rod is implicated in
CC dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1
CC filament and is implicated in motor binding (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P38696; Q04549: ARP10; NbExp=5; IntAct=EBI-2920, EBI-2977;
CC P38696; P36224: JNM1; NbExp=7; IntAct=EBI-2920, EBI-9415;
CC P38696; P33420: NIP100; NbExp=4; IntAct=EBI-2920, EBI-12049;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:16291862}. Membrane {ECO:0000269|PubMed:16291862}.
CC Note=Membrane-associated.
CC -!- MISCELLANEOUS: Present with 1580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily. {ECO:0000305}.
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DR EMBL; X79811; CAA56206.1; -; Genomic_DNA.
DR EMBL; U10398; AAB68412.1; -; Genomic_DNA.
DR EMBL; AY693084; AAT93103.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06822.1; -; Genomic_DNA.
DR PIR; S48973; S48973.
DR RefSeq; NP_011997.1; NM_001179259.1.
DR AlphaFoldDB; P38696; -.
DR SMR; P38696; -.
DR BioGRID; 36562; 438.
DR ComplexPortal; CPX-1805; Dynactin.
DR DIP; DIP-1205N; -.
DR IntAct; P38696; 13.
DR MINT; P38696; -.
DR STRING; 4932.YHR129C; -.
DR MaxQB; P38696; -.
DR PaxDb; P38696; -.
DR PRIDE; P38696; -.
DR DNASU; 856530; -.
DR EnsemblFungi; YHR129C_mRNA; YHR129C; YHR129C.
DR GeneID; 856530; -.
DR KEGG; sce:YHR129C; -.
DR SGD; S000001171; ARP1.
DR VEuPathDB; FungiDB:YHR129C; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000170518; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P38696; -.
DR OMA; YTTWTGG; -.
DR BioCyc; YEAST:G3O-31168-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P38696; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38696; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005869; C:dynactin complex; IDA:SGD.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:SGD.
DR GO; GO:0030048; P:actin filament-based movement; IC:ComplexPortal.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
DR GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IGI:SGD.
DR GO; GO:0007097; P:nuclear migration; IMP:SGD.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Dynein; Membrane; Microtubule; Reference proteome.
FT CHAIN 1..384
FT /note="Centractin"
FT /id="PRO_0000089066"
FT MUTAGEN 2
FT /note="D->A: Temperature-sensitive; when associated with A-
FT 6."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 6
FT /note="D->A: Temperature-sensitive; when associated with A-
FT 2."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 46
FT /note="K->A: Strongly reduces interaction with JNM1.
FT Reduces nuclear migration in mitosis; when associated with
FT 48-A-A-49."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 48..49
FT /note="DK->AA: Strongly reduces interaction with JNM1.
FT Reduces nuclear migration in mitosis; when associated with
FT A-46."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 73
FT /note="K->A: Reduces spindle formation; when associated
FT with A-75."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 75
FT /note="R->A: Reduces spindle formation; when associated
FT with A-73."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 79..80
FT /note="KH->AA: Reduces nuclear migration in mitosis."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 84..85
FT /note="ED->AA: Reduces spindle formation. Strongly reduces
FT interaction with JNM1. Reduces nuclear migration in
FT mitosis; when associated with A-87."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 87
FT /note="D->A: Reduces spindle formation. Reduces nuclear
FT migration in mitosis; when associated with 84-A-A-85."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 108..109
FT /note="EH->AA: Reduces nuclear migration in mitosis."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 133
FT /note="E->A: Lethal. Strongly reduces interaction with
FT JNM1; when associated with A-136."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 136
FT /note="D->A: Lethal. Strongly reduces interaction with
FT JNM1; when associated with A-133."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 162
FT /note="D->A: Reduces spindle formation. Reduces nuclear
FT migration in mitosis; when associated with A-165."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 165
FT /note="E->A: Reduces spindle formation. Reduces nuclear
FT migration in mitosis; when associated with A-162."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 185
FT /note="R->A: Temperature-sensitive. Strongly reduces
FT interaction with JNM1; when associated with A-187."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 187
FT /note="D->A: Temperature-sensitive. Strongly reduces
FT interaction with JNM1; when associated with A-185."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 214..216
FT /note="ERE->AAA: Lethal. Reduces spindle formation. Reduces
