CPNS1_PIG
ID CPNS1_PIG Reviewed; 266 AA.
AC P04574; Q8SPJ8;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 161.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2994060; DOI=10.1073/pnas.82.18.6075;
RA Sakihama T., Kakidani H., Zenita K., Yumoto N., Kikuchi T., Sasaki T.,
RA Kannagi R., Nakanishi S., Ohmori M., Takio K., Titani K., Murachi T.;
RT "A putative Ca2+-binding protein: structure of the light subunit of porcine
RT calpain elucidated by molecular cloning and protein sequence analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6075-6079(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Leeb T.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 94-266, DOMAIN, AND
RP CALCIUM-BINDING SITES.
RX PubMed=9228946; DOI=10.1038/nsb0797-539;
RA Lin G.D., Chattopadhyay D., Maki M., Wang K.K., Carson M., Jin L.,
RA Yuen P.W., Takano E., Hatanaka M., Delucas L.J., Narayana S.V.;
RT "Crystal structure of calcium bound domain VI of calpain at 1.9-A
RT resolution and its role in enzyme assembly, regulation, and inhibitor
RT binding.";
RL Nat. Struct. Biol. 4:539-547(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 94-266 IN COMPLEX WITH INHIBITOR,
RP DOMAIN, AND CALCIUM-BINDING SITES.
RX PubMed=12684003; DOI=10.1016/s0022-2836(03)00274-2;
RA Todd B., Moore D., Deivanayagam C.C., Lin G.D., Chattopadhyay D., Maki M.,
RA Wang K.K., Narayana S.V.;
RT "A structural model for the inhibition of calpain by calpastatin: crystal
RT structures of the native domain VI of calpain and its complexes with
RT calpastatin peptide and a small molecule inhibitor.";
RL J. Mol. Biol. 328:131-146(2003).
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 (By similarity).
CC {ECO:0000250|UniProtKB:O88456}.
CC -!- SUBUNIT: Homodimer or heterodimer of a large (catalytic) and a small
CC (regulatory) subunit. In presence of calcium, the heterodimer
CC dissociates. {ECO:0000269|PubMed:12684003}.
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.
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.
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DR EMBL; M11778; AAA31010.1; -; mRNA.
DR EMBL; M11779; AAA31011.1; -; mRNA.
DR EMBL; AJ410870; CAC85483.2; -; Genomic_DNA.
DR PIR; A25166; CIPGL.
DR PIR; S39392; S39392.
DR RefSeq; NP_999483.1; NM_214318.2.
DR PDB; 1ALV; X-ray; 1.90 A; A/B=94-266.
DR PDB; 1ALW; X-ray; 2.03 A; A/B=94-266.
DR PDB; 1NX0; X-ray; 2.30 A; A/B=94-266.
DR PDB; 1NX1; X-ray; 2.00 A; A/B=94-266.
DR PDB; 1NX2; X-ray; 2.20 A; A=94-266.
DR PDB; 1NX3; X-ray; 2.45 A; A=94-266.
DR PDB; 4PHN; X-ray; 1.79 A; A/B=94-266.
DR PDBsum; 1ALV; -.
DR PDBsum; 1ALW; -.
DR PDBsum; 1NX0; -.
DR PDBsum; 1NX1; -.
DR PDBsum; 1NX2; -.
DR PDBsum; 1NX3; -.
DR PDBsum; 4PHN; -.
DR AlphaFoldDB; P04574; -.
DR SMR; P04574; -.
DR IntAct; P04574; 1.
DR STRING; 9823.ENSSSCP00000025968; -.
DR BindingDB; P04574; -.
DR ChEMBL; CHEMBL2205; -.
DR PaxDb; P04574; -.
DR PeptideAtlas; P04574; -.
DR PRIDE; P04574; -.
DR Ensembl; ENSSSCT00025084678; ENSSSCP00025036836; ENSSSCG00025061681.
DR Ensembl; ENSSSCT00030034851; ENSSSCP00030015901; ENSSSCG00030024958.
DR Ensembl; ENSSSCT00035044573; ENSSSCP00035017837; ENSSSCG00035033634.
DR Ensembl; ENSSSCT00040103090; ENSSSCP00040046648; ENSSSCG00040074544.
DR Ensembl; ENSSSCT00045065012; ENSSSCP00045045985; ENSSSCG00045037628.
DR Ensembl; ENSSSCT00050032028; ENSSSCP00050013378; ENSSSCG00050023744.
DR Ensembl; ENSSSCT00055045351; ENSSSCP00055036144; ENSSSCG00055023005.
DR Ensembl; ENSSSCT00055045479; ENSSSCP00055036250; ENSSSCG00055023005.
DR Ensembl; ENSSSCT00060093870; ENSSSCP00060040612; ENSSSCG00060068749.
DR Ensembl; ENSSSCT00065095464; ENSSSCP00065041775; ENSSSCG00065069526.
DR Ensembl; ENSSSCT00070016339; ENSSSCP00070013531; ENSSSCG00070008417.
DR GeneID; 397587; -.
DR KEGG; ssc:397587; -.
DR CTD; 826; -.
DR eggNOG; KOG0037; Eukaryota.
DR HOGENOM; CLU_051357_2_0_1; -.
DR InParanoid; P04574; -.
DR OMA; MCRAFQT; -.
DR OrthoDB; 1330600at2759; -.
DR TreeFam; TF314682; -.
DR BRENDA; 3.4.22.B24; 6170.
DR Reactome; R-SSC-1474228; Degradation of the extracellular matrix.
DR Reactome; R-SSC-6809371; Formation of the cornified envelope.
DR EvolutionaryTrace; P04574; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 6.
DR Genevisible; P04574; SS.
DR GO; GO:0110158; C:calpain complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:CAFA.
DR GO; GO:0006508; P:proteolysis; IDA:CAFA.
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 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 3D-structure; Acetylation; Calcium; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..266
FT /note="Calpain small subunit 1"
FT /id="PRO_0000073715"
FT DOMAIN 94..128
FT /note="EF-hand 1; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 137..170
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 167..202
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 203..231
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT DOMAIN 232..266
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 110
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 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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:0000250|UniProtKB:Q64537,
FT 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 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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:0000250|UniProtKB:Q64537,
FT 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 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 223
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 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04632"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:4PHN"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:4PHN"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:4PHN"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:4PHN"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4PHN"
FT HELIX 159..179
FT /evidence="ECO:0007829|PDB:4PHN"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:4PHN"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:4PHN"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:4PHN"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:4PHN"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:4PHN"
FT HELIX 224..244
FT /evidence