CANB1_MOUSE
ID CANB1_MOUSE Reviewed; 170 AA.
AC Q63810; Q3V067; Q5F225;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Calcineurin subunit B type 1;
DE AltName: Full=Protein phosphatase 2B regulatory subunit 1;
DE AltName: Full=Protein phosphatase 3 regulatory subunit B alpha isoform 1;
GN Name=Ppp3r1; Synonyms=Cnb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1325794; DOI=10.1016/s0006-291x(05)81527-x;
RA Ueki K., Muramatsu T., Kincaid R.L.;
RT "Structure and expression of two isoforms of the murine calmodulin-
RT dependent protein phosphatase regulatory subunit (calcineurin B).";
RL Biochem. Biophys. Res. Commun. 187:537-543(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16286645; DOI=10.1073/pnas.0508480102;
RA Sun L., Blair H.C., Peng Y., Zaidi N., Adebanjo O.A., Wu X.B., Wu X.Y.,
RA Iqbal J., Epstein S., Abe E., Moonga B.S., Zaidi M.;
RT "Calcineurin regulates bone formation by the osteoblast.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17130-17135(2005).
RN [5]
RP PROTEIN SEQUENCE OF 58-85; 104-117; 126-135 AND 148-164, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH CIB1, AND SUBCELLULAR LOCATION.
RX PubMed=20639889; DOI=10.1038/nm.2181;
RA Heineke J., Auger-Messier M., Correll R.N., Xu J., Benard M.J., Yuan W.,
RA Drexler H., Parise L.V., Molkentin J.D.;
RT "CIB1 is a regulator of pathological cardiac hypertrophy.";
RL Nat. Med. 16:872-879(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) IN COMPLEX WITH PPP3CA AND CALCIUM,
RP AND FUNCTION.
RX PubMed=26794871; DOI=10.1038/cr.2016.14;
RA Li S.J., Wang J., Ma L., Lu C., Wang J., Wu J.W., Wang Z.X.;
RT "Cooperative autoinhibition and multi-level activation mechanisms of
RT calcineurin.";
RL Cell Res. 26:336-349(2016).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC {ECO:0000269|PubMed:26794871}.
CC -!- SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic
CC subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding
CC subunit (also known as calcineurin B) (PubMed:26794871). There are
CC three catalytic subunits, each encoded by a separate gene (PPP3CA,
CC PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded
CC by separate genes (PPP3R1 and PPP3R2). The regulatory subunit confers
CC calcium sensitivity. Interacts with catalytic subunit
CC PPP3CA/calcineurin A (PubMed:26794871). Interacts with catalytic
CC subunit PPP3CB/calcineurin A (By similarity). Isoform 1 and isoform 2
CC interact with CIB1 (via C-terminal region); the interaction increases
CC upon cardiomyocyte hypertrophy (PubMed:20639889). Interacts with
CC SPATA33 (via PQIIIT motif) (By similarity).
CC {ECO:0000250|UniProtKB:P63098, ECO:0000269|PubMed:20639889,
CC ECO:0000269|PubMed:26794871}.
CC -!- INTERACTION:
CC Q63810; O35099: Map3k5; NbExp=3; IntAct=EBI-6666164, EBI-777493;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20639889}.
CC Cell membrane {ECO:0000269|PubMed:20639889}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:20639889}. Cell membrane
CC {ECO:0000250|UniProtKB:P63098}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P63098}. Note=Translocates from the cytosol to
CC the sarcolemma in a CIB1-dependent manner during cardiomyocyte
CC hypertrophy. {ECO:0000269|PubMed:20639889}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q63810-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63810-2; Sequence=VSP_024842;
CC -!- TISSUE SPECIFICITY: Expressed in osteoblasts and bone marrow (at
CC protein level) (PubMed:16286645). Expressed in the brain, kidney,
CC liver, lung, muscle, ovary, spleen, thymus, heart and testis
CC (PubMed:1325794). {ECO:0000269|PubMed:1325794,
CC ECO:0000269|PubMed:16286645}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000269|PubMed:26794871}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; S43864; AAB23171.1; -; mRNA.
DR EMBL; AK133403; BAE21637.1; -; mRNA.
DR EMBL; AK145541; BAE26495.1; -; mRNA.