FT nuclear migration in mitosis. Alters complex assembly; when
FT associated with A-219."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 219
FT /note="R->A: Lethal; when associated with 214-A--A-216."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 222..224
FT /note="KEK->AAA: Lethal. Reduces spindle formation. Reduces
FT nuclear migration in mitosis."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 233..238
FT /note="KKEEEK->AAAAAA: Temperature-sensitive. Strongly
FT reduces interaction with JNM1."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 233..235
FT /note="KKE->AAA: Reduces spindle formation."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 236..238
FT /note="EEK->AAA: Reduces spindle formation."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 251
FT /note="K->A: Lethal and dominant cold-sensitive. Reduces
FT nuclear migration in mitosis; when associated with A-254."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 254
FT /note="D->A: Lethal and dominant cold-sensitive. Reduces
FT nuclear migration in mitosis; when associated with A-251."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 263..264
FT /note="DR->AA: Reduces spindle formation."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 266
FT /note="R->A: Lethal. Reduces spindle formation. Reduces
FT nuclear migration in mitosis; when associated with A-269."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 269
FT /note="E->A: Lethal. Reduces spindle formation. Reduces
FT nuclear migration in mitosis; when associated with A-266."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 294
FT /note="K->A: Reduces nuclear migration in mitosis; when
FT associated with A-296 and A-298."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 296
FT /note="D->A: Reduces nuclear migration in mitosis; when
FT associated with A-294 and A-298."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 298
FT /note="D->A: Reduces nuclear migration in mitosis; when
FT associated with A-294 and A-296."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 321..322
FT /note="DR->AA: Lethal. Strongly reduces interaction with
FT JNM1."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 326
FT /note="D->A: Temperature-sensitive. Reduces nuclear
FT migration in mitosis. Strongly reduces interaction with
FT JNM1; when associated with A-328."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 328
FT /note="E->A: Temperature-sensitive. Reduces nuclear
FT migration in mitosis. Strongly reduces interaction with
FT JNM1; when associated with A-326."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 336
FT /note="K->A: Strongly reduces interaction with JNM1; when
FT associated with A-338."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 338
FT /note="K->A: Strongly reduces interaction with JNM1; when
FT associated with A-336."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 344..346
FT /note="ERK->AAA: Temperature-sensitive. Reduces nuclear
FT migration in mitosis. Strongly reduces interaction with
FT JNM1."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 368..369
FT /note="KK->AA: Reduces nuclear migration in mitosis; when
FT associated with A-371."
FT /evidence="ECO:0000269|PubMed:16415535"
FT MUTAGEN 369
FT /note="K->A: Lethal. Strongly reduces interaction with
FT JNM1; when associated with A-371."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 371
FT /note="D->A: Lethal. Strongly reduces interaction with
FT JNM1; when associated with A-369."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 371
FT /note="D->AA: Reduces nuclear migration in mitosis; when
FT associated with 368-A-A-369."
FT /evidence="ECO:0000269|PubMed:15975903,
FT ECO:0000269|PubMed:16415535"
FT MUTAGEN 374..375
FT /note="ED->AA: Temperature-sensitive. Reduces nuclear
FT migration in mitosis. Strongly reduces interaction with
FT JNM1; when associated with A-378."
FT /evidence="ECO:0000269|PubMed:15975903"
FT MUTAGEN 378
FT /note="R->A: Temperature-sensitive. Reduces nuclear
FT migration in mitosis. Strongly reduces interaction with
FT JNM1; when associated with 374-A-A-375."
FT /evidence="ECO:0000269|PubMed:15975903"
FT CONFLICT 3
FT /note="Q -> P (in Ref. 5; AAT93103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 42995 MW; 98EEA90DC9497B81 CRC64;
MDQLSDSYAL YNQPVVIDNG SGIIKAGFSG EERPKALEYC LVGNTKYDKV MLEGLQGDTF
IGNNAQKLRG LLKLRYPIKH GVVEDWDSME LIWSYVLNEV LQLQNIGEHP LLITEAPMNP
LKNREQMAQV LFETFDVSAL YVSNPAVLSL YASGRTTGCV VDCGEGYCST VPIYDGFALP
ASMMRMDIGG ADITEQLQFQ LRKSAGVSLF SSSEREIVRT MKEKVCYLAK NIKKEEEKYL
QGTQDLISTF KLPDGRCIEV GNDRYRAPEI LFSPQIIGLG YDGLSDMCMQ SIWKVDLDLR
KPLLSSIILS GGTTTLKGFG DRMLWDLEAL TKGTSKIKII APSERKYTTW IGGSILTGLS
TFQRLWTKKS DWLEDSTRVY SNLM
