CPNS1_HUMAN
ID CPNS1_HUMAN Reviewed; 268 AA.
AC P04632; A8K0P1; Q8WTX3; Q96EW0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Calpain small subunit 1;
DE Short=CSS1;
DE AltName: Full=Calcium-activated neutral proteinase small subunit;
DE Short=CANP small subunit;
DE AltName: Full=Calcium-dependent protease small subunit;
DE Short=CDPS;
DE AltName: Full=Calcium-dependent protease small subunit 1;
DE AltName: Full=Calpain regulatory subunit;
GN Name=CAPNS1; Synonyms=CAPN4, CAPNS;
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].
RX PubMed=3016651;
RA Ohno S., Emori Y., Suzuki K.;
RT "Nucleotide sequence of a cDNA coding for the small subunit of human
RT calcium-dependent protease.";
RL Nucleic Acids Res. 14:5559-5559(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3024120; DOI=10.1093/nar/14.22.8805;
RA Miyake S., Emori Y., Suzuki K.;
RT "Gene organization of the small subunit of human calcium-activated neutral
RT protease.";
RL Nucleic Acids Res. 14:8805-8817(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-224.
RG NIEHS SNPs program;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Muscle, Pancreas, Skin, and Uterus;
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 PROTEIN SEQUENCE OF 1-9; 61-84 AND 159-165, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=10639123; DOI=10.1073/pnas.97.2.588;
RA Strobl S., Fernandez-Catalan C., Braun M., Huber R., Masumoto H.,
RA Nakagawa K., Irie A., Sorimachi H., Bourenkow G., Bartunik H., Suzuki K.,
RA Bode W.;
RT "The crystal structure of calcium-free human m-calpain suggests an
RT electrostatic switch mechanism for activation by calcium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:588-592(2000).
CC -!- FUNCTION: Regulatory subunit of the calcium-regulated non-lysosomal
CC thiol-protease which catalyzes limited proteolysis of substrates
CC involved in cytoskeletal remodeling and signal transduction. Essential
CC for embryonic development (By similarity).
CC {ECO:0000250|UniProtKB:O88456}.
CC -!- SUBUNIT: Homodimer or heterodimer of a large (catalytic) and a small
CC (regulatory) subunit. In presence of calcium, the heterodimer
CC dissociates (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P04632; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-711828, EBI-741181;
CC P04632; P17655: CAPN2; NbExp=5; IntAct=EBI-711828, EBI-1028956;
CC P04632; Q96NL8: CFAP418; NbExp=2; IntAct=EBI-711828, EBI-11904873;
CC P04632; P20936: RASA1; NbExp=3; IntAct=EBI-711828, EBI-1026476;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium
CC binding. {ECO:0000250}.
CC -!- DOMAIN: The contact of the 5th EF-hand domain from each monomer allows
CC the formation of the homodimer and also appears to mediate the contact
CC between the large catalytic subunit and small regulatory subunit for
CC the formation of the heterodimer. {ECO:0000250}.
CC -!- DOMAIN: EF-hand domains are paired. EF-hand 1 is paired with EF-hand 2
CC and EF-hand 3 is paired with EF-hand 4. The fifth EF-hand domain, left
CC unpaired, does not bind the calcium but is responsible of the
CC dimerization by EF-embrace. The first four EF-hand domains bind
CC calcium, however it is not sure if the binding of EF-hand 4 to calcium
CC is physiologically relevant.
CC -!- WEB RESOURCE: Name=CaBP; Note=Calpain;
CC URL="http://structbio.vanderbilt.edu/cabp_database/general/prot_pages/calpain.html";
CC -!- WEB RESOURCE: Name=Calpains homepage;
CC URL="https://cals.arizona.edu/calpains/";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/capns1/";
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DR EMBL; X04106; CAA27726.1; -; mRNA.
DR EMBL; M31511; AAA35646.1; -; Genomic_DNA.
DR EMBL; M31502; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; M31503; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; M31504; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; M31505; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; M31506; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; M31507; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; M31508; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; M31509; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; M31510; AAA35646.1; JOINED; Genomic_DNA.
DR EMBL; AK289606; BAF82295.1; -; mRNA.
