ID   CAN10_HUMAN             Reviewed;         672 AA.
AC   Q9HC96; A8MVS7; Q4ZFV1; Q8NCD4; Q96IG4; Q96JI2; Q9HC89; Q9HC90; Q9HC91;
AC   Q9HC92; Q9HC93; Q9HC94; Q9HC95;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   24-JAN-2024, entry version 188.
DE   RecName: Full=Calpain-10;
DE            EC=3.4.22.-;
DE   AltName: Full=Calcium-activated neutral proteinase 10;
DE            Short=CANP 10;
GN   Name=CAPN10; Synonyms=KIAA1845;
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], ALTERNATIVE SPLICING, VARIANTS THR-200;
RP   HIS-202; VAL-341; ALA-504; SER-529; ASN-613 AND VAL-666, AND INVOLVEMENT IN
RP   SUSCEPTIBILITY TO T2D1.
RX   PubMed=11017071; DOI=10.1038/79876;
RA   Horikawa Y., Oda N., Cox N.J., Li X., Orho-Melander M., Hara M.,
RA   Hinokio Y., Lindner T.H., Mashima H., Schwarz P.E.H., del Bosque-Plata L.,
RA   Horikawa Y., Oda Y., Yoshiuchi I., Colilla S., Polonsky K.S., Wei S.,
RA   Concannon P., Iwasaki N., Schulze J., Baier L.J., Bogardus C., Groop L.,
RA   Boerwinkle E., Hanis C.L., Bell G.I.;
RT   "Genetic variation in the gene encoding calpain-10 is associated with type
RT   2 diabetes mellitus.";
RL   Nat. Genet. 26:163-175(2000).
RN   [2]
RP   ERRATUM OF PUBMED:11017071.
RA   Horikawa Y., Oda N., Cox N.J., Li X., Orho-Melander M., Hara M.,
RA   Hinokio Y., Lindner T.H., Mashima H., Schwarz P.E.H., del Bosque-Plata L.,
RA   Horikawa Y., Oda Y., Yoshiuchi I., Colilla S., Polonsky K.S., Wei S.,
RA   Concannon P., Iwasaki N., Schulze J., Baier L.J., Bogardus C., Groop L.,
RA   Boerwinkle E., Hanis C.L., Bell G.I.;
RL   Nat. Genet. 26:502-502(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT VAL-666.
RC   TISSUE=Brain;
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANTS ALA-504
RP   AND VAL-666.
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=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT VAL-666.
RC   TISSUE=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   [7]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
RN   [8]
RP   INVOLVEMENT IN SUSCEPTIBILITY TO T2D1.
RX   PubMed=16721485; DOI=10.1007/s10038-006-0410-9;
RA   Kang E.S., Kim H.J., Nam M., Nam C.M., Ahn C.W., Cha B.S., Lee H.C.;
RT   "A novel 111/121 diplotype in the Calpain-10 gene is associated with type 2
RT   diabetes.";
RL   J. Hum. Genet. 51:629-633(2006).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17572128; DOI=10.1016/j.ymgme.2007.05.001;
RA   Brown A.E., Yeaman S.J., Walker M.;
RT   "Targeted suppression of calpain-10 expression impairs insulin-stimulated
RT   glucose uptake in cultured primary human skeletal muscle cells.";
RL   Mol. Genet. Metab. 91:318-324(2007).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] GLY-276.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC       catalyzes limited proteolysis of substrates involved in cytoskeletal
CC       remodeling and signal transduction. May play a role in insulin-
CC       stimulated glucose uptake. {ECO:0000269|PubMed:17572128}.
CC   -!- INTERACTION:
CC       Q9HC96; Q96G97-4: BSCL2; NbExp=3; IntAct=EBI-3915761, EBI-10178113;
CC       Q9HC96; Q16595: FXN; NbExp=3; IntAct=EBI-3915761, EBI-949340;
CC       Q9HC96; P04792: HSPB1; NbExp=3; IntAct=EBI-3915761, EBI-352682;
CC       Q9HC96; P42858: HTT; NbExp=12; IntAct=EBI-3915761, EBI-466029;
CC       Q9HC96; Q99732: LITAF; NbExp=3; IntAct=EBI-3915761, EBI-725647;
CC       Q9HC96; P02545-2: LMNA; NbExp=3; IntAct=EBI-3915761, EBI-351953;
CC       Q9HC96; P10636: MAPT; NbExp=3; IntAct=EBI-3915761, EBI-366182;
CC       Q9HC96; Q9P1N4; NbExp=3; IntAct=EBI-3915761, EBI-25878161;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=A; Synonyms=CAPN10a;
CC         IsoId=Q9HC96-1; Sequence=Displayed;
CC       Name=B; Synonyms=CAPN10b;
CC         IsoId=Q9HC96-2; Sequence=VSP_005232, VSP_005233;
CC       Name=C; Synonyms=CAPN10c;
CC         IsoId=Q9HC96-3; Sequence=VSP_005234;
CC       Name=D; Synonyms=CAPN10d;
CC         IsoId=Q9HC96-4; Sequence=VSP_005235, VSP_005236;
CC       Name=E; Synonyms=CAPN10e;
CC         IsoId=Q9HC96-5; Sequence=VSP_005237, VSP_005238;
CC       Name=F; Synonyms=CAPN10f;
CC         IsoId=Q9HC96-6; Sequence=VSP_005239, VSP_005240;
CC       Name=G; Synonyms=CAPN10g;
CC         IsoId=Q9HC96-7; Sequence=VSP_005241, VSP_005242;
CC       Name=H; Synonyms=CAPN10h;
CC         IsoId=Q9HC96-8; Sequence=VSP_005243;
CC   -!- TISSUE SPECIFICITY: Detected in primary skeletal muscle cells (at
CC       protein level). Ubiquitous. {ECO:0000269|PubMed:17572128}.
