CPNS1_MOUSE
ID CPNS1_MOUSE Reviewed; 268 AA.
AC O88456; A0A0R4IZW8; D3YW48; Q3V0X5; Q5BKQ2; Q8CEI2; Q8VEK4; Q9R1C5;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Calpain small subunit 1;
DE Short=CSS1;
DE AltName: Full=Calcium-activated neutral proteinase small subunit;
DE Short=CANP small subunit;
DE AltName: Full=Calcium-dependent protease small subunit;
DE Short=CDPS;
DE AltName: Full=Calcium-dependent protease small subunit 1;
DE AltName: Full=Calpain regulatory subunit;
GN Name=Capns1; Synonyms=Capn4;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv;
RX PubMed=9774740; DOI=10.1016/s0167-4838(98)00166-6;
RA Arthur J.S.C., Greer P.A., Elce J.S.;
RT "Structure of the mouse calpain small subunit gene.";
RL Biochim. Biophys. Acta 1388:247-252(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-268.
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum, Kidney, and Testis;
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10825211; DOI=10.1128/mcb.20.12.4474-4481.2000;
RA Arthur J.S.C., Elce J.S., Hegadorn C., Williams K., Greer P.A.;
RT "Disruption of the murine calpain small subunit gene, Capn4: calpain is
RT essential for embryonic development but not for cell growth and division.";
RL Mol. Cell. Biol. 20:4474-4481(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulatory subunit of the calcium-regulated non-lysosomal
CC thiol-protease which catalyzes limited proteolysis of substrates
CC involved in cytoskeletal remodeling and signal transduction. Essential
CC for embryonic development (PubMed:10825211).
CC {ECO:0000269|PubMed:10825211}.
CC -!- SUBUNIT: Homodimer or heterodimer of a large (catalytic) and a small
CC (regulatory) subunit. In presence of calcium, the heterodimer
CC dissociates (By similarity). {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}.
CC -!- DOMAIN: The contact of the 5th EF-hand domain from each monomer allows
CC the formation of the homodimer and also appears to mediate the contact
CC between the large catalytic subunit and small regulatory subunit for
CC the formation of the heterodimer. {ECO:0000250}.
CC -!- DOMAIN: EF-hand domains are paired. EF-hand 1 is paired with EF-hand 2
CC and EF-hand 3 is paired with EF-hand 4. The fifth EF-hand domain, left
CC unpaired, does not bind the calcium but is responsible of the
CC dimerization by EF-embrace. The first four EF-hand domains bind
CC calcium, however it is not sure if the binding of EF-hand 4 to calcium
CC is physiologically relevant.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality by 11.5 dpc, with indications
CC of defects in both vasculogenesis and erythropoiesis.
CC {ECO:0000269|PubMed:10825211}.
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DR EMBL; AF139373; AAD38363.2; -; Genomic_DNA.
DR EMBL; AF058298; AAC97194.1; -; mRNA.
DR EMBL; JH584274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC090988; AAH90988.1; -; mRNA.
DR EMBL; BC018352; AAH18352.1; -; mRNA.
DR EMBL; AK028092; BAC25743.1; -; mRNA.
DR EMBL; AK132819; BAE21378.1; -; mRNA.
DR CCDS; CCDS21082.1; -.
DR RefSeq; NP_033925.2; NM_009795.4.
DR RefSeq; XP_006539551.1; XM_006539488.2.
DR AlphaFoldDB; O88456; -.
DR SMR; O88456; -.
DR BioGRID; 198473; 17.
DR ComplexPortal; CPX-4301; M-Calpain complex.
DR ComplexPortal; CPX-4304; mu-Calpain complex.
DR IntAct; O88456; 1.
DR STRING; 10090.ENSMUSP00000001845; -.
DR iPTMnet; O88456; -.
DR PhosphoSitePlus; O88456; -.
DR EPD; O88456; -.
DR jPOST; O88456; -.
DR MaxQB; O88456; -.
DR PaxDb; O88456; -.
DR PeptideAtlas; O88456; -.
DR PRIDE; O88456; -.
DR ProteomicsDB; 283817; -.
DR ProteomicsDB; 328663; -.
DR Antibodypedia; 1704; 260 antibodies from 33 providers.
DR DNASU; 12336; -.
DR Ensembl; ENSMUST00000001845; ENSMUSP00000001845; ENSMUSG00000001794.
DR Ensembl; ENSMUST00000126116; ENSMUSP00000117951; ENSMUSG00000001794.
DR GeneID; 12336; -.
DR KEGG; mmu:12336; -.
DR UCSC; uc009gdq.1; mouse.
DR UCSC; uc009gdr.1; mouse.
DR CTD; 826; -.
DR MGI; MGI:88266; Capns1.
DR VEuPathDB; HostDB:ENSMUSG00000001794; -.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000155478; -.
DR InParanoid; O88456; -.
DR OMA; MCRAFQT; -.
DR OrthoDB; 1330600at2759; -.
DR PhylomeDB; O88456; -.
DR TreeFam; TF314682; -.
DR BRENDA; 3.4.22.B24; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 12336; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Capns1; mouse.
DR PRO; PR:O88456; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O88456; protein.
DR Bgee; ENSMUSG00000001794; Expressed in spermatid and 265 other tissues.
DR GO; GO:0110158; C:calpain complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IC:ComplexPortal.
DR InterPro; IPR029642; CAPN4.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR46735:SF1; PTHR46735:SF1; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..268
FT /note="Calpain small subunit 1"
FT /id="PRO_0000073714"
FT DOMAIN 96..130
FT /note="EF-hand 1; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 139..172
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 169..204
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 205..233
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT DOMAIN 234..268
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
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 158
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 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P04632"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04632"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04632"
FT CONFLICT 45
FT /note="G -> GG (in Ref. 1; AAC97194)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..69
FT /note="AI -> PL (in Ref. 4; BAC25743)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="I -> M (in Ref. 4; BAE21378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 28406 MW; 49C6DD51FBF5026F CRC64;
MFLVNSFLKG GGGGGGGGGL GGGLGNVLGG LISGAAGGGG GGGGGMGLGG GGGGGGTAMR
ILGGVISAIS EAAAQYNPEP PPPRSHYSNI EANESEEVRQ FRKLFVQLAG DDMEVSATEL
MNILNKVVTR HPDLKTDGFG IDTCRSMVAV MDSDTTGKLG FEEFKYLWNN IKKWQAIYKR
FDTDRSGTIG SHELPGAFEA AGFHLNEHLY SMIIRRYADE SGNMDFDNFI SCLVRLDAMF
RAFKSLDKNG TGQIQVNIQE WLQLTMYS