DR EMBL; BT009775; AAP88777.1; -; mRNA.
DR EMBL; AY789642; AAV40829.1; -; Genomic_DNA.
DR EMBL; AD001527; AAB51183.1; -; Genomic_DNA.
DR EMBL; AC002984; AAB81546.1; -; Genomic_DNA.
DR EMBL; BC000592; AAH00592.1; -; mRNA.
DR EMBL; BC007779; AAH07779.1; -; mRNA.
DR EMBL; BC011903; AAH11903.1; -; mRNA.
DR EMBL; BC017308; AAH17308.1; -; mRNA.
DR EMBL; BC018931; AAH18931.1; -; mRNA.
DR EMBL; BC021933; AAH21933.1; -; mRNA.
DR EMBL; BC023643; AAH23643.1; -; mRNA.
DR EMBL; BC064998; AAH64998.1; -; mRNA.
DR CCDS; CCDS12489.1; -.
DR PIR; A26107; CIHUL.
DR RefSeq; NP_001003962.1; NM_001003962.2.
DR RefSeq; NP_001289561.1; NM_001302632.1.
DR RefSeq; NP_001289562.1; NM_001302633.1.
DR RefSeq; NP_001740.1; NM_001749.3.
DR RefSeq; XP_005259352.1; XM_005259295.1.
DR RefSeq; XP_005259353.1; XM_005259296.1.
DR PDB; 1KFU; X-ray; 2.50 A; S=85-268.
DR PDB; 1KFX; X-ray; 3.15 A; S=85-268.
DR PDB; 4PHJ; X-ray; 1.60 A; A/B=96-268.
DR PDB; 4PHK; X-ray; 2.05 A; A/B=96-268.
DR PDB; 4PHM; X-ray; 2.03 A; A/B=96-268.
DR PDB; 4WQ2; X-ray; 1.64 A; A/B=96-268.
DR PDB; 4WQ3; X-ray; 1.79 A; A/B=96-268.
DR PDB; 5D69; X-ray; 1.97 A; A/B=96-268.
DR PDB; 6QLB; X-ray; 2.32 A; A/B/C/D=96-268.
DR PDBsum; 1KFU; -.
DR PDBsum; 1KFX; -.
DR PDBsum; 4PHJ; -.
DR PDBsum; 4PHK; -.
DR PDBsum; 4PHM; -.
DR PDBsum; 4WQ2; -.
DR PDBsum; 4WQ3; -.
DR PDBsum; 5D69; -.
DR PDBsum; 6QLB; -.
DR AlphaFoldDB; P04632; -.
DR SMR; P04632; -.
DR BioGRID; 107276; 91.
DR ComplexPortal; CPX-2674; M-Calpain complex.
DR ComplexPortal; CPX-4302; mu-Calpain complex.
DR CORUM; P04632; -.
DR IntAct; P04632; 45.
DR MINT; P04632; -.
DR STRING; 9606.ENSP00000246533; -.
DR BindingDB; P04632; -.
DR ChEMBL; CHEMBL2111357; -.
DR DrugBank; DB02570; PD150606.
DR GlyGen; P04632; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P04632; -.
DR MetOSite; P04632; -.
DR PhosphoSitePlus; P04632; -.
DR SwissPalm; P04632; -.
DR BioMuta; CAPNS1; -.
DR DMDM; 115612; -.
DR OGP; P04632; -.
DR REPRODUCTION-2DPAGE; IPI00025084; -.
DR SWISS-2DPAGE; P04632; -.
DR CPTAC; CPTAC-470; -.
DR CPTAC; CPTAC-471; -.
DR EPD; P04632; -.
DR jPOST; P04632; -.
DR MassIVE; P04632; -.
DR MaxQB; P04632; -.
DR PaxDb; P04632; -.
DR PeptideAtlas; P04632; -.
DR PRIDE; P04632; -.
DR ProteomicsDB; 51727; -.
DR TopDownProteomics; P04632; -.
DR Antibodypedia; 1704; 260 antibodies from 33 providers.
DR DNASU; 826; -.
DR Ensembl; ENST00000246533.8; ENSP00000246533.2; ENSG00000126247.11.