CC   -!- DISEASE: Type 2 diabetes mellitus 1 (T2D1) [MIM:601283]: A
CC       multifactorial disorder of glucose homeostasis caused by a lack of
CC       sensitivity to the body's own insulin. Affected individuals usually
CC       have an obese body habitus and manifestations of a metabolic syndrome
CC       characterized by diabetes, insulin resistance, hypertension and
CC       hypertriglyceridemia. The disease results in long-term complications
CC       that affect the eyes, kidneys, nerves, and blood vessels.
CC       {ECO:0000269|PubMed:11017071, ECO:0000269|PubMed:16721485}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform B]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform D]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform E]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform F]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47474.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF089088; AAG17966.1; -; mRNA.
DR   EMBL; AF089090; AAG17968.1; -; mRNA.
DR   EMBL; AF089091; AAG17969.1; -; mRNA.
DR   EMBL; AF089092; AAG17970.1; -; mRNA.
DR   EMBL; AF089093; AAG17971.1; -; mRNA.
DR   EMBL; AF089094; AAG17972.1; -; mRNA.
DR   EMBL; AF089095; AAG17973.1; -; mRNA.
DR   EMBL; AF089096; AAG17974.1; -; mRNA.
DR   EMBL; AB058748; BAB47474.1; ALT_INIT; mRNA.
DR   EMBL; AK074807; BAC11220.1; -; mRNA.
DR   EMBL; AC124862; AAX88944.1; -; Genomic_DNA.
DR   EMBL; BC004260; AAH04260.1; -; mRNA.
DR   EMBL; BC007553; AAH07553.2; -; mRNA.
DR   CCDS; CCDS33420.1; -. [Q9HC96-3]
DR   CCDS; CCDS42838.1; -. [Q9HC96-1]
DR   RefSeq; NP_075571.1; NM_023083.3. [Q9HC96-1]
DR   RefSeq; NP_075573.2; NM_023085.3. [Q9HC96-3]
DR   AlphaFoldDB; Q9HC96; -.
DR   SMR; Q9HC96; -.
DR   BioGRID; 116305; 34.
DR   IntAct; Q9HC96; 13.
DR   STRING; 9606.ENSP00000375844; -.
DR   MEROPS; C02.018; -.
DR   iPTMnet; Q9HC96; -.
DR   PhosphoSitePlus; Q9HC96; -.
DR   BioMuta; CAPN10; -.
DR   DMDM; 317373329; -.
DR   MassIVE; Q9HC96; -.
DR   PaxDb; 9606-ENSP00000375844; -.
DR   PeptideAtlas; Q9HC96; -.
DR   ProteomicsDB; 81650; -. [Q9HC96-1]
DR   ProteomicsDB; 81651; -. [Q9HC96-2]
DR   ProteomicsDB; 81652; -. [Q9HC96-3]
DR   ProteomicsDB; 81653; -. [Q9HC96-4]
DR   ProteomicsDB; 81654; -. [Q9HC96-5]
DR   Antibodypedia; 1333; 190 antibodies from 24 providers.
DR   DNASU; 11132; -.
DR   Ensembl; ENST00000270361.15; ENSP00000270361.11; ENSG00000142330.20. [Q9HC96-6]
DR   Ensembl; ENST00000270364.11; ENSP00000270364.7; ENSG00000142330.20. [Q9HC96-7]
DR   Ensembl; ENST00000352879.8; ENSP00000289381.6; ENSG00000142330.20. [Q9HC96-8]
DR   Ensembl; ENST00000354082.8; ENSP00000270362.6; ENSG00000142330.20. [Q9HC96-3]
DR   Ensembl; ENST00000357048.8; ENSP00000349556.4; ENSG00000142330.20. [Q9HC96-4]
DR   Ensembl; ENST00000391983.7; ENSP00000375843.3; ENSG00000142330.20. [Q9HC96-2]
DR   Ensembl; ENST00000391984.7; ENSP00000375844.2; ENSG00000142330.20. [Q9HC96-1]
DR   Ensembl; ENST00000416591.5; ENSP00000400144.1; ENSG00000142330.20. [Q9HC96-5]
DR   GeneID; 11132; -.
