ID Q5KCZ4_CRYNJ Unreviewed; 705 AA.
AC Q5KCZ4; Q55IQ3;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN OrderedLocusNames=CNH02750 {ECO:0000313|EMBL:AAW45141.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW45141.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW45141.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
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DR EMBL; AE017348; AAW45141.1; -; Genomic_DNA.
DR RefSeq; XP_572448.1; XM_572448.1.
DR AlphaFoldDB; Q5KCZ4; -.
DR STRING; 214684.Q5KCZ4; -.
DR PaxDb; 214684-Q5KCZ4; -.
DR EnsemblFungi; AAW45141; AAW45141; CNH02750.
DR GeneID; 3259342; -.
DR KEGG; cne:CNH02750; -.
DR VEuPathDB; FungiDB:CNH02750; -.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_1_1_1; -.
DR InParanoid; Q5KCZ4; -.
DR OMA; VKMFATN; -.
DR OrthoDB; 5473951at2759; -.
DR Proteomes; UP000002149; Chromosome 8.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0000776; C:kinetochore; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005816; C:spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:EnsemblFungi.
DR GO; GO:0070199; P:establishment of protein localization to chromosome; IEA:EnsemblFungi.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IEA:EnsemblFungi.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:EnsemblFungi.
DR GO; GO:0031107; P:septin ring disassembly; IEA:EnsemblFungi.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0031134; P:sister chromatid biorientation; IEA:EnsemblFungi.
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 Reference proteome {ECO:0000313|Proteomes:UP000002149}.
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 79730 MW; D01671870C7C924C CRC64;
MKGLKKAMNL SRTKSSEKSK SPNPPAHKQS TASSGPSSPS VNSPSRQASD APGLQGGAPI
TPRRSPINDK TSPAPPLVVI SGAPQPPPIN TEMPSDPIPH SPHGRYGSPE RTLGADGQPT
PPKVGPMNRL RGPKDTIPAV GKTPRKQRSS RFYVTEKVEI EKLPNFADVR PEQRNELFVQ
KLQQCRVVFD FNDASSDLEG KQIKSQTLHE MLEYITSQRG VITESIYPEV VSMFATNLFR
SIPPQVNPTG DAFDPEEDEP VLELAWPHLQ IVYEFFLRFV ESPDFNTNIG KRYIDQSFVL
QLLELFDSED PRERDFLKTT LHRIYGKFLN LRAFIRRSIS HVFFQFVYET ERHNGIAELL
EILGSIINGF ALPLKEEHKT FLTRALIPLH KAKSLALYHP QLAYCVVQFL EKDPALTEEV
VLGLLRYWPK VNSPKEVMFL NEVEEILDVI EHNEFIKIMQ PLFVQLARCI NSAHFQVAER
ALYYWNNEYI VNLMGEHISI ILPIVFPALY QNSKTHWNRT IHGMVYNALK LFMEINQEVF
EECQNNYRAQ RKAESDRAIE RYDEWLQLRE QAIQNWESAH PSSPLPERLQ EPPPPRPEPY
EDEPMMDVSV DMTANGFDPS ESFTLDRSIA EETVPVADPG VDRAPPLSPT SPTQLLGQQG
QAPSSPTPSG GGTAPHLRRK SVLPIDAGVM RDLQNHRSLE NDANP
//
