2AB1_CAEEL
ID 2AB1_CAEEL Reviewed; 495 AA.
AC G5EDR3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit sur-6 {ECO:0000305};
DE AltName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit sur-6 {ECO:0000305};
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B sur-6 {ECO:0000305};
DE Short=SUR-6/B55 {ECO:0000303|PubMed:21497766, ECO:0000303|PubMed:24192838};
DE Short=SUR-6/PR55 {ECO:0000303|PubMed:14724126};
GN Name=sur-6 {ECO:0000312|WormBase:F26E4.1};
GN ORFNames=F26E4.1 {ECO:0000312|WormBase:F26E4.1};
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|EMBL:AAD51977.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF GLU-230 AND CYS-302.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAD51977.1};
RX PubMed=10521400; DOI=10.1101/gad.13.19.2562;
RA Sieburth D.S., Sundaram M., Howard R.M., Han M.;
RT "A PP2A regulatory subunit positively regulates Ras-mediated signaling
RT during Caenorhabditis elegans vulval induction.";
RL Genes Dev. 13:2562-2569(1999).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14724126; DOI=10.1242/dev.00987;
RA Kao G., Tuck S., Baillie D., Sundaram M.V.;
RT "C. elegans SUR-6/PR55 cooperates with LET-92/protein phosphatase 2A and
RT promotes Raf activity independently of inhibitory Akt phosphorylation
RT sites.";
RL Development 131:755-765(2004).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH LET-92, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21497766; DOI=10.1016/j.devcel.2011.03.007;
RA Song M.H., Liu Y., Anderson D.E., Jahng W.J., O'Connell K.F.;
RT "Protein phosphatase 2A-SUR-6/B55 regulates centriole duplication in C.
RT elegans by controlling the levels of centriole assembly factors.";
RL Dev. Cell 20:563-571(2011).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24192838; DOI=10.1534/g3.113.006718;
RA Jiu Y., Hasygar K., Tang L., Liu Y., Holmberg C.I., Buerglin T.R.,
RA Hietakangas V., Jaentti J.;
RT "par-1, atypical pkc, and PP2A/B55 sur-6 are implicated in the regulation
RT of exocyst-mediated membrane trafficking in Caenorhabditis elegans.";
RL G3 (Bethesda) 4:173-183(2014).
CC -!- FUNCTION: Probable regulatory subunit of serine/threonine phosphatase
CC let-92. Together with let-92 and constant regulatory subunit paa-1,
CC positively regulates centriole duplication during early embryonic cell
CC divisions by preventing the degradation of sas-5 and kinase zyg-1
CC (PubMed:21497766). In addition, during vulva development, may play a
CC role with phosphatase let-92 and regulatory subunit paa-1 in the
CC induction of vulva cell precursors by positively regulating let-60/Ras-
CC MAP kinase signaling, probably by promoting lin-45 activation
CC (PubMed:10521400, PubMed:14724126). In intestinal epithelial cells, may
CC play a role in the late secretory pathway probably by regulating the
CC exocyst, a protein complex involved in targeting secretory vesicles to
CC the plasma membrane (PubMed:24192838). {ECO:0000269|PubMed:10521400,
CC ECO:0000269|PubMed:14724126, ECO:0000269|PubMed:21497766,
CC ECO:0000269|PubMed:24192838}.
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 (Probable).
CC Interacts with let-92 (PubMed:21497766). {ECO:0000269|PubMed:21497766,
CC ECO:0000303|PubMed:14724126, ECO:0000303|PubMed:21497766}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21497766}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes severe embryonic
CC lethality (PubMed:10521400). In mutants, during the first embryonic
CC divisions, P1 cell initiates division prior to AB cell, spindles appear
CC abnormal or collapse during anaphase and chromatin bridges and
CC supernumerary centrosomes are often detected (PubMed:14724126). In
CC addition, RNAi-mediated knockdown causes a partial defect in centriole
CC duplication during the first embryonic divisions where 24% of spindles
CC are monopolar and 47% have asymmetric spindles, a decrease in the
CC spindle protein sas-5 levels and occasional bridging of chromatin with
CC no obvious defects in cell cycle progression or mitotic exit
CC (PubMed:21497766). The few surviving animals of RNAi-mediated knockdown
CC lack a vulva resulting from defects in vulva cell induction, vulva
CC precursor cell (VPC) generation and in vulval execution lineage, and
CC are slightly uncoordinated (PubMed:10521400). In L4 larvae mutants,
CC somatic mpk-1/ERK phosphorylation is also severely reduced
CC (PubMed:14724126). In intestinal epithelial cells, RNAi-mediated
CC knockdown causes an accumulation of SNARE proteins including snb-1,
CC snap-29 and syx-4 (PubMed:24192838). RNAi-mediated knockdown at the L1
CC larval stage in the exocyst component exoc-8 (ok2523) mutant background
CC results in lethality (PubMed:24192838). {ECO:0000269|PubMed:10521400,
CC ECO:0000269|PubMed:14724126, ECO:0000269|PubMed:21497766,
CC ECO:0000269|PubMed:24192838}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000255|RuleBase:RU331113}.