DR   KEGG; hsa:11132; -.
DR   MANE-Select; ENST00000391984.7; ENSP00000375844.2; NM_023083.4; NP_075571.2.
DR   UCSC; uc002vzk.2; human. [Q9HC96-1]
DR   AGR; HGNC:1477; -.
DR   CTD; 11132; -.
DR   DisGeNET; 11132; -.
DR   GeneCards; CAPN10; -.
DR   HGNC; HGNC:1477; CAPN10.
DR   HPA; ENSG00000142330; Low tissue specificity.
DR   MalaCards; CAPN10; -.
DR   MIM; 601283; phenotype.
DR   MIM; 605286; gene.
DR   neXtProt; NX_Q9HC96; -.
DR   OpenTargets; ENSG00000142330; -.
DR   PharmGKB; PA26058; -.
DR   VEuPathDB; HostDB:ENSG00000142330; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   GeneTree; ENSGT00940000159706; -.
DR   HOGENOM; CLU_010982_3_3_1; -.
DR   InParanoid; Q9HC96; -.
DR   OMA; ECALSCS; -.
DR   OrthoDB; 142935at2759; -.
DR   PhylomeDB; Q9HC96; -.
DR   TreeFam; TF314748; -.
DR   BRENDA; 3.4.22.B30; 2681.
DR   PathwayCommons; Q9HC96; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   SignaLink; Q9HC96; -.
DR   SIGNOR; Q9HC96; -.
DR   BioGRID-ORCS; 11132; 19 hits in 1154 CRISPR screens.
DR   ChiTaRS; CAPN10; human.
DR   GeneWiki; CAPN10; -.
DR   GenomeRNAi; 11132; -.
DR   Pharos; Q9HC96; Tbio.
DR   PRO; PR:Q9HC96; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9HC96; Protein.
DR   Bgee; ENSG00000142330; Expressed in apex of heart and 128 other cell types or tissues.
DR   ExpressionAtlas; Q9HC96; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR   GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IMP:BHF-UCL.
DR   GO; GO:0008092; F:cytoskeletal protein binding; ISS:BHF-UCL.
DR   GO; GO:0000149; F:SNARE binding; ISS:BHF-UCL.
DR   GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; IC:BHF-UCL.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR   GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL.
DR   GO; GO:0032388; P:positive regulation of intracellular transport; ISS:BHF-UCL.
DR   GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IMP:BHF-UCL.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:BHF-UCL.
DR   GO; GO:0097050; P:type B pancreatic cell apoptotic process; IDA:BHF-UCL.
DR   CDD; cd00214; Calpain_III; 2.
DR   CDD; cd00044; CysPc; 1.
DR   Gene3D; 2.60.120.380; -; 2.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR033883; C2_III.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR022683; Calpain_III.
DR   InterPro; IPR036213; Calpain_III_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR10183; CALPAIN; 1.
DR   PANTHER; PTHR10183:SF30; CALPAIN-10; 1.
DR   Pfam; PF01067; Calpain_III; 2.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00720; calpain_III; 2.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   Genevisible; Q9HC96; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Diabetes mellitus; Hydrolase; Protease;
KW   Reference proteome; Repeat; Thiol protease.
