CPNS2_HUMAN
ID CPNS2_HUMAN Reviewed; 248 AA.
AC Q96L46; Q9BPV4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Calpain small subunit 2;
DE Short=CSS2;
DE AltName: Full=Calcium-dependent protease small subunit 2;
GN Name=CAPNS2;
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 [MRNA].
RX PubMed=11853546; DOI=10.1042/0264-6021:3620383;
RA Schad E., Farkas A., Jekely G., Tompa P., Friedrich P.;
RT "A novel human small subunit of calpains.";
RL Biochem. J. 362:383-388(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder carcinoma;
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).
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.
CC -!- SUBUNIT: Heterodimer of a large (catalytic) and a small (regulatory)
CC subunit.
CC -!- INTERACTION:
CC Q96L46; Q8N2F6-2: ARMC10; NbExp=3; IntAct=EBI-12188723, EBI-12902762;
CC Q96L46; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-12188723, EBI-11522780;
CC Q96L46; Q96HP4: OXNAD1; NbExp=3; IntAct=EBI-12188723, EBI-2862111;
CC Q96L46; Q96KR7: PHACTR3; NbExp=3; IntAct=EBI-12188723, EBI-717068;
CC Q96L46; P45877: PPIC; NbExp=3; IntAct=EBI-12188723, EBI-953909;
CC Q96L46; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-12188723, EBI-1567797;
CC Q96L46; Q13671: RIN1; NbExp=3; IntAct=EBI-12188723, EBI-366017;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium
CC binding. {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Calpains homepage;
CC URL="https://cals.arizona.edu/calpains/";
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DR EMBL; AY052551; AAL02241.1; -; mRNA.
DR EMBL; BC005397; AAH05397.1; -; mRNA.
DR EMBL; BC006000; AAH06000.1; -; mRNA.
DR CCDS; CCDS54010.1; -.
DR RefSeq; NP_115706.1; NM_032330.2.
DR AlphaFoldDB; Q96L46; -.
DR SMR; Q96L46; -.
DR BioGRID; 124017; 70.
DR IntAct; Q96L46; 21.
DR STRING; 9606.ENSP00000400882; -.
DR iPTMnet; Q96L46; -.
DR PhosphoSitePlus; Q96L46; -.
DR BioMuta; CAPNS2; -.
DR DMDM; 45476965; -.
DR jPOST; Q96L46; -.
DR MassIVE; Q96L46; -.
DR MaxQB; Q96L46; -.
DR PaxDb; Q96L46; -.
DR PeptideAtlas; Q96L46; -.
DR PRIDE; Q96L46; -.
DR ProteomicsDB; 77149; -.
DR Antibodypedia; 58579; 166 antibodies from 26 providers.
DR DNASU; 84290; -.
DR Ensembl; ENST00000457326.3; ENSP00000400882.2; ENSG00000256812.2.
DR GeneID; 84290; -.
DR KEGG; hsa:84290; -.
DR MANE-Select; ENST00000457326.3; ENSP00000400882.2; NM_032330.3; NP_115706.1.
DR UCSC; uc002eid.2; human.
DR CTD; 84290; -.
DR DisGeNET; 84290; -.
DR GeneCards; CAPNS2; -.
DR HGNC; HGNC:16371; CAPNS2.
DR HPA; ENSG00000256812; Tissue enhanced (esophagus, skin, vagina).
DR neXtProt; NX_Q96L46; -.
DR OpenTargets; ENSG00000256812; -.
DR PharmGKB; PA134873146; -.
DR VEuPathDB; HostDB:ENSG00000256812; -.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000166682; -.
DR HOGENOM; CLU_051357_2_0_1; -.
DR InParanoid; Q96L46; -.
DR OMA; NLDIKEW; -.
DR OrthoDB; 1330600at2759; -.
DR PhylomeDB; Q96L46; -.
DR TreeFam; TF314682; -.
DR PathwayCommons; Q96L46; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
DR SignaLink; Q96L46; -.
DR BioGRID-ORCS; 84290; 7 hits in 1071 CRISPR screens.
DR GenomeRNAi; 84290; -.
DR Pharos; Q96L46; Tbio.
DR PRO; PR:Q96L46; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96L46; protein.
DR Bgee; ENSG00000256812; Expressed in esophagus squamous epithelium and 101 other tissues.
DR Genevisible; Q96L46; HS.
DR GO; GO:0110158; C:calpain complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:MGI.
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 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..248
FT /note="Calpain small subunit 2"
FT /id="PRO_0000073718"
FT DOMAIN 119..152
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 149..184
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 185..213
FT /note="EF-hand 3"
FT /evidence="ECO:0000305"
FT DOMAIN 214..248
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
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 138
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 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT CONFLICT 74
FT /note="E -> Q (in Ref. 1; AAL02241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27660 MW; F40AD8778FF41600 CRC64;
MFLAKALLEG ADRGLGEALG GLFGGGGQRR EGGGRNIGGI VGGIVNFISE AAAAQYTPEP
PPTQQHFTSV EASESEEVRR FRQQFTQLAG PDMEVGATDL MNILNKVLSK HKDLKTDGFS
LDTCRSIVSV MDSDTTGKLG FEEFKYLWNN IKKWQCVYKQ YDRDHSGSLG SSQLRGALQA
AGFQLNEQLY QMIVRRYANE DGDMDFNNFI SCLVRLDAMF RAFKSLDRDR DGLIQVSIKE
WLQLTMYS
