CAN6_MOUSE
ID CAN6_MOUSE Reviewed; 641 AA.
AC O35646; Q3UM55;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Calpain-6;
GN Name=Capn6; Synonyms=Capa6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9503024; DOI=10.1006/geno.1997.5133;
RA Matena K., Boehm T., Dear N.T.;
RT "Genomic organization of mouse Capn5 and Capn6 genes confirms that they are
RT a distinct calpain subfamily.";
RL Genomics 48:117-120(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP DEVELOPMENTAL STAGE, FUNCTION, INTERACTION WITH MICROTUBULE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17210638; DOI=10.1128/mcb.00992-06;
RA Tonami K., Kurihara Y., Aburatani H., Uchijima Y., Asano T., Kurihara H.;
RT "Calpain 6 is involved in microtubule stabilization and cytoskeletal
RT organization.";
RL Mol. Cell. Biol. 27:2548-2561(2007).
RN [5]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20814968; DOI=10.1002/jbmr.241;
RA Hong J.M., Teitelbaum S.L., Kim T.H., Ross F.P., Kim S.Y., Kim H.J.;
RT "Calpain-6, a target molecule of glucocorticoids, regulates osteoclastic
RT bone resorption via cytoskeletal organization and microtubule
RT acetylation.";
RL J. Bone Miner. Res. 26:657-665(2011).
RN [6]
RP FUNCTION, AND INTERACTION WITH ARHGEF2.
RX PubMed=21406564; DOI=10.1242/jcs.072561;
RA Tonami K., Kurihara Y., Arima S., Nishiyama K., Uchijima Y., Asano T.,
RA Sorimachi H., Kurihara H.;
RT "Calpain-6, a microtubule-stabilizing protein, regulates Rac1 activity and
RT cell motility through interaction with GEF-H1.";
RL J. Cell Sci. 124:1214-1223(2011).
CC -!- FUNCTION: Microtubule-stabilizing protein that may be involved in the
CC regulation of microtubule dynamics and cytoskeletal organization. May
CC act as a regulator of RAC1 activity through interaction with ARHGEF2 to
CC control lamellipodial formation and cell mobility. Does not seem to
CC have protease activity as it has lost the active site residues.
CC {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:21406564}.
CC -!- SUBUNIT: Interacts (via domain III) with microtubules. Interacts (via
CC domain II) with ARHGEF2 (via the N-terminal zinc finger).
CC {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:21406564}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17210638,
CC ECO:0000269|PubMed:20814968}.
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc expressed in the mandibular arches,
CC heart and limb buds. {ECO:0000269|PubMed:17210638}.
CC -!- INDUCTION: Up-regulated during the osteoclasogenic process. Inhibited
CC by dexamethaxone during the osteoclasogenic process.
CC {ECO:0000269|PubMed:20814968}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; Y12582; CAA73161.1; -; mRNA.
DR EMBL; AK145116; BAE26243.1; -; mRNA.
DR EMBL; BX530055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30455.1; -.
DR RefSeq; NP_031629.3; NM_007603.3.
DR AlphaFoldDB; O35646; -.
DR SMR; O35646; -.
DR BioGRID; 198475; 8.
DR STRING; 10090.ENSMUSP00000084573; -.
DR MEROPS; C02.971; -.
DR iPTMnet; O35646; -.
DR PhosphoSitePlus; O35646; -.
DR MaxQB; O35646; -.
DR PaxDb; O35646; -.
DR PeptideAtlas; O35646; -.
DR PRIDE; O35646; -.
DR ProteomicsDB; 281765; -.
DR Antibodypedia; 29529; 218 antibodies from 33 providers.
DR DNASU; 12338; -.
DR Ensembl; ENSMUST00000087316; ENSMUSP00000084573; ENSMUSG00000067276.
DR GeneID; 12338; -.
DR KEGG; mmu:12338; -.
DR UCSC; uc009umk.2; mouse.
DR CTD; 827; -.
DR MGI; MGI:1100850; Capn6.
DR VEuPathDB; HostDB:ENSMUSG00000067276; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000156128; -.
DR HOGENOM; CLU_010982_3_2_1; -.
DR InParanoid; O35646; -.
DR OMA; QKGRYTD; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; O35646; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.B26; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 12338; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Capn6; mouse.
DR PRO; PR:O35646; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O35646; protein.
DR Bgee; ENSMUSG00000067276; Expressed in humerus cartilage element and 205 other tissues.
DR Genevisible; O35646; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
DR CDD; cd04046; C2_Calpain; 1.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR033884; C2_Calpain.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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; IPR001300; Peptidase_C2_calpain_cat.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT CHAIN 1..641
FT /note="Calpain-6"
FT /id="PRO_0000207718"
FT DOMAIN 26..343
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 498..621
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 344..495
FT /note="Domain III"
FT CONFLICT 568
FT /note="I -> V (in Ref. 1; CAA73161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 74543 MW; 3F7D8DBC615B57A1 CRC64;
MGPPLKLFKN QKYQELKQEC MKDGRLFCDP TFLPENDSLF FNRLLPGKVV WKRPQDISDD
PHLIVGNISN HQLIQGRLGN KAMISAFSCL AVQESHWTKA IPNHKDQEWD PRKPEKYAGI
FHFRFWHFGE WTEVVIDDLL PTINGDLVFS FSTSMNEFWN ALLEKAYAKL LGCYEALDGL
TITDIIMDFT GTLAEIIDMQ KGRYTDLVEE KYKLFGELYK TFTKGGLICC SIESPSQEEQ
EVETDWGLLK GYTYTMTDIR KLRLGERLVE VFSTEKLYMV RLRNPLGRQE WSGPWSEISE
EWQQLTVTDR KNLGLVMSDD GEFWMSLEDF CHNFHKLNVC RNVNNPVFGR KELESVVGCW
TVDDDPLMNR SGGCYNNRDT FLQNPQYIFT VPEDGHKVIM SLQQKDLRTY RRMGRPDNYI
IGFELFKVEM NRRFRLHHLY IQERAGTSTY IDTRTVFLSK YLKKGSYVLV PTMFQHGRTS
EFLLRIFSEV PVQLRELTLD MPKMSCWNLA RGYPKVVTQI TVHSAEGLEK KYANETVNPY
LIIKCGKEEV RSPVQKNTVH AIFDTQAIFY RRTTDIPIII QVWNSRKFCD QFLGQVTLDA
DPSDCRDLKS LYLRKKGGPT AKVKQGHISF KVISSDDLTE L
