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PSRA_DICDI
ID   PSRA_DICDI              Reviewed;         628 AA.
AC   Q54VB6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit psrA;
DE   AltName: Full=Protein PPP2R5A/B56 homolog;
DE   AltName: Full=Protein phosphatase 2A regulatory B subunit;
DE   AltName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit;
DE   AltName: Full=protein phosphatase 2A B56 regulatory subunit homolog;
GN   Name=psrA; Synonyms=B56, DB56; ORFNames=DDB_G0280469;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=18673380; DOI=10.1111/j.1432-0436.2008.00301.x;
RA   Lee N.-S., Veeranki S., Kim B., Kim L.;
RT   "The function of PP2A/B56 in non-metazoan multicellular development.";
RL   Differentiation 76:1104-1110(2008).
CC   -!- FUNCTION: Involved in developmental cell fate decision.
CC       {ECO:0000269|PubMed:18673380}.
CC   -!- SUBUNIT: PP2A consists of a trimeric holoenzyme, composed of a 37 kDa
CC       catalytic subunit (C subunit) and a 65 kDa constant regulatory subunit
CC       (A subunit), that associates with a variety of regulatory subunits (B
CC       subunit) such as phr2AB (B55) and psrA (B56 homolog). The trimer may
CC       partially dissociates into a core 'AC' dimer equally active compared to
CC       the trimer. Seems to play a role in proper anterior patterning (pstO
CC       and pstAB).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18673380}.
CC   -!- DISRUPTION PHENOTYPE: Null cells displays higher PP2A phosphatase
CC       activity compared with the wild type, around 10 hours of delayed
CC       expression of ecmA and ecmB prestalk markers, inefficient culmination
CC       and higher GSK3 kinase activity. {ECO:0000269|PubMed:18673380}.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC       family. {ECO:0000305}.
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DR   EMBL; AAFI02000036; EAL67213.1; -; Genomic_DNA.
DR   RefSeq; XP_641193.1; XM_636101.1.
DR   AlphaFoldDB; Q54VB6; -.
DR   SMR; Q54VB6; -.
DR   STRING; 44689.DDB0302351; -.
DR   PaxDb; Q54VB6; -.
DR   EnsemblProtists; EAL67213; EAL67213; DDB_G0280469.
DR   GeneID; 8622574; -.
DR   KEGG; ddi:DDB_G0280469; -.
DR   dictyBase; DDB_G0280469; psrA.
DR   eggNOG; KOG2085; Eukaryota.
DR   HOGENOM; CLU_012437_3_2_1; -.
DR   InParanoid; Q54VB6; -.
DR   OMA; FMEINQR; -.
DR   PhylomeDB; Q54VB6; -.
DR   Reactome; R-DDI-198753; ERK/MAPK targets.
DR   Reactome; R-DDI-202670; ERKs are inactivated.
DR   Reactome; R-DDI-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-DDI-5673000; RAF activation.
DR   Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-DDI-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   PRO; PR:Q54VB6; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IPI:dictyBase.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IDA:dictyBase.
DR   GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
DR   GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR   GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR   GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
DR   GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:dictyBase.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IMP:dictyBase.
DR   GO; GO:1904643; P:response to curcumin; IMP:dictyBase.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002554; PP2A_B56.
DR   PANTHER; PTHR10257; PTHR10257; 1.
DR   Pfam; PF01603; B56; 1.
DR   PIRSF; PIRSF028043; PP2A_B56; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..628
FT                   /note="Serine/threonine-protein phosphatase 2A regulatory
FT                   subunit psrA"
FT                   /id="PRO_0000368205"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   628 AA;  73394 MW;  12B541AD7FA43FFD CRC64;
     MKNDHINYQQ NLSQSPILNS NKNQTQQNQQ QQQQQQQQNP QQQQQFQHQQ VPQLSPQQIP
     FSEPLKNNLT LQHQQQQQQH QQLAGGQHGS LLRKSYSSRF HEKPQGELTK IANFQDVSPE
     ERPSLFLLKL KQCCYVYDFS DNTYMVSKGV KQEALLQCVN FLSTNDQPLH ESIYKMVFEM
     VAVNLFRPLP PRINPYGVMY DPEEDEPILE AAWPHIQVVY EVLLRFIDSP TFNTHIAKNY
     VDDRFVLQML DLFDSEDPRE RDYLKTTLHR IYGKFLGLRG FIRTAIRNLF CTFVYESHQH
     NGISEILEVL GSIINGFLVP LKDEHKQFLI KVLIPLHKPK SYSVYCSHLG YCMSQFIEKE
     PSLAEPIFKS ILRLWPCGNS QKEVLFLSEM EDLLGLVSDE QFAKFRNQFF RQMTKCFQSE
     HFQVAERALY LFSNENIVLL IASKNNFTLA LETFYKPLHE NSISHWNRSI RNLSISSLKL
     FMEIDMDLFN KISEKYKESK KKQQQIQQRE KFKQNAPETQ KSKQINQNNN NNNNNINNNN
     NNNNNNNGST ETKADKPSMI RRKSLLPVDP STIAALSSHR SLEDIMSTNS NSGNDDDDEN
     NHTNHDSEIE NEVKEDFRVP VNNRYTFT
 
 
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