CANB2_HUMAN
ID CANB2_HUMAN Reviewed; 170 AA.
AC Q96LZ3; Q5VTR4; Q7Z4V8; Q8WYJ4;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Calcineurin subunit B type 2;
DE AltName: Full=Calcineurin B-like protein;
DE Short=CBLP;
DE AltName: Full=Calcineurin BII;
DE Short=CNBII;
DE AltName: Full=PPP3R1-like;
DE AltName: Full=Protein phosphatase 2B regulatory subunit 2;
DE AltName: Full=Protein phosphatase 3 regulatory subunit B beta isoform;
GN Name=PPP3R2; Synonyms=CBLP, PPP3RL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15865209; DOI=10.1007/s11033-004-4250-4;
RA Liu L., Zhang J., Yuan J., Dang Y., Yang C., Chen X., Xu J., Yu L.;
RT "Characterization of a human regulatory subunit of protein phosphatase 3
RT gene (PPP3RL) expressed specifically in testis.";
RL Mol. Biol. Rep. 32:41-45(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Guo J.H., She X.Y., Dai F.Y., Yu L.;
RT "cDNA cloning of a novel calcineurin B-like protein (CBLP).";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tu Q., Yu L., Bi A., Zhang H., He W., Zhao S.;
RT "Cloning of a novel human cDNA, CNBII, whose product shows significant
RT homology to calcineurin B.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH SPATA33.
RX PubMed=34446558; DOI=10.1073/pnas.2106673118;
RA Miyata H., Oura S., Morohoshi A., Shimada K., Mashiko D., Oyama Y.,
RA Kaneda Y., Matsumura T., Abbasi F., Ikawa M.;
RT "SPATA33 localizes calcineurin to the mitochondria and regulates sperm
RT motility in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC {ECO:0000250|UniProtKB:P63098}.
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). There are three catalytic
CC subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC)
CC and two regulatory subunits which are also encoded by separate genes
CC (PPP3R1 and PPP3R2) (By similarity). Interacts with SPATA33 (via PQIIIT
CC motif) (PubMed:34446558). {ECO:0000250|UniProtKB:P63098,
CC ECO:0000269|PubMed:34446558}.
CC -!- INTERACTION:
CC Q96LZ3; Q12800: TFCP2; NbExp=3; IntAct=EBI-3906025, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q63811}.
CC Note=Localizes in the mitochondria in a SPATA33-dependent manner.
CC {ECO:0000250|UniProtKB:Q63811}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15865209}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000250|UniProtKB:P63098}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30595.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH66299.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP57772.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71521.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW58961.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF145026; AAP97278.1; -; mRNA.
DR EMBL; AF400667; AAP57772.1; ALT_INIT; mRNA.
DR EMBL; AF085237; AAL40395.1; -; mRNA.
DR EMBL; AK057524; BAB71521.1; ALT_INIT; mRNA.
DR EMBL; AL591377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58961.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC030595; AAH30595.1; ALT_INIT; mRNA.
DR EMBL; BC066299; AAH66299.1; ALT_INIT; mRNA.
DR CCDS; CCDS6759.1; -.
DR RefSeq; NP_671709.1; NM_147180.3.
DR AlphaFoldDB; Q96LZ3; -.
DR SMR; Q96LZ3; -.
DR BioGRID; 111527; 31.
DR ComplexPortal; CPX-1002; Calcineurin-Calmodulin complex, beta-R2 variant.
DR ComplexPortal; CPX-1048; Calcineurin-Calmodulin complex, alpha-R2 variant.
DR ComplexPortal; CPX-1050; Calcineurin-Calmodulin complex, gamma-R2 variant.
DR ComplexPortal; CPX-1114; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant.
DR ComplexPortal; CPX-1116; Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant.
DR ComplexPortal; CPX-1118; Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant.
DR IntAct; Q96LZ3; 14.
DR MINT; Q96LZ3; -.
DR STRING; 9606.ENSP00000363939; -.
DR DrugBank; DB00091; Cyclosporine.
DR DrugBank; DB11693; Voclosporin.
DR CarbonylDB; Q96LZ3; -.
DR iPTMnet; Q96LZ3; -.
DR PhosphoSitePlus; Q96LZ3; -.
DR BioMuta; PPP3R2; -.
DR DMDM; 52000731; -.
DR EPD; Q96LZ3; -.
DR jPOST; Q96LZ3; -.
DR MassIVE; Q96LZ3; -.
DR MaxQB; Q96LZ3; -.
DR PaxDb; Q96LZ3; -.
DR PeptideAtlas; Q96LZ3; -.
DR PRIDE; Q96LZ3; -.
DR ProteomicsDB; 77271; -.
DR Antibodypedia; 29196; 200 antibodies from 28 providers.
DR DNASU; 5535; -.
DR Ensembl; ENST00000374806.2; ENSP00000363939.2; ENSG00000188386.8.
DR GeneID; 5535; -.
DR KEGG; hsa:5535; -.
DR MANE-Select; ENST00000374806.2; ENSP00000363939.2; NM_147180.4; NP_671709.2.
DR UCSC; uc004bbr.3; human.
DR CTD; 5535; -.
DR DisGeNET; 5535; -.
DR GeneCards; PPP3R2; -.
DR HGNC; HGNC:9318; PPP3R2.
DR HPA; ENSG00000188386; Tissue enriched (testis).
DR MIM; 613821; gene.
DR neXtProt; NX_Q96LZ3; -.
DR OpenTargets; ENSG00000188386; -.
DR PharmGKB; PA33682; -.
DR VEuPathDB; HostDB:ENSG00000188386; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000165130; -.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; Q96LZ3; -.
DR OMA; SYPAEMC; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q96LZ3; -.
DR TreeFam; TF105558; -.
DR BRENDA; 3.1.3.16; 2681.
DR PathwayCommons; Q96LZ3; -.
DR SignaLink; Q96LZ3; -.
DR BioGRID-ORCS; 5535; 11 hits in 1070 CRISPR screens.
DR GeneWiki; PPP3R2; -.
DR GenomeRNAi; 5535; -.
DR Pharos; Q96LZ3; Tbio.
DR PRO; PR:Q96LZ3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96LZ3; protein.
DR Bgee; ENSG00000188386; Expressed in adult organism and 32 other tissues.
DR ExpressionAtlas; Q96LZ3; baseline and differential.
DR Genevisible; Q96LZ3; HS.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR GO; GO:0097226; C:sperm mitochondrial sheath; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IDA:MGI.
DR GO; GO:0019902; F:phosphatase binding; IBA:GO_Central.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
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:0007341; P:penetration of zona pellucida; IEA:Ensembl.
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:1901387; P:positive regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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 Calcium; Lipoprotein; Metal-binding; Mitochondrion; Myristate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..170
FT /note="Calcineurin subunit B type 2"
FT /id="PRO_0000073499"
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:0000250|UniProtKB:P63098"
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 BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT CONFLICT 16
FT /note="D -> N (in Ref. 3; AAL40395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 170 AA; 19533 MW; 322F9CA4123BA2C3 CRC64;
MGNEASYPAE MCSHFDNDEI KRLGRRFKKL DLDKSGSLSV EEFMSLPELR HNPLVRRVID
VFDTDGDGEV DFKEFILGTS QFSVKGDEEQ KLRFAFSIYD MDKDGYISNG ELFQVLKMMV
GNNLTDWQLQ QLVDKTIIIL DKDGDGKISF EEFSAVVRDL EIHKKLVLIV
