RSA2_CAEEL
ID RSA2_CAEEL Reviewed; 949 AA.
AC G5EFV3; G5EDA1;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Regulator of spindle assembly protein 2 {ECO:0000312|WormBase:Y48A6B.11b};
GN Name=rsa-2 {ECO:0000312|WormBase:Y48A6B.11b};
GN ORFNames=Y48A6B.11 {ECO:0000312|WormBase:Y48A6B.11b};
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 RSA-1; TPXL-1 AND SPD-5, SUBCELLULAR LOCATION,
RP 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, INTERACTION WITH SYS-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25819561; DOI=10.1016/j.cub.2015.02.020;
RA Vora S., Phillips B.T.;
RT "Centrosome-associated degradation limits beta-catenin inheritance by
RT daughter cells after asymmetric division.";
RL Curr. Biol. 25:1005-1016(2015).
CC -!- FUNCTION: Recruits rsa-1 and, thereby, phosphatase let-92/paa-1 complex
CC to the centrosomes (PubMed:17218259). Recruits sys-1/beta-catenin to
CC mitotic centrosomes during the first embryonic cell divisions
CC (PubMed:25819561). {ECO:0000269|PubMed:17218259,
CC ECO:0000269|PubMed:25819561}.
CC -!- SUBUNIT: Interacts with phosphatase regulatory subunit rsa-1 and tpxl-1
CC (PubMed:17218259). May interact with spd-5 (PubMed:17218259). May
CC interact with sys-1 (PubMed:25819561). {ECO:0000269|PubMed:17218259,
CC ECO:0000269|PubMed:25819561}.
CC -!- INTERACTION:
CC G5EFV3; Q9GRZ1: ebp-1; NbExp=4; IntAct=EBI-1187461, EBI-313130;
CC G5EFV3; O02217: rsa-1; NbExp=5; IntAct=EBI-1187461, EBI-1187455;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17218259,
CC ECO:0000269|PubMed:25819561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:Y48A6B.11b};
CC IsoId=G5EFV3-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y48A6B.11a};
CC IsoId=G5EFV3-2; Sequence=VSP_058485;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes defects in spindle
CC assembly characterized by kinetochore microtubule instability, a
CC reduction in centrosomal microtubules and a decrease in outgrowth of
CC microtubule plus ends from centrosomes (PubMed:17218259). Also causes a
CC reduction of sys-1/beta-catenin enrichment at centrosomes throughout
CC early embryonic cleavages (PubMed:25819561). Increases sys-1 nuclear
CC accumulation without affecting sys-1 asymmetric distribution in E and
CC MS blastomers (PubMed:25819561). {ECO:0000269|PubMed:17218259,
CC ECO:0000269|PubMed:25819561}.
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DR EMBL; BX284603; CAA19535.2; -; Genomic_DNA.
DR EMBL; BX284603; CAE11312.1; -; Genomic_DNA.
DR PIR; E88594; E88594.
DR PIR; T26314; T26314.
DR RefSeq; NP_001022886.1; NM_001027715.2. [G5EFV3-2]
DR RefSeq; NP_001022887.1; NM_001027716.1. [G5EFV3-1]
DR AlphaFoldDB; G5EFV3; -.
DR SMR; G5EFV3; -.
DR ComplexPortal; CPX-1357; RSA centrosome-targeting complex.
DR IntAct; G5EFV3; 10.
DR STRING; 6239.Y48A6B.11b; -.
DR EPD; G5EFV3; -.
DR PaxDb; G5EFV3; -.
DR EnsemblMetazoa; Y48A6B.11a.1; Y48A6B.11a.1; WBGene00012972. [G5EFV3-2]
DR EnsemblMetazoa; Y48A6B.11b.1; Y48A6B.11b.1; WBGene00012972. [G5EFV3-1]
DR GeneID; 176536; -.
DR KEGG; cel:CELE_Y48A6B.11; -.
DR CTD; 176536; -.
DR WormBase; Y48A6B.11a; CE24379; WBGene00012972; rsa-2. [G5EFV3-2]
DR WormBase; Y48A6B.11b; CE34514; WBGene00012972; rsa-2. [G5EFV3-1]
DR eggNOG; ENOG502TGH4; Eukaryota.
DR HOGENOM; CLU_310188_0_0_1; -.
DR InParanoid; G5EFV3; -.
DR OMA; KMEENFS; -.
DR OrthoDB; 769614at2759; -.
DR SignaLink; G5EFV3; -.
DR PRO; PR:G5EFV3; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012972; 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:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:WormBase.
DR GO; GO:0048566; P:embryonic digestive tract development; IGI:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:WormBase.
DR GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..949
FT /note="Regulator of spindle assembly protein 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437088"
FT REGION 27..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..324
FT /evidence="ECO:0000255"
FT COILED 567..595
FT /evidence="ECO:0000255"
FT COMPBIAS 27..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 40..41
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058485"
SQ SEQUENCE 949 AA; 107767 MW; D02F9AF1ABDB246B CRC64;
MSKIPVFKGS FKSWLAKNDE KPAKSVLLEP KYRDHHEKIS FRNKENMEEG EKPVFVSMAN
PQPTREDYER YDEDRRLKDK ARDLRIARRR NSATPEASPS SDQYFTPEPA DDEFVTPSTS
KKSQKPRSSD ATPVSSKPPR YLPRTPLSEQ YTSCLSRKME ENFSRMQELM ISGHSPHEAR
QQTIQESSEQ LEPRAKVTRS SSQPPPIDTL KPRVPRIESP LVKKTTETPI RRTSYVDTLV
ATHQIQLQYS DRVVVGVERQ MTKLESIKNL AAANRSPIIA EEAKKRRNEA EAVRKLIEVE
TQNAKKRAVI QELKDRIDKL TQAQLAIHQL VSSQPFSGDP YNQRLLRSID NWMALPFREF
DIQTAREMLE LARKMKITID HFRNVATLHR NSKSLNRSLN TSRKSIAVKI NPSSQLNQQS
SSDAAPPPSM REASTQMTSR LAESAMTQTS PRRIGVEPLD LSQLLEKHNS SSQTTPPVVE
PVLAEVSAEP QRPPVTLSMT APVSTIAEFD SMLNSISLHN ESLETVAEPF SRLKTDISFP
STVEETTPRS GRVSLDSESA RRLSAGLSHY LEQVKKERES MEAQESESES MELEIPVVSE
VSVTTESENL EEVVSEHSDS KSPETLVASD NGEDSSGGSE DPNATQFEHE IEEHKEPEKL
GLIIDPEDEQ DETKRFVNHD EFEQSLEEEL EPRGNNDSAD DSGFLLDNSP APRLKSIFDN
LPPAAASAAV TDTPRVPAEA DETTFAGMDM EEYCQREFLK EISPIMVQKA IELQDELRGV
DWLTAQDVWQ PPSFKDVQME FDDNFEYFDS FSILIWSAVV DLINKNYLKF GRKMTENEEI
AFEAEALKML QTEHGPESRK SEWCTDVKMS KKLEGMMPME LDYRYDVRRG LPDAEKQKYQ
WQQVQMTVIA ARYANKNLIN EANEVYATEK EKLGQMVLES EIDATVTDV
