ID A0A0K0DVS2_STRER Unreviewed; 483 AA.
AC A0A0K0DVS2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Serine/threonine protein phosphatase 2A regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN Name=pptr-2 {ECO:0000313|EMBL:QWX95810.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000133800.1};
RN [1] {ECO:0000313|EMBL:QWX95810.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PV001 {ECO:0000313|EMBL:QWX95810.1};
RX PubMed=23145190;
RA Stoltzfus JD, Minot S, Berriman M, Nolan TJ Lok.JB.;
RT "RNAseq analysis of the parasitic nematode Strongyloides stercoralis
RT reveals divergent regulation of canonical dauer pathways.";
RL PLoS Negl. Trop. Dis. 6:0-e1854(2012).
RN [2] {ECO:0000313|WBParaSite:SSTP_0000133800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
RN [3] {ECO:0000313|EMBL:QWX95810.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PV001 {ECO:0000313|EMBL:QWX95810.1};
RX PubMed=33859232;
RA Gonzalez Akimori D, Dalessandro EJ, Nolan TJ, Stieha CR,
RA Lok JB Stoltzfus.JDC.;
RT "Transcriptional profiles in Strongyloides stercoralis males reveal
RT deviations from the Caenorhabditis sex determination model.";
RL Sci. Rep. 11:0-8254(2021).
RN [4] {ECO:0000313|EMBL:QWX95810.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PV001 {ECO:0000313|EMBL:QWX95810.1};
RA Stoltzfus J.D.C.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000256|ARBA:ARBA00009745}.
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DR EMBL; MZ297850; QWX95810.1; -; mRNA.
DR STRING; 6248.A0A0K0DVS2; -.
DR WBParaSite; SSTP_0000133800.1; SSTP_0000133800.1; SSTP_0000133800.
DR Proteomes; UP000035681; Unassembled WGS sequence.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; SERINE/THREONINE PROTEIN PHOSPHATASE 2A PP2A REGULATORY SUBUNIT B; 1.
DR PANTHER; PTHR10257:SF3; WELL-ROUNDED, ISOFORM B; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681}.
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..458
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 55986 MW; B2876328C39CD345 CRC64;
MNSQVEDRNL KEDNDADSKI QEDSSDVNKN TELEKLNSIN HNISSTSTST QADNDDDEPI
TEKYIIQMLN ECCKVCDFTN DINLEEIERK RGKLLELAEI FSHPGFEQTP ELWDALTKMF
AENVFRVLSP PTVGPSGEFD PEEDEPQTDP SWPHLQLVYE IFLRAIGSAD FKAPVAKPYM
ERDMFAVKIL DLFDSEDPRE RDILKSTIHR IYAKFLPLRT TLRKHINNIF YTFIYETERH
NGIGELLEIL GSIINGFALP LKSEHKCFLF RVLMPLHKPK CLSLYQIPLS YCVVQFVEKD
PSLSEQIILN LLRYWPKNNS PKEIMFLNEI EEVLDVMESK HFESVMVPLC QQLAKSVSSP
HFQVSERALF FFNNEYVMNL ITEYASTLIP IVFPALYKTS KTHWNKTIGG LIYNAMKVFM
TANQCLVNEC TENFNKELQR QEEQQKNKEK MWEKVERLAK ENPCYHIYAG LKNNSESSSD
GTL
//