2ABA_CANTR
ID 2ABA_CANTR Reviewed; 508 AA.
AC P53031;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein phosphatase PP2A regulatory subunit B;
DE AltName: Full=Cell division control protein 55;
DE AltName: Full=PR55;
GN Name=CDC55;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCYC 2512;
RX PubMed=8923737;
RX DOI=10.1002/(sici)1097-0061(199610)12:13<1321::aid-yea27>3.0.co;2-6;
RA Rodriguez P.L., Ali R., Serrano R.;
RT "CtCdc55p and CtHa13p: two putative regulatory proteins from Candida
RT tropicalis with long acidic domains.";
RL Yeast 12:1321-1329(1996).
CC -!- FUNCTION: Phosphatase 2A affects a variety of biological processes in
CC the cell such as transcription, cell cycle progression and cellular
CC morphogenesis, and provides an initial identification of critical
CC substrates for this phosphatase. The regulatory subunit may direct the
CC catalytic subunit to distinct, albeit overlapping, subsets of
CC substrates (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which consist of
CC a core composed of a catalytic subunit associated with a 65 kDa (PR65)
CC (Subunit A) and a 55 kDa (PR55) (Subunit B) regulatory subunit.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; X88899; CAA61361.1; -; Genomic_DNA.
DR PIR; S57751; S57751.
DR AlphaFoldDB; P53031; -.
DR SMR; P53031; -.
DR VEuPathDB; FungiDB:CTMYA2_019400; -.
DR VEuPathDB; FungiDB:CTRG_01251; -.
DR GO; GO:0072686; C:mitotic spindle; IEA:EnsemblFungi.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:EnsemblFungi.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; IEA:EnsemblFungi.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:EnsemblFungi.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR018067; PP2A_PR55_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR Pfam; PF00400; WD40; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 3: Inferred from homology;
KW Cell cycle; Repeat; WD repeat.
FT CHAIN 1..508
FT /note="Protein phosphatase PP2A regulatory subunit B"
FT /id="PRO_0000071440"
FT REPEAT 19..58
FT /note="WD 1"
FT REPEAT 81..122
FT /note="WD 2"
FT REPEAT 166..204
FT /note="WD 3"
FT REPEAT 215..255
FT /note="WD 4"
FT REPEAT 274..312
FT /note="WD 5"
FT REPEAT 329..370
FT /note="WD 6"
FT REPEAT 477..507
FT /note="WD 7"
FT REGION 369..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 57914 MW; 619B4C78BBC7A324 CRC64;
MNLDFSQCFG DKGDIENITE ADIISTVEFD HTGDFLATGD KGGRVVLFER NQSKKKQSCE
YKFFTEFQSH DAEFDYLKSL EIEEKINKIK WLKSANDSLC LLSTNDKTIK LWKIQERQIK
LVSENNLNGL NHLPSSNIGI ESLKLPQLQL HDKLISAQPK KIYANAHAYH INSISVNSDQ
ETYLSADDLR INLWNLGIAD QSFNIVDIKP ANMEELTEVI TSAEFHPLQC NLFMYSSSKG
TIKLSDMRSN SLCDSHAKIF EEYLDPSSHN FFTEITSSIS DVKFSHDGRY IASRDYMTVK
IWDLAMENKP IKTIDVHEHL RERLCDTYEN DAIFDKFEVQ FGGDNKSVMT GSYNNQFVIY
PNAVNTGNDD KPKFKSAFKN SSKRSKKNGF STRTTDDDDD DDDDDDDEEA DDEFDEEVPA
TKNSPGSQLE DDDEQEEIIL QADKSAFKSK KSGQHPMRRR MTSGVGSNLG REFDDVDFKK
SILHLSWHPR ENSVAIAATN NLYIFSTL