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DR EMBL; AF174643; AAD51977.1; -; mRNA.
DR EMBL; BX284601; CAB03008.1; -; Genomic_DNA.
DR PIR; T21422; T21422.
DR RefSeq; NP_492591.1; NM_060190.5.
DR AlphaFoldDB; G5EDR3; -.
DR SMR; G5EDR3; -.
DR ComplexPortal; CPX-1366; PP2A-SUR-6 phosphatase complex.
DR IntAct; G5EDR3; 2.
DR STRING; 6239.F26E4.1; -.
DR EPD; G5EDR3; -.
DR PaxDb; G5EDR3; -.
DR PeptideAtlas; G5EDR3; -.
DR EnsemblMetazoa; F26E4.1.1; F26E4.1.1; WBGene00006352.
DR GeneID; 172826; -.
DR KEGG; cel:CELE_F26E4.1; -.
DR CTD; 172826; -.
DR WormBase; F26E4.1; CE09685; WBGene00006352; sur-6.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; G5EDR3; -.
DR OMA; HPISCNW; -.
DR OrthoDB; 810409at2759; -.
DR PhylomeDB; G5EDR3; -.
DR Reactome; R-CEL-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-CEL-69231; Cyclin D associated events in G1.
DR Reactome; R-CEL-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-CEL-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; G5EDR3; -.
DR PRO; PR:G5EDR3; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006352; Expressed in embryo and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0098534; P:centriole assembly; IC:ComplexPortal.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:WormBase.
DR GO; GO:0040028; P:regulation of vulval development; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR Pfam; PF00400; WD40; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..495
FT /note="Serine/threonine-protein phosphatase 2A regulatory
FT subunit sur-6"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437752"
FT REPEAT 64..103
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 130..171
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 215..253
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 264..304
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 323..361
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 378..419
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 464..495
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 230
FT /note="E->K: In cs24; viable with no visible phenotype.
FT Suppresses multivulva formation in a let-60 n1046 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:10521400"
FT MUTAGEN 302
FT /note="C->Y: In ku123; viable with no visible phenotype.
FT Suppresses multivulva formation in a let-60 n1046 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:10521400"
SQ SEQUENCE 495 AA; 57078 MW; 6E41BB4BE4502B70 CRC64;
MVMEVDEPAV AATTSQNQPQ EHANDFDMDT SEGPIENDET FEPVDQINWK FNQVKGNIDA
DVHTEADVIS CVEFSHDGEY LATGDKGGRV VIFQRDQSGK YVKGVRSREY NVYSTFQSHE
PEFDYLKSLE IDEKINQIRW LKKKNAANFI LSTNDKTIKL WKISERERKI GDDAWNLPRT
NRINTSSFRG RLQIPSIVPM ELIVEASPRR VYGNAHTYHV NSISVNSDQE TFLSADDLRV
NLWNLEITNE SFNIVDIKPA NMEELTEVIT AAEFHPTQCN WFVYSSSKGS IRLCDMRDRA
LCDAYAKIFE EPEDPQSRSF FSEIIASVSD VKFSHNGRYL LTRDYLTVKV WDLNMESQPV
ETYPVHNYLR TKLCALYEND SIFDKFECDW SGDDKHILTG SYHNLFRSYA RGNNQDAKTW
EARPQEPHSQ LRSRFVVPSA KRKRNNLSSS GETTEEDLSS DQLQFDRKIL HTAWHPKDNI
IALAATNNLY IFSDV
