CPNS2_MOUSE
ID CPNS2_MOUSE Reviewed; 247 AA.
AC Q9D7J7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Calpain small subunit 2;
DE Short=CSS2;
DE AltName: Full=Calcium-dependent protease small subunit 2;
GN Name=Capns2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyzes limited proteolysis of substrates involved in cytoskeletal
CC remodeling and signal transduction. This small subunit may act as a
CC tissue-specific chaperone of the large subunit, possibly by helping it
CC fold into its correct conformation for activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of a large (catalytic) and a small (regulatory)
CC subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium
CC binding. {ECO:0000250}.
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DR EMBL; AK009171; BAB26120.1; -; mRNA.
DR CCDS; CCDS52634.1; -.
DR RefSeq; NP_081388.1; NM_027112.1.
DR AlphaFoldDB; Q9D7J7; -.
DR SMR; Q9D7J7; -.
DR BioGRID; 213517; 1.
DR STRING; 10090.ENSMUSP00000100553; -.
DR iPTMnet; Q9D7J7; -.
DR PhosphoSitePlus; Q9D7J7; -.
DR MaxQB; Q9D7J7; -.
DR PaxDb; Q9D7J7; -.
DR PeptideAtlas; Q9D7J7; -.
DR PRIDE; Q9D7J7; -.
DR ProteomicsDB; 278021; -.
DR Antibodypedia; 58579; 166 antibodies from 26 providers.
DR Ensembl; ENSMUST00000104947; ENSMUSP00000100553; ENSMUSG00000078144.
DR GeneID; 69543; -.
DR KEGG; mmu:69543; -.
DR UCSC; uc012gik.1; mouse.
DR CTD; 84290; -.
DR MGI; MGI:1916793; Capns2.
DR VEuPathDB; HostDB:ENSMUSG00000078144; -.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000166682; -.
DR HOGENOM; CLU_051357_2_0_1; -.
DR InParanoid; Q9D7J7; -.
DR OMA; NLDIKEW; -.
DR OrthoDB; 1330600at2759; -.
DR PhylomeDB; Q9D7J7; -.
DR TreeFam; TF314682; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 69543; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9D7J7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D7J7; protein.
DR Bgee; ENSMUSG00000078144; Expressed in skin of external ear and 38 other tissues.
DR Genevisible; Q9D7J7; MM.
DR GO; GO:0110158; C:calpain complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:Ensembl.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13833; EF-hand_8; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..247
FT /note="Calpain small subunit 2"
FT /id="PRO_0000073719"
FT DOMAIN 118..151
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 148..183
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 184..212
FT /note="EF-hand 3"
FT /evidence="ECO:0000305"
FT DOMAIN 213..247
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q64537,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q64537,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
SQ SEQUENCE 247 AA; 27190 MW; 0507EF8C3D7E46F2 CRC64;
MFLAKAILEG ADRGLGGALG GLLGGGGQAR AGGGNIGGIL GGIVNFISEA AAAQYTPEPP
PQQQHFTVVE ASESEEVRRF RQQFTQLAGP DMEVGATDLM NILNKVLSKH KELKTEGFSL
DTCRSIVSVM DSDTTGKLGF EEFKYLWNNI KKWQCVFKQY DSDHSGSLGS SQLHGAMQAA
GFQLNEQLYL MIVRRYADED GGMDFNNFIS CLVRLDAMFR AFKALDRDRD GLIQVSIREW
LQLTMYS
