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CAN13_HUMAN
ID   CAN13_HUMAN             Reviewed;         669 AA.
AC   Q6MZZ7; Q17RF0; Q580X1; Q8TE80;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Calpain-13;
DE            EC=3.4.22.-;
DE   AltName: Full=Calcium-activated neutral proteinase 13;
DE            Short=CANP 13;
GN   Name=CAPN13;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-280.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Esophageal carcinoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-280.
RC   TISSUE=Colon;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=11675017; DOI=10.1016/s0378-1119(01)00599-6;
RA   Dear T.N., Boehm T.;
RT   "Identification and characterization of two novel calpain large subunit
RT   genes.";
RL   Gene 274:245-252(2001).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 515-669.
RG   Structural genomics consortium (SGC);
RT   "Structure of human calpain 13.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Probable non-lysosomal thiol-protease. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6MZZ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6MZZ7-2; Sequence=VSP_021476, VSP_021477;
CC   -!- TISSUE SPECIFICITY: Weakly expressed in lung and testis. Weakly or not
CC       expressed in other tissues. {ECO:0000269|PubMed:11675017}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC   -!- CAUTION: It is unlikely that this protein binds calcium as none of the
CC       2 EF-hand domains seem to contain a canonical calcium-binding site.
CC       {ECO:0000305}.
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DR   EMBL; AK074418; BAB85075.1; -; mRNA.
DR   EMBL; BX640793; CAE45878.1; -; mRNA.
DR   EMBL; AC092569; AAX82015.1; -; Genomic_DNA.
DR   EMBL; BC117347; AAI17348.1; -; mRNA.
DR   EMBL; BC117345; AAI17346.1; -; mRNA.
DR   CCDS; CCDS46252.1; -. [Q6MZZ7-1]
DR   RefSeq; NP_653176.2; NM_144575.2. [Q6MZZ7-1]
DR   RefSeq; XP_011531461.1; XM_011533159.2. [Q6MZZ7-1]
DR   RefSeq; XP_011531462.1; XM_011533160.2. [Q6MZZ7-1]
DR   RefSeq; XP_011531463.1; XM_011533161.2. [Q6MZZ7-1]
DR   RefSeq; XP_016860753.1; XM_017005264.1. [Q6MZZ7-1]
DR   RefSeq; XP_016860754.1; XM_017005265.1.
DR   PDB; 2I7A; X-ray; 1.80 A; A=515-669.
DR   PDBsum; 2I7A; -.
DR   AlphaFoldDB; Q6MZZ7; -.
DR   SMR; Q6MZZ7; -.
DR   BioGRID; 124928; 19.
DR   IntAct; Q6MZZ7; 12.
DR   STRING; 9606.ENSP00000295055; -.
DR   MEROPS; C02.020; -.
DR   iPTMnet; Q6MZZ7; -.
DR   PhosphoSitePlus; Q6MZZ7; -.
DR   BioMuta; CAPN13; -.
DR   DMDM; 117949375; -.
DR   jPOST; Q6MZZ7; -.
DR   MassIVE; Q6MZZ7; -.
DR   MaxQB; Q6MZZ7; -.
DR   PaxDb; Q6MZZ7; -.
DR   PeptideAtlas; Q6MZZ7; -.
DR   PRIDE; Q6MZZ7; -.
DR   ProteomicsDB; 66593; -. [Q6MZZ7-1]
DR   ProteomicsDB; 66594; -. [Q6MZZ7-2]
DR   Antibodypedia; 28998; 83 antibodies from 22 providers.
DR   DNASU; 92291; -.
DR   Ensembl; ENST00000295055.12; ENSP00000295055.8; ENSG00000162949.16. [Q6MZZ7-1]
DR   Ensembl; ENST00000458085.6; ENSP00000416191.2; ENSG00000162949.16. [Q6MZZ7-2]
DR   GeneID; 92291; -.
DR   KEGG; hsa:92291; -.
DR   MANE-Select; ENST00000295055.12; ENSP00000295055.8; NM_144575.3; NP_653176.2.
DR   UCSC; uc061hvv.1; human. [Q6MZZ7-1]
DR   CTD; 92291; -.
DR   DisGeNET; 92291; -.
DR   GeneCards; CAPN13; -.
DR   HGNC; HGNC:16663; CAPN13.
DR   HPA; ENSG00000162949; Tissue enhanced (intestine, stomach).
DR   MIM; 610228; gene.
DR   neXtProt; NX_Q6MZZ7; -.
DR   OpenTargets; ENSG00000162949; -.
DR   PharmGKB; PA134931170; -.
DR   VEuPathDB; HostDB:ENSG00000162949; -.
DR   eggNOG; KOG0037; Eukaryota.