DR EMBL; AK160938; BAE36102.1; -; mRNA.
DR EMBL; AK163241; BAE37251.1; -; mRNA.
DR EMBL; AL606466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24448.1; -. [Q63810-1]
DR PIR; JC1220; JC1220.
DR RefSeq; NP_077779.2; NM_024459.2. [Q63810-1]
DR PDB; 4ORB; X-ray; 3.11 A; B=1-170.
DR PDBsum; 4ORB; -.
DR AlphaFoldDB; Q63810; -.
DR SMR; Q63810; -.
DR BioGRID; 202347; 6.
DR ComplexPortal; CPX-1006; Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant.
DR ComplexPortal; CPX-1007; Calcineurin-Calmodulin complex, gamma-R1 variant.
DR ComplexPortal; CPX-1010; Calcineurin-Calmodulin complex, alpha-R1 variant.
DR ComplexPortal; CPX-1011; Calcineurin-Calmodulin complex, beta-R1 variant.
DR ComplexPortal; CPX-1113; Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant.
DR ComplexPortal; CPX-881; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant.
DR IntAct; Q63810; 2.
DR MINT; Q63810; -.
DR STRING; 10090.ENSMUSP00000099944; -.
DR iPTMnet; Q63810; -.
DR PhosphoSitePlus; Q63810; -.
DR EPD; Q63810; -.
DR jPOST; Q63810; -.
DR MaxQB; Q63810; -.
DR PaxDb; Q63810; -.
DR PeptideAtlas; Q63810; -.
DR PRIDE; Q63810; -.
DR ProteomicsDB; 265524; -. [Q63810-1]
DR ProteomicsDB; 265525; -. [Q63810-2]
DR DNASU; 19058; -.
DR Ensembl; ENSMUST00000102880; ENSMUSP00000099944; ENSMUSG00000033953. [Q63810-1]
DR GeneID; 19058; -.
DR KEGG; mmu:19058; -.
DR UCSC; uc007ibz.1; mouse. [Q63810-1]
DR CTD; 5534; -.
DR MGI; MGI:107172; Ppp3r1.
DR VEuPathDB; HostDB:ENSMUSG00000033953; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000156530; -.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; Q63810; -.
DR OMA; DTNFDRD; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q63810; -.
DR TreeFam; TF105558; -.
DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-MMU-2025928; Calcineurin activates NFAT.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR BioGRID-ORCS; 19058; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp3r1; mouse.
DR PRO; PR:Q63810; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q63810; protein.
DR Bgee; ENSMUSG00000033953; Expressed in CA3 field of hippocampus and 261 other tissues.
DR Genevisible; Q63810; MM.
DR GO; GO:0005955; C:calcineurin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IGI:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IMP:MGI.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IC:ComplexPortal.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IMP:SynGO.
DR GO; GO:0014044; P:Schwann cell development; IMP:MGI.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR015757; Calcineur_B.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR45942; PTHR45942; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63099"
FT CHAIN 2..170
FT /note="Calcineurin subunit B type 1"
FT /id="PRO_0000073485"
FT DOMAIN 18..46
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 87..122
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 128..163
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 131..136
FT /note="Calcineurin A binding"
FT /evidence="ECO:0000269|PubMed:26794871"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB"
FT SITE 118
FT /note="Interaction with PxVP motif in substrates of the
FT catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT SITE 122
FT /note="Interaction with PxVP motif in substrates of the
FT catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT MOD_RES 106
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024842"
FT CONFLICT 3
FT /note="N -> S (in Ref. 1; AAB23171)"
FT /evidence="ECO:0000305"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:4ORB"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:4ORB"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:4ORB"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4ORB"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4ORB"
SQ SEQUENCE 170 AA; 19300 MW; C904715DC0386056 CRC64;
MGNEASYPLE MCSHFDADEI KRLGKRFKKL DLDNSGSLSV EEFMSLPELQ QNPLVQRVID
IFDTDGNGEV DFKEFIEGVS QFSVKGDKEQ KLRFAFRIYD MDKDGYISNG ELFQVLKMMV
GNNLKDTQLQ QIVDKTIINA DKDGDGRISF EEFCAVVGGL DIHKKMVVDV
