CAN11_HUMAN
ID CAN11_HUMAN Reviewed; 739 AA.
AC Q9UMQ6; B2RA64; Q5T3G1; Q8N4R5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Calpain-11;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase 11;
DE Short=CANP 11;
GN Name=CAPN11;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-441.
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 4-739, AND TISSUE SPECIFICITY.
RX PubMed=10409436; DOI=10.1006/geno.1999.5859;
RA Dear T.N., Moller A., Boehm T.;
RT "CAPN11: a calpain with high mRNA levels in testis and located on
RT chromosome 6.";
RL Genomics 59:243-247(1999).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyzes limited proteolysis of substrates involved in cytoskeletal
CC remodeling and signal transduction.
CC -!- SUBUNIT: Heterodimer of a large (catalytic) and a small (regulatory)
CC subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest expression in testis.
CC {ECO:0000269|PubMed:10409436}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33733.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG36761.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB52137.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK314054; BAG36761.1; ALT_INIT; mRNA.
DR EMBL; AL365192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04250.1; -; Genomic_DNA.
DR EMBL; BC033733; AAH33733.1; ALT_INIT; mRNA.
DR EMBL; AJ242832; CAB52137.1; ALT_INIT; mRNA.
DR CCDS; CCDS47436.1; -.
DR RefSeq; NP_008989.2; NM_007058.3.
DR AlphaFoldDB; Q9UMQ6; -.
DR SMR; Q9UMQ6; -.
DR BioGRID; 116304; 10.
DR IntAct; Q9UMQ6; 7.
DR MINT; Q9UMQ6; -.
DR STRING; 9606.ENSP00000381758; -.
DR MEROPS; C02.013; -.
DR iPTMnet; Q9UMQ6; -.
DR PhosphoSitePlus; Q9UMQ6; -.
DR BioMuta; CAPN11; -.
DR DMDM; 218511961; -.
DR MassIVE; Q9UMQ6; -.
DR PaxDb; Q9UMQ6; -.
DR PeptideAtlas; Q9UMQ6; -.
DR PRIDE; Q9UMQ6; -.
DR ProteomicsDB; 85193; -.
DR Antibodypedia; 4328; 176 antibodies from 26 providers.
DR DNASU; 11131; -.
DR Ensembl; ENST00000398776.2; ENSP00000381758.1; ENSG00000137225.13.
DR GeneID; 11131; -.
DR KEGG; hsa:11131; -.
DR MANE-Select; ENST00000398776.2; ENSP00000381758.1; NM_007058.4; NP_008989.2.
DR UCSC; uc003owt.1; human.
DR CTD; 11131; -.
DR DisGeNET; 11131; -.
DR GeneCards; CAPN11; -.
DR HGNC; HGNC:1478; CAPN11.
DR HPA; ENSG00000137225; Tissue enriched (testis).
DR MIM; 604822; gene.
DR neXtProt; NX_Q9UMQ6; -.
DR OpenTargets; ENSG00000137225; -.
DR PharmGKB; PA26059; -.
DR VEuPathDB; HostDB:ENSG00000137225; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000158672; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR InParanoid; Q9UMQ6; -.
DR OMA; KNWRLGQ; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q9UMQ6; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.B31; 2681.
DR PathwayCommons; Q9UMQ6; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR SignaLink; Q9UMQ6; -.
DR BioGRID-ORCS; 11131; 15 hits in 1069 CRISPR screens.
DR GenomeRNAi; 11131; -.
DR Pharos; Q9UMQ6; Tbio.
DR PRO; PR:Q9UMQ6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UMQ6; protein.
DR Bgee; ENSG00000137225; Expressed in left testis and 102 other tissues.
DR ExpressionAtlas; Q9UMQ6; baseline and differential.
DR Genevisible; Q9UMQ6; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
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:0008233; F:peptidase activity; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasmic vesicle; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..739
FT /note="Calpain-11"
FT /id="PRO_0000207729"
FT DOMAIN 79..378
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 610..636
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 640..675
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..551
FT /note="Domain III"
FT REGION 552..567
FT /note="Linker"
FT REGION 568..738
FT /note="Domain IV"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT ACT_SITE 296
FT /evidence="ECO:0000250"
FT ACT_SITE 320
FT /evidence="ECO:0000250"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 625
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 627
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 629
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 634
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 655
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 657
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 659
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 664
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VARIANT 266
FT /note="V -> M (in dbSNP:rs6938938)"
FT /id="VAR_033713"
FT VARIANT 441
FT /note="V -> A (in dbSNP:rs16871612)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033714"
FT VARIANT 521
FT /note="I -> V (in dbSNP:rs34710081)"
FT /id="VAR_033715"
FT VARIANT 544
FT /note="S -> R (in dbSNP:rs35527493)"
FT /id="VAR_033716"
FT VARIANT 728
FT /note="S -> N (in dbSNP:rs7761137)"
FT /id="VAR_024587"
SQ SEQUENCE 739 AA; 84423 MW; 8B102AF286259EFB CRC64;
MLYSPGPSLP ESAESLDGSQ EDKPRGSCAE PTFTDTGMVA HINNSRLKAK GVGQHDNAQN
FGNQSFEELR AACLRKGELF EDPLFPAEPS SLGFKDLGPN SKNVQNISWQ RPKDIINNPL
FIMDGISPTD ICQGILGDCW LLAAIGSLTT CPKLLYRVVP RGQSFKKNYA GIFHFQIWQF
GQWVNVVVDD RLPTKNDKLV FVHSTERSEF WSALLEKAYA KLSGSYEALS GGSTMEGLED
FTGGVAQSFQ LQRPPQNLLR LLRKAVERSS LMGCSIEVTS DSELESMTDK MLVRGHAYSV
TGLQDVHYRG KMETLIRVRN PWGRIEWNGA WSDSAREWEE VASDIQMQLL HKTEDGEFWM
SYQDFLNNFT LLEICNLTPD TLSGDYKSYW HTTFYEGSWR RGSSAGGCRN HPGTFWTNPQ
FKISLPEGDD PEDDAEGNVV VCTCLVALMQ KNWRHARQQG AQLQTIGFVL YAVPKEFQNI
QDVHLKKEFF TKYQDHGFSE IFTNSREVSS QLRLPPGEYI IIPSTFEPHR DADFLLRVFT
EKHSESWELD EVNYAEQLQE EKVSEDDMDQ DFLHLFKIVA GEGKEIGVYE LQRLLNRMAI
KFKSFKTKGF GLDACRCMIN LMDKDGSGKL GLLEFKILWK KLKKWMDIFR ECDQDHSGTL
NSYEMRLVIE KAGIKLNNKV MQVLVARYAD DDLIIDFDSF ISCFLRLKTM FTFFLTMDPK
NTGHICLSLE QWLQMTMWG