FT   CHAIN           1..672
FT                   /note="Calpain-10"
FT                   /id="PRO_0000207725"
FT   DOMAIN          13..321
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   REGION          322..494
FT                   /note="Domain III 1"
FT   REGION          513..654
FT                   /note="Domain III 2"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         48..581
FT                   /note="Missing (in isoform H)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005243"
FT   VAR_SEQ         93..139
FT                   /note="IPPGQPSWADQEYRGSFTCRIWQFGRWVEVTTDDRLPCLAGRLCFSR -> S
FT                   CPVQLPADWTCKVQPVWLEFPCLPISCRLRVSSDTSPDSATWGSWK (in isoform
FT                   G)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005241"
FT   VAR_SEQ         140..672
FT                   /note="Missing (in isoform G)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005242"
FT   VAR_SEQ         154..274
FT                   /note="VYAKVHGSYEHLWAGQVADALVDLTGGLAERWNLKGVAGSGGQQDRPGRWEH
FT                   RTCRQLLHLKDQCLISCCVLSPRAGARELGEFHAFIVSDLRELQGQAGQCILLLRIQNP
FT                   WGRRCWQGLW -> GPWVLRAPVGRAGGGCPGGPDRRPGRKMEPEGRSRKRRPAGQARP
FT                   LGAQDLSAAAPPEGPVSDQLLRAQPQSRCPGAGGVPCLHCLGPAGAPGSGGPVHPAAAD
FT                   PEPLGPAVLAGALERGG (in isoform F)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005239"
FT   VAR_SEQ         275..672
FT                   /note="Missing (in isoform F)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005240"
FT   VAR_SEQ         427..444
FT                   /note="VEKRRVNLPRVLSMPPVA -> GVTLGTTLFPVPSWMWPT (in isoform
FT                   E)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005237"
FT   VAR_SEQ         428..582
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005234"
FT   VAR_SEQ         445..672
FT                   /note="Missing (in isoform E)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005238"
FT   VAR_SEQ         494..544
FT                   /note="SAIRAVAKNTTPGAALPAGEWGTVQLRGSWRVGQTAGGSRNFASYPTNPCF
FT                   -> RALAPAASASLCISTAGPVTPSSTPSASISSRSQRVEGARTHPHCCCRSRC (in
FT                   isoform B)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005232"
FT   VAR_SEQ         494..513
FT                   /note="SAIRAVAKNTTPGAALPAGE -> RSQRVEGARTHPHCCCRSRC (in
FT                   isoform D)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005235"
FT   VAR_SEQ         514..672
FT                   /note="Missing (in isoform D)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005236"
FT   VAR_SEQ         545..672
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005233"
FT   VARIANT         200
FT                   /note="P -> T (in dbSNP:rs3792268)"
FT                   /evidence="ECO:0000269|PubMed:11017071"
FT                   /id="VAR_014437"
FT   VARIANT         202
FT                   /note="R -> H (in dbSNP:rs768407925)"
FT                   /evidence="ECO:0000269|PubMed:11017071"
FT                   /id="VAR_014438"
FT   VARIANT         276
FT                   /note="E -> G (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036049"
FT   VARIANT         341
FT                   /note="A -> V (in dbSNP:rs776848131)"
FT                   /evidence="ECO:0000269|PubMed:11017071"
FT                   /id="VAR_014439"
FT   VARIANT         504
FT                   /note="T -> A (in dbSNP:rs7607759)"
FT                   /evidence="ECO:0000269|PubMed:11017071,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_014440"
FT   VARIANT         529
FT                   /note="A -> S"
FT                   /evidence="ECO:0000269|PubMed:11017071"
FT                   /id="VAR_014441"
FT   VARIANT         613
FT                   /note="S -> N (in dbSNP:rs146148004)"
FT                   /evidence="ECO:0000269|PubMed:11017071"
FT                   /id="VAR_014442"
FT   VARIANT         666
FT                   /note="I -> V (in dbSNP:rs2975766)"
FT                   /evidence="ECO:0000269|PubMed:11017071,
FT                   ECO:0000269|PubMed:11347906, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_014443"
FT   CONFLICT        195
FT                   /note="G -> S (in Ref. 4; BAC11220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="E -> K (in Ref. 1; AAG17969/AAG17971)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   672 AA;  74952 MW;  74A48D879E896C71 CRC64;
     MRAGRGATPA RELFRDAAFP AADSSLFCDL STPLAQFRED ITWRRPQEIC ATPRLFPDDP
     REGQVKQGLL GDCWFLCACA ALQKSRHLLD QVIPPGQPSW ADQEYRGSFT CRIWQFGRWV
     EVTTDDRLPC LAGRLCFSRC QREDVFWLPL LEKVYAKVHG SYEHLWAGQV ADALVDLTGG
     LAERWNLKGV AGSGGQQDRP GRWEHRTCRQ LLHLKDQCLI SCCVLSPRAG ARELGEFHAF
     IVSDLRELQG QAGQCILLLR IQNPWGRRCW QGLWREGGEG WSQVDAAVAS ELLSQLQEGE
     FWVEEEEFLR EFDELTVGYP VTEAGHLQSL YTERLLCHTR ALPGAWVKGQ SAGGCRNNSG
     FPSNPKFWLR VSEPSEVYIA VLQRSRLHAA DWAGRARALV GDSHTSWSPA SIPGKHYQAV
     GLHLWKVEKR RVNLPRVLSM PPVAGTACHA YDREVHLRCE LSPGYYLAVP STFLKDAPGE
     FLLRVFSTGR VSLSAIRAVA KNTTPGAALP AGEWGTVQLR GSWRVGQTAG GSRNFASYPT
     NPCFPFSVPE GPGPRCVRIT LHQHCRPSDT EFHPIGFHIF QVPEGGRSQD APPLLLQEPL
     LSCVPHRYAQ EVSRLCLLPA GTYKVVPSTY LPDTEGAFTV TIATRIDRPS IHSQEMLGQF
     LQEVSIMAVM KT
//