ID A0A0K9PPM8_ZOSMR Unreviewed; 469 AA.
AC A0A0K9PPM8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Serine/threonine protein phosphatase 2A regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN ORFNames=ZOSMA_1G01350 {ECO:0000313|EMBL:KMZ70162.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ70162.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment.
CC {ECO:0000256|PIRNR:PIRNR028043}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit.
CC {ECO:0000256|PIRNR:PIRNR028043}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ70162.1}.
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DR EMBL; LFYR01000729; KMZ70162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PPM8; -.
DR STRING; 29655.A0A0K9PPM8; -.
DR OrthoDB; 1457at2759; -.
DR Proteomes; UP000036987; 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:SF31; SERINE_THREONINE PROTEIN PHOSPHATASE 2A 57 KDA REGULATORY SUBUNIT B' KAPPA ISOFORM; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
SQ SEQUENCE 469 AA; 54958 MW; 0491488025027415 CRC64;
MVERREQETT ELGERIFMDC RLDNISTSSP SAKRNPPSAI FPSNVVVGIV PLVAFKDVPD
HEKEKLLIAK LNHCCFIFDF SDPDKNSVEK DIKRQILIHI VDYVSTETFR FTESAIATCC
RMFMENLYRT FPPRYRTAKT NGRENEEDPP VYDPAWWHLQ IVYELLIKFV SSTSLDETIA
NKYLDHIFIS RLLELFDSED PREKDCLKIV VQKIYTKIVS LRPYICKSIN NILYTFPFEK
QKHNGITELL EVFGTVISGF EPPLKEEHKV FLCRTLIPLH KPKNLGSYHL ELTYCLTQFL
EKEPKLSSTL INGLLKYWPV TNSQKEVMFL SELEEILETA SAVEFQKIIF PMFRRIALCL
NSFHYQVAER ALLLWNNAHI VRLIAENRWV ILPLVFPALE RNIREHWNRL VLNATQNVMK
TFTEMDEELF LACQSKFEED RKLQETMEEK HRMTWENLES AASVSKLCV
//