DR Ensembl; ENST00000588815.5; ENSP00000464849.1; ENSG00000126247.11.
DR GeneID; 826; -.
DR KEGG; hsa:826; -.
DR MANE-Select; ENST00000246533.8; ENSP00000246533.2; NM_001749.4; NP_001740.1.
DR UCSC; uc002odi.2; human.
DR CTD; 826; -.
DR DisGeNET; 826; -.
DR GeneCards; CAPNS1; -.
DR HGNC; HGNC:1481; CAPNS1.
DR HPA; ENSG00000126247; Low tissue specificity.
DR MIM; 114170; gene.
DR neXtProt; NX_P04632; -.
DR OpenTargets; ENSG00000126247; -.
DR PharmGKB; PA26067; -.
DR VEuPathDB; HostDB:ENSG00000126247; -.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000155478; -.
DR InParanoid; P04632; -.
DR OMA; MCRAFQT; -.
DR OrthoDB; 1330600at2759; -.
DR PhylomeDB; P04632; -.
DR TreeFam; TF314682; -.
DR BRENDA; 3.4.22.53; 2681.
DR BRENDA; 3.4.22.B24; 2681.
DR PathwayCommons; P04632; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
DR SignaLink; P04632; -.
DR BioGRID-ORCS; 826; 16 hits in 1074 CRISPR screens.
DR ChiTaRS; CAPNS1; human.
DR EvolutionaryTrace; P04632; -.
DR GeneWiki; CAPNS1; -.
DR GenomeRNAi; 826; -.
DR Pharos; P04632; Tbio.
DR PRO; PR:P04632; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P04632; protein.
DR Bgee; ENSG00000126247; Expressed in metanephros cortex and 204 other tissues.
DR ExpressionAtlas; P04632; baseline and differential.
DR Genevisible; P04632; HS.
DR GO; GO:0110158; C:calpain complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IC:ComplexPortal.
DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR InterPro; IPR029642; CAPN4.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR46735:SF1; PTHR46735:SF1; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..268
FT /note="Calpain small subunit 1"
FT /id="PRO_0000073713"
FT DOMAIN 91..125
FT /note="EF-hand 1; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 139..172
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 169..204
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 205..233
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT DOMAIN 234..268
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q64537,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q64537,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 224
FT /note="M -> V (in dbSNP:rs17878750)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021089"
FT CONFLICT 5
FT /note="N -> D (in Ref. 7; AAH64998)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="N -> G (in Ref. 7; AAH64998)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="S -> G (in Ref. 7; AAH64998)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..268
FT /note="WLQLTMYS -> VRTPILGYGCLGGPHPSALHTSSELQSPSSYFASRPWVRA
FT KGLVLLGFPVLTLHPPLPSGCS (in Ref. 7; AAH11903)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="Y -> F (in Ref. 7; AAH21933)"
FT /evidence="ECO:0000305"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:4PHJ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4PHJ"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:4PHJ"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:4PHJ"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:4PHJ"
FT HELIX 161..181
FT /evidence="ECO:0007829|PDB:4PHJ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4PHJ"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4PHJ"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:4PHJ"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:4PHJ"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:4PHJ"
FT HELIX 226..246
FT /evidence="ECO:0007829|PDB:4PHJ"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:4PHK"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:4PHJ"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:4PHJ"
SQ SEQUENCE 268 AA; 28316 MW; 17B87A8E47A90632 CRC64;
MFLVNSFLKG GGGGGGGGGG LGGGLGNVLG GLISGAGGGG GGGGGGGGGG GGGGGGTAMR
ILGGVISAIS EAAAQYNPEP PPPRTHYSNI EANESEEVRQ FRRLFAQLAG DDMEVSATEL
MNILNKVVTR HPDLKTDGFG IDTCRSMVAV MDSDTTGKLG FEEFKYLWNN IKRWQAIYKQ
FDTDRSGTIC SSELPGAFEA AGFHLNEHLY NMIIRRYSDE SGNMDFDNFI SCLVRLDAMF
RAFKSLDKDG TGQIQVNIQE WLQLTMYS
