(data stored in ACNUC27125 zone)

HOGENOM: MOUSE3_PE2104

ID   MOUSE3_PE2104                        STANDARD;      PRT;   511 AA.
AC   MOUSE3_PE2104; P63328; P12816; P20652; Q3UCU1; Q64135;
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; (MOUSE3.PE2104).
GN   Name=Ppp3ca; Synonyms=Calna;
OS   MUS MUSCULUS.
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; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE3.PE2104.
CC       Mus musculus chromosome 3 NCBIM37  sequence 1..159599783 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:PP2BA_MOUSE
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein
CC       phosphatase. This subunit may have a role in the calmodulin
CC       activation of calcineurin. Dephosphorylates DNM1L and HSPB1 (By
CC       similarity). Dephosphorylates SSH1.
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. Note=Colocalizes with ACTN1 and
CC       MYOZ2 at the Z line in heart and skeletal muscle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P63328-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P63328-2; Sequence=VSP_018563;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000172699 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000028161;ENSMUST00000070198;ENSMUSP00000071040.
DR   EMBL; AK076570; - ;
DR   EMBL; AK146387; - ;
DR   EMBL; AK150393; - ;
DR   EMBL; J04134; - ;
DR   EMBL; J05479; - ;
DR   EMBL; S78668; - ;
DR   UniProtKB/Swiss-Prot; P63328; P12816; P20652; Q3UCU1; Q64135; -.
DR   EMBL; J05479; AAA37359.1; -; mRNA.
DR   EMBL; AK146387; BAE27131.1; -; mRNA.
DR   EMBL; AK150393; BAE29521.1; -; mRNA.
DR   EMBL; J04134; AAA37432.1; -; mRNA.
DR   EMBL; S78668; AAB34675.1; -; mRNA.
DR   IPI; IPI00121545; -.
DR   IPI; IPI00756703; -.
DR   PIR; A42232; A31257.
DR   RefSeq; NP_032939.1; NM_008913.4.
DR   UniGene; Mm.331389; -.
DR   ProteinModelPortal; P63328; -.
DR   SMR; P63328; 1-372.
DR   IntAct; P63328; 6.
DR   MINT; MINT-135995; -.
DR   STRING; P63328; -.
DR   PhosphoSite; P63328; -.
DR   PRIDE; P63328; -.
DR   Ensembl; ENSMUST00000056758; ENSMUSP00000053101; ENSMUSG00000028161.
DR   Ensembl; ENSMUST00000070198; ENSMUSP00000071040; ENSMUSG00000028161.
DR   GeneID; 19055; -.
DR   KEGG; mmu:19055; -.
DR   UCSC; uc008rmh.1; mouse.
DR   CTD; 5530; -.
DR   MGI; MGI:107164; Ppp3ca.
DR   eggNOG; roNOG11256; -.
DR   GeneTree; ENSGT00530000063087; -.
DR   InParanoid; P63328; -.
DR   OMA; SVWPAGP; -.
DR   OrthoDB; EOG4PVNZK; -.
DR   PhylomeDB; P63328; -.
DR   NextBio; 295542; -.
DR   ArrayExpress; P63328; -.
DR   Bgee; P63328; -.
DR   Genevestigator; P63328; -.
DR   GermOnline; ENSMUSG00000028161; Mus musculus.
DR   GO; GO:0005955; C:calcineurin complex; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IGI:MGI.
DR   GO; GO:0050804; P:regulation of synaptic transmission; IMP:MGI.
DR   GO; GO:0006950; P:response to stress; IDA:MGI.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
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; MOUSE3.PE2104; -.
KW   ENSMUSG000000281615old_1320000031; ENSMUSP000000710401old_1320000031;
KW   Q8C649_MOUSE; AK076570; AK146387; AK150393; J04134; J05479; S78668;
KW   Alternative splicing; Calmodulin-binding; Complete proteome;
KW   Direct protein sequencing; Hydrolase; Iron; Metal-binding; Nitration;
KW   Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome;
KW   Zinc.
SQ   SEQUENCE   511 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 HNNLLSILRA HEAQDAGYRM YRKSQTTGFP
     SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK
     VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV
     LTLKGLTPTG MLPSGVLSGG KQTLQSAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDAM
     PSDANLNSIN KALASETNGT DSNGSNSSNI Q
//

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