CAN11_RAT
ID CAN11_RAT Reviewed; 716 AA.
AC Q4V8Q1; Q6IE72;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Calpain 11 {ECO:0000312|EMBL:AAH97256.1};
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase 11 {ECO:0000250|UniProtKB:Q9UMQ6};
DE Short=CANP 11 {ECO:0000250|UniProtKB:Q9UMQ6};
GN Name=Capn11 {ECO:0000312|RGD:1302946};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH97256.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis {ECO:0000312|EMBL:AAH97256.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:CAE48376.1}
RP IDENTIFICATION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAE48376.1};
RX PubMed=15060002; DOI=10.1101/gr.1946304;
RA Puente X.S., Lopez-Otin C.;
RT "A genomic analysis of rat proteases and protease inhibitors.";
RL Genome Res. 14:609-622(2004).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyzes limited proteolysis of substrates involved in cytoskeletal
CC remodeling and signal transduction. {ECO:0000250|UniProtKB:Q9UMQ6}.
CC -!- SUBUNIT: Heterodimer of a large (catalytic) and a small (regulatory)
CC subunit. {ECO:0000250|UniProtKB:Q9UMQ6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250|UniProtKB:Q6J756}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=Q4V8Q1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15057822};
CC IsoId=Q4V8Q1-2; Sequence=VSP_052993;
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000255}.
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DR EMBL; AC097557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC097256; AAH97256.1; -; mRNA.
DR EMBL; BN000321; CAE48376.1; -; mRNA.
DR RefSeq; NP_001002806.2; NM_001002806.2.
DR AlphaFoldDB; Q4V8Q1; -.
DR SMR; Q4V8Q1; -.
DR STRING; 10116.ENSRNOP00000059934; -.
DR MEROPS; C02.013; -.
DR PaxDb; Q4V8Q1; -.
DR GeneID; 408218; -.
DR KEGG; rno:408218; -.
DR UCSC; RGD:1302946; rat. [Q4V8Q1-1]
DR CTD; 11131; -.
DR RGD; 1302946; Capn11.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; Q4V8Q1; -.
DR OrthoDB; 704215at2759; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR PRO; PR:Q4V8Q1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
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: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 Alternative splicing; Calcium; Cytoplasmic vesicle; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..716
FT /note="Calpain 11"
FT /id="PRO_0000356220"
FT DOMAIN 55..354
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 587..613
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 617..652
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 355..528
FT /note="Domain III"
FT /evidence="ECO:0000250|UniProtKB:Q9UMQ6"
FT REGION 529..544
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q9UMQ6"
FT REGION 545..715
FT /note="Domain IV"
FT /evidence="ECO:0000250|UniProtKB:Q9UMQ6"
FT ACT_SITE 115
FT /evidence="ECO:0000255"
FT ACT_SITE 272
FT /evidence="ECO:0000255"
FT ACT_SITE 296
FT /evidence="ECO:0000255"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 602
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 604
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 606
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 611
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 630
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 632
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 634
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 636
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15057822"
FT /id="VSP_052993"
FT CONFLICT 254
FT /note="V -> A (in Ref. 2; AAH97256)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..453
FT /note="WYVQ -> PKE (in Ref. 2; AAH97256)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="V -> F (in Ref. 2; AAH97256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 83241 MW; 634800A30B3CA3D4 CRC64;
MLNFSDISYA ERGMVATINS NRLKDKGVGQ YQNAYNYKNQ NFEDLRASCL KMGELFEDPF
FPAEPQSIGF KELGPKSQEV HNVYWQRPKD IIHNPQFITN DFSPTDICQG ILGDCWLLAA
IGSLTTSPKL LFRVVPRSQS FKKNYAGIFH FQLWQFGHWL NVVVDDRLPT KNNKLVFVHA
SHRQEFWGAL LEKAYAKLNG SYEALTGGST MEGLEDFTGG MAQCIRLQNP PHNLLRLLRK
ALEKSSLMGC SIEVTNSDDV EKMAHNMLVK GHAYAITGLQ DVYYRDKLET LIRIQNPWGR
IEWNGAWSDK AKEWEEVMPE VQMQLLHKKE DGEFWMSYED FMSNFTLLEI CNLTPDALSS
WDYKSCWHTT FFEGSWRRGS TAGGCRNYPE TFWSNPQFRI SLPETDDPED SSDKSEMVCT
CLVALMQKNW RHAREGPQLL TIGFVVFSVW YVQFQNLQDI HLKKDFFMKY RDHGFSEIFT
NTREVNSHLR LPPGEYVIIP STFEPHKDAD FLLRVFTEKH SETWLLDEVN MLEQLQEETI
TDADLDQNSV ELFETLANRD SQVDMYDLQK LLNKMSSKVK SFKSKGFSLD VCRRMVNLMD
KDDSGKLGLH EFHILWKKIK KWMEIFKECD QDRSGNLNSY EMRLAIEKAG IRMNNRVTEV
VVARYADANM IVDFDNFINC FLRLKAMFAF FLSMDTKKTG SICLNINQWL HITMWG