DR   eggNOG; KOG0045; Eukaryota.
DR   GeneTree; ENSGT00940000160921; -.
DR   HOGENOM; CLU_010982_0_3_1; -.
DR   InParanoid; Q6MZZ7; -.
DR   OMA; SQHAYTV; -.
DR   OrthoDB; 704215at2759; -.
DR   PhylomeDB; Q6MZZ7; -.
DR   TreeFam; TF314748; -.
DR   PathwayCommons; Q6MZZ7; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   SignaLink; Q6MZZ7; -.
DR   BioGRID-ORCS; 92291; 9 hits in 1067 CRISPR screens.
DR   ChiTaRS; CAPN13; human.
DR   EvolutionaryTrace; Q6MZZ7; -.
DR   GenomeRNAi; 92291; -.
DR   Pharos; Q6MZZ7; Tdark.
DR   PRO; PR:Q6MZZ7; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q6MZZ7; protein.
DR   Bgee; ENSG00000162949; Expressed in palpebral conjunctiva and 125 other tissues.
DR   ExpressionAtlas; Q6MZZ7; baseline and differential.
DR   Genevisible; Q6MZZ7; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00044; CysPc; 1.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR036213; Calpain_III_sf.
DR   InterPro; IPR029544; CANP13.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR10183:SF333; PTHR10183:SF333; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF49758; SSF49758; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Hydrolase; Protease;
KW   Reference proteome; Repeat; Thiol protease.
FT   CHAIN           1..669
FT                   /note="Calpain-13"
FT                   /id="PRO_0000259582"
FT   DOMAIN          34..333
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   DOMAIN          538..573
FT                   /note="EF-hand 1"
FT   DOMAIN          636..669
FT                   /note="EF-hand 2"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   VAR_SEQ         417..423
FT                   /note="RFREKFP -> KHCPKLK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021476"
FT   VAR_SEQ         424..669
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021477"
FT   VARIANT         249
FT                   /note="H -> Y (in dbSNP:rs17010210)"
FT                   /id="VAR_028964"
FT   VARIANT         280
FT                   /note="A -> T (in dbSNP:rs508405)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_028965"
FT   VARIANT         596
FT                   /note="I -> T (in dbSNP:rs2276568)"
FT                   /id="VAR_028966"
FT   CONFLICT        562
FT                   /note="E -> G (in Ref. 2; CAE45878)"
FT                   /evidence="ECO:0000305"
FT   HELIX           518..529
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   HELIX           540..550
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   STRAND          555..558
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   HELIX           560..580
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   STRAND          586..588
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   HELIX           589..591
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   HELIX           592..597
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   HELIX           600..602
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   HELIX           609..619
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   STRAND          624..626
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   HELIX           628..648
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   STRAND          650..653
FT                   /evidence="ECO:0007829|PDB:2I7A"
FT   HELIX           659..667
FT                   /evidence="ECO:0007829|PDB:2I7A"
SQ   SEQUENCE   669 AA;  76696 MW;  BB24CF09D55CF790 CRC64;
     MAYYQEPSVE TSIIKFKDQD FTTLRDHCLS MGRTFKDETF PAADSSIGQK LLQEKRLSNV
     IWKRPQDLPG GPPHFILDDI SRFDIQQGGA ADCWFLAALG SLTQNPQYRQ KILMVQSFSH
     QYAGIFRFRF WQCGQWVEVV IDDRLPVQGD KCLFVRPRHQ NQEFWPCLLE KAYAKLLGSY
     SDLHYGFLED ALVDLTGGVI TNIHLHSSPV DLVKAVKTAT KAGSLITCAT PSGPTDTAQA
     MENGLVSLHA YTVTGAEQIQ YRRGWEEIIS LWNPWGWGEA EWRGRWSDGS QEWEETCDPR
     KSQLHKKRED GEFWMSCQDF QQKFIAMFIC SEIPITLDHG NTLHEGWSQI MFRKQVILGN
     TAGGPRNDAQ FNFSVQEPME GTNVVVCVTV AVTPSNLKAE DAKFPLDFQV ILAGSQRFRE
     KFPPVFFSSF RNTVQSSNNK FRRNFTMTYH LSPGNYVVVA QTRRKSAEFL LRIFLKMPDS
     DRHLSSHFNL RMKGSPSEHG SQQSIFNRYA QQRLDIDATQ LQGLLNQELL TGPPGDMFSL
     DECRSLVALM ELKVNGRLDQ EEFARLWKRL VHYQHVFQKV QTSPGVLLSS DLWKAIENTD
     FLRGIFISRE LLHLVTLRYS DSVGRVSFPS LVCFLMRLEA MAKTFRNLSK DGKGLYLTEM
     EWMSLVMYN
 
 
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