(data stored in ACNUC27125 zone)

HOGENOM: RAT2_PE1924

ID   RAT2_PE1924                          STANDARD;      PRT;   521 AA.
AC   RAT2_PE1924; P63329; P12816; P20652; Q6LDJ8; Q9WUV7; Q9Z1I5;
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   alpha isoform; EC=3.1.3 16;AltName: Full=CAM-PRP catalytic
DE   subunit;AltName: Full=Calmodulin-dependent calcineurin A subunit alpha
DE   isoform; (RAT2.PE1924).
GN   Name=Ppp3ca; Synonyms=Calna;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT2.PE1924.
CC       Rattus norvegicus chromosome 2 RGSC3.4  sequence 1..258207540
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PP2BA_RAT
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein
CC       phosphatase. This subunit may have a role in the calmodulin
CC       activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1
CC       (By similarity).
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. Interacts with CRTC2, MYOZ1, MYOZ2 and MYOZ3
CC       Interacts with DNM1L; the interaction dephosphorylates DNM1L and
CC       regulates its translocation to mitochondria (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Colocalizes
CC       with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P63329-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P63329-2; Sequence=VSP_018564;
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000172699 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000009882;ENSRNOT00000013305;ENSRNOP00000013305.
DR   EMBL; D10480; - ;
DR   EMBL; D90035; - ;
DR   EMBL; M29275; - ;
DR   EMBL; M58440; - ;
DR   EMBL; X57115; - ;
DR   UniProtKB/Swiss-Prot; P63329; P12816; P20652; Q6LDJ8; Q9WUV7; Q9Z1I5; -.
DR   EMBL; D90035; BAA14083.1; -; mRNA.
DR   EMBL; M29275; AAA40940.1; -; mRNA.
DR   EMBL; X57115; CAA40398.2; -; mRNA.
DR   EMBL; D10480; BAA01283.1; -; Genomic_DNA.
DR   EMBL; M58440; AAA41914.1; -; mRNA.
DR   IPI; IPI00201410; -.
DR   IPI; IPI00559849; -.
DR   PIR; A33264; A33264.
DR   RefSeq; NP_058737.1; NM_017041.1.
DR   UniGene; Rn.6866; -.
DR   ProteinModelPortal; P63329; -.
DR   SMR; P63329; 1-372.
DR   STRING; P63329; -.
DR   PhosphoSite; P63329; -.
DR   PRIDE; P63329; -.
DR   GeneID; 24674; -.
DR   KEGG; rno:24674; -.
DR   UCSC; NM_017041; rat.
DR   CTD; 5530; -.
DR   RGD; 3382; Ppp3ca.
DR   eggNOG; roNOG11256; -.
DR   GeneTree; ENSGT00530000063087; -.
DR   InParanoid; P63329; -.
DR   OrthoDB; EOG4PVNZK; -.
DR   PhylomeDB; P63329; -.
DR   NextBio; 604055; -.
DR   ArrayExpress; P63329; -.
DR   Genevestigator; P63329; -.
DR   GermOnline; ENSRNOG00000009882; Rattus norvegicus.
DR   GO; GO:0005955; C:calcineurin complex; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; IDA:RGD.
DR   GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IMP:BHF-UCL.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IMP:BHF-UCL.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
DR   GO; GO:0001975; P:response to amphetamine; IEP:RGD.
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; RAT2.PE1924; -.
KW   ENSRNOG00000009882820036002503210000011;
KW   Ppp3ca; PP2BA_RAT; D10480; D90035; M29275; M58440; X57115;
KW   Alternative splicing; Calmodulin-binding; Complete proteome;
KW   Direct protein sequencing; Hydrolase; Iron; Metal-binding; Nucleus;
KW   Phosphoprotein; Protein phosphatase; Reference proteome; Zinc.
SQ   SEQUENCE   521 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV
     ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV
     DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD
     AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG
     NEKTQEHFTH NTVRGCSYFY SYPAVCDFLQ HNNXLSILRA HEAQDAGYRM YRKSQTTGFP
     SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK
     VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV
     LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN
     ERMPPRRDAM PSDANLNSIN KALASETNGT DSNGSNSSNI Q
//

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