(data stored in ACNUC27125 zone)

HOGENOM: YEASTXII_PE547

ID   YEASTXII_PE547                       STANDARD;      PRT;   553 AA.
AC   YEASTXII_PE547; P23287; D6VZ68;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit
DE   A1; EC=3.1.3 16;AltName: Full=Calcineurin A1;AltName:
DE   Full=Calmodulin-binding protein 1; (YEASTXII.PE547).
GN   Name=CNA1; Synonyms=CMP1; OrderedLocusNames=YLR433C; ORFNames=L9753.6;
OS   SACCHAROMYCES CEREVISIAE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS YEASTXII.PE547.
CC       Saccharomyces cerevisiae chromosome XII EF2  sequence 1..1078175
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PP2B1_YEAST
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein
CC       phosphatase. This subunit may have a role in the calmodulin
CC       activation of calcineurin.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 Fe(3+) ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Composed of two components (A and B), the A component is
CC       the catalytic subunit and the B component confers calcium
CC       sensitivity.
CC   -!- INTERACTION:
CC       P06787:CMD1; NbExp=4; IntAct=EBI-12771, EBI-3976;
CC   -!- MISCELLANEOUS: Present with 7040 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000172699 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Saccharomyces_cerevisiae;YLR433C;YLR433C;YLR433C.
DR   EMBL; AY693079; - ;
DR   EMBL; M64839; - ;
DR   EMBL; U21094; - ;
DR   EMBL; X54963; - ;
DR   EMBL; X66490; - ;
DR   UniProtKB/Swiss-Prot; P23287; D6VZ68; -.
DR   EMBL; M64839; AAA34465.1; -; Genomic_DNA.
DR   EMBL; X66490; CAA47117.1; -; Genomic_DNA.
DR   EMBL; X54963; CAA38711.1; -; Genomic_DNA.
DR   EMBL; U21094; AAB67518.1; -; Genomic_DNA.
DR   EMBL; AY693079; AAT93098.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09734.1; -; Genomic_DNA.
DR   PIR; S16809; S16809.
DR   RefSeq; NP_013537.1; NM_001182321.1.
DR   ProteinModelPortal; P23287; -.
DR   SMR; P23287; 42-420.
DR   DIP; DIP-662N; -.
DR   IntAct; P23287; 11.
DR   MINT; MINT-397444; -.
DR   STRING; P23287; -.
DR   PeptideAtlas; P23287; -.
DR   EnsemblFungi; YLR433C; YLR433C; YLR433C.
DR   GeneID; 851153; -.
DR   KEGG; sce:YLR433C; -.
DR   NMPDR; fig|4932.3.peg.4567; -.
DR   CYGD; YLR433c; -.
DR   SGD; S000004425; CNA1.
DR   eggNOG; fuNOG05461; -.
DR   GeneTree; EFGT00050000001947; -.
DR   OMA; DLLKQHF; -.
DR   OrthoDB; EOG45XC4G; -.
DR   PhylomeDB; P23287; -.
DR   NextBio; 967933; -.
DR   ArrayExpress; P23287; -.
DR   Genevestigator; P23287; -.
DR   GermOnline; YLR433C; Saccharomyces cerevisiae.
DR   GO; GO:0005955; C:calcineurin complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; TAS:SGD.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fuDR   GO; GO:0006873; P:cellular ion homeostasis; IMP:SGD.
DR   GO; GO:0006873; P:cellular ion homeostasis; IMP:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR   InterPro; IPR004843; Metallo_PEstase_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   HOGENOMDNA; YEASTXII.PE547; -.
KW   YLR433C-A100026476820036002503210000011; YLR433C-A1; PP2B1_YEAST;
KW   M64839; U21094; X54963; X66490;
KW   Calmodulin-binding; Complete proteome; Hydrolase; Iron; Metal-binding;
KW   Protein phosphatase; Reference proteome; Zinc.
SQ   SEQUENCE   553 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSKDLNSSRI KIIKPNDSYI KVDRKKDLTK YELENGKVIS TKDRPIASVP AITGKIPSDE
     EVFDSKTGLP NHSFLREHFF HEGRLSKEQA IKILNMSTVA LSKEPNLLKL KAPITICGDI
     HGQYYDLLKL FEVGGDPAEI DYLFLGDYVD RGAFSFECLI YLYSLKLNNL GRFWMLRGNH
     ECKHLTSYFT FKNEMLHKYD MEVYDACCRS FNVLPLAALM NGQYFCVHGG ISPELKSVED
     VNKINRFREI PSRGLMCDLL WADPVENYDD ARDGSEFDQS EDEFVPNSLR GCSFAFTFKA
     SCKFLKANGL LSIIRAHEAQ DAGYRMYKNN KVTGFPSLIT MFSAPNYLDT YHNKAAVLKY
     EENVMNIRQF HMSPHPYWLP DFMDVFTWSL PFVGEKVTSM LVSILNICSE QELDPESEPK
     AAEETVKARA NATKETGTPS DEKASSAILE DETRRKALRN KILAIAKVSR MFSVLREESE
     KVEYLKTMNA GVLPRGALAR GTEGLNETLS TFEKARKEDL INEKLPPSLS EVEQEKIKYY
     EKILKGAEKK PQL
//

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