ID A0A0A2JXZ1_PENEN Unreviewed; 678 AA.
AC A0A0A2JXZ1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN ORFNames=PEX2_054970 {ECO:0000313|EMBL:KGO59656.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO59656.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO59656.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO59656.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO59656.1}.
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DR EMBL; JQFZ01000090; KGO59656.1; -; Genomic_DNA.
DR RefSeq; XP_016600769.1; XM_016742771.1.
DR AlphaFoldDB; A0A0A2JXZ1; -.
DR STRING; 27334.A0A0A2JXZ1; -.
DR GeneID; 27678190; -.
DR HOGENOM; CLU_012437_1_2_1; -.
DR OrthoDB; 5473951at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 656..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 77289 MW; 72E026EB85F3B1DD CRC64;
MKGFRQRVHD QLSRAKDNKS SKKKDSNSTS QNQSLGISNT QQSTSPNQGT PTSSTTSLND
SRNKSPDNAS PAGTPSAGAP HPGTPVQHYI PQPGAAGQPV SNGPATPNRQ GQPAAPSVVI
SPSAPHVPPP GAAETMPGDL APPRKSHVFD RLQTTPKDMS EGIRTPKRQH SSRFDISDQR
QRELEKLPGF HEVPPNRRQD LFMQKIDQCN IIFDFNDPTA DMKSKEIKRL ALHELLDYVA
NNRSVITEPM YPRVVEMFAK NLFRPIPPPM TPQGEAFDPE EDEPVLEVAW PHIQVVYEFF
LRFIESQDFN TNIAKGYIDH QFVLSLLNLF DSEDPRERDF LKTTLHRIYG KFLNLRSYIR
RSINNVFFQF MYETERHNGI AELLEILGSI INGFALPLKE EHKLFLTRVL LPMHKVKSLS
MYHPQLAYCI VQFLEKDSSL TEDVVLGLLR FWPKTNSTKE VMYLNEVEDI FEVMDPGEFA
KVQEPLFNQL AKSVASPHFQ VAERALYFWN NEYFCNLVSD NVETILPLMF APLYENSKGH
WNRTIHSMVY NAMKMFMEIN PQLFDECSHD YTEHQNNADQ REKSRTDRWD VIEQQAKDRK
NGIPAPPPPV LDVPEPIDEV EAMTHESQKR LNSLKLQEDP DISKERPSRE GTPNSIRAFL
CGLLLFLFGP IALVLVFC
//
