P2R31_CAEEL
ID P2R31_CAEEL Reviewed; 404 AA.
AC O02217; A5Z2U4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1 {ECO:0000305};
DE AltName: Full=Regulator of spindle assembly protein 1 {ECO:0000303|PubMed:17218259};
DE AltName: Full=Serine/threonine-protein phosphatase 2A 72kDa regulatory subunit rsa-1 {ECO:0000305};
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' rsa-1 {ECO:0000305};
GN Name=rsa-1 {ECO:0000312|WormBase:C25A1.9a};
GN ORFNames=C25A1.9 {ECO:0000312|WormBase:C25A1.9a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH LET-92; PAA-1; RSA-2; SPD-5 AND TPXL-1,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17218259; DOI=10.1016/j.cell.2006.10.050;
RA Schlaitz A.L., Srayko M., Dammermann A., Quintin S., Wielsch N.,
RA MacLeod I., de Robillard Q., Zinke A., Yates J.R. III, Mueller-Reichert T.,
RA Shevchenko A., Oegema K., Hyman A.A.;
RT "The C. elegans RSA complex localizes protein phosphatase 2A to centrosomes
RT and regulates mitotic spindle assembly.";
RL Cell 128:115-127(2007).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-319.
RX PubMed=23336080; DOI=10.1242/bio.20122956;
RA Lange K.I., Heinrichs J., Cheung K., Srayko M.;
RT "Suppressor mutations identify amino acids in PAA-1/PR65 that facilitate
RT regulatory RSA-1/B'' subunit targeting of PP2A to centrosomes in C.
RT elegans.";
RL Biol. Open 2:88-94(2013).
CC -!- FUNCTION: Regulatory subunit of phosphatase let-92 which recruits let-
CC 92/paa-1 complex to the centrosomes, thereby regulating microtubule
CC outgrowth from centrosomes and mitotic spindle assembly ensuring the
CC stability of kinetochore microtubules. {ECO:0000269|PubMed:17218259,
CC ECO:0000269|PubMed:23336080}.
CC -!- SUBUNIT: Part of a complex consisting of a common heterodimeric core
CC enzyme, composed of catalytic subunit let-92 and constant regulatory
CC subunit paa-1, that associates with a variety of regulatory subunits
CC which confer distinct properties to the holoenzyme. Interacts with rsa-
CC 2, spd-5 and tpxl-1. {ECO:0000269|PubMed:17218259}.
CC -!- INTERACTION:
CC O02217; G5EFV3: rsa-2; NbExp=5; IntAct=EBI-1187455, EBI-1187461;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17218259,
CC ECO:0000269|PubMed:23336080}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C25A1.9a};
CC IsoId=O02217-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C25A1.9b};
CC IsoId=O02217-2; Sequence=VSP_058569;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes defects in spindle
CC assembly characterized by kinetochore microtubule instability and a
CC reduction in centrosomal microtubules, a decrease in outgrowth of
CC microtubule plus ends from centrosomes. tpxl-1 recruitment to
CC centrosomes is reduced whereas microtubule-depolymerizing kinesin klp-7
CC recruitment is increased. {ECO:0000269|PubMed:17218259}.
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DR EMBL; BX284601; CAB02769.1; -; Genomic_DNA.
DR EMBL; BX284601; CAN99683.1; -; Genomic_DNA.
DR PIR; T19445; T19445.
DR RefSeq; NP_001122424.1; NM_001128952.2. [O02217-2]
DR RefSeq; NP_492683.1; NM_060282.5. [O02217-1]
DR AlphaFoldDB; O02217; -.
DR ComplexPortal; CPX-1357; RSA centrosome-targeting complex.
DR ComplexPortal; CPX-1361; PP2A-RSA-1 phosphatase complex.
DR IntAct; O02217; 6.
DR STRING; 6239.C25A1.9a; -.
DR EPD; O02217; -.
DR PaxDb; O02217; -.
DR EnsemblMetazoa; C25A1.9a.1; C25A1.9a.1; WBGene00007710. [O02217-1]
DR EnsemblMetazoa; C25A1.9b.1; C25A1.9b.1; WBGene00007710. [O02217-2]
DR GeneID; 172886; -.
DR KEGG; cel:CELE_C25A1.9; -.
DR UCSC; C25A1.9a; c. elegans.
DR CTD; 172886; -.
DR WormBase; C25A1.9a; CE18532; WBGene00007710; rsa-1. [O02217-1]
DR WormBase; C25A1.9b; CE08375; WBGene00007710; rsa-1. [O02217-2]
DR eggNOG; KOG2562; Eukaryota.
DR HOGENOM; CLU_681942_0_0_1; -.
DR InParanoid; O02217; -.
DR OMA; HKFWAYE; -.
DR OrthoDB; 1119300at2759; -.
DR PhylomeDB; O02217; -.
DR Reactome; R-CEL-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-CEL-451308; Activation of Ca-permeable Kainate Receptor.
DR SignaLink; O02217; -.
DR PRO; PR:O02217; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00007710; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:WormBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:WormBase.
DR GO; GO:0033365; P:protein localization to organelle; IMP:WormBase.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..404
FT /note="Serine/threonine-protein phosphatase 2A regulatory
FT subunit rsa-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437753"
FT VAR_SEQ 335..338
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058569"
FT MUTAGEN 319
FT /note="D->G: In or598; embryonic lethal. Defects in mitotic
FT spindle formation and reduced paa-1 levels at mitotic
FT centrosomes with normal rsa-1 centrosome localization. May
FT prevent interaction with paa-1."
FT /evidence="ECO:0000269|PubMed:23336080"
SQ SEQUENCE 404 AA; 46805 MW; AA18C957ABDFDB35 CRC64;
MPTDEPSKRK SILPTIPTSL MLKKSNEALS DFERTFNDRV MDIFAENRRI DVEEFKKNAE
CFLNIIRSNK IDLNWGEGGE SRYVTITRLM KILKTSPQSI KDLLPHNTVS NFVKITNYNL
TIDITLLEEL VRTVIHAEES YIKLLPFSEN STEISSYSLQ DFVATHFIPI MIEEPENPVY
YTAYAVGTIF FLLGARRRDC VYLKDLLAST LLLQLEECIH AENHCLSPPK IDVFTVAQFR
TTLSEFRFLD SQRKGLLAPA DLKFFRDGIF NEVFTKRIFE ISITYEDGRI DFKAFVDFVT
ALKFRHTTAS AKYHFEILDL KDDGLLDEEE IRSISSFQLQ NLPDYVPEDN SVNPEVATAE
LRDMMRLNQN GITLEEFLAN RMNSTFAGFL SNSDDYMKYE RREQ
