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 27-MAR-2024, entry version 234. 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 107. DR ComplexPortal; CPX-2674; M-Calpain complex. DR ComplexPortal; CPX-4302; mu-Calpain complex. DR CORUM; P04632; -. DR IntAct; P04632; 46. DR MINT; P04632; -. DR STRING; 9606.ENSP00000464849; -. DR BindingDB; P04632; -. DR ChEMBL; CHEMBL2111357; -. DR DrugBank; DB02570; PD150606. DR GlyCosmos; P04632; 2 sites, 1 glycan. DR GlyGen; P04632; 4 sites, 2 O-linked glycans (4 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 CPTAC; CPTAC-470; -. DR CPTAC; CPTAC-471; -. DR EPD; P04632; -. DR jPOST; P04632; -. DR MassIVE; P04632; -. DR MaxQB; P04632; -. DR PaxDb; 9606-ENSP00000246533; -. DR PeptideAtlas; P04632; -. DR ProteomicsDB; 51727; -. DR Pumba; P04632; -. DR TopDownProteomics; P04632; -. DR Antibodypedia; 1704; 283 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 AGR; HGNC:1481; -. 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; RTHYSNV; -. DR OrthoDB; 4075143at2759; -. 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 1155 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 206 other cell types or tissues. DR ExpressionAtlas; P04632; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL. DR CDD; cd16188; EFh_PEF_CPNS1_2; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. 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; CALPAIN SMALL SUBUNIT 1; 1. DR PANTHER; PTHR46735; CALPAIN, SMALL SUBUNIT 1 A-RELATED; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 3. DR SWISS-2DPAGE; P04632; -. DR Genevisible; P04632; HS. 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 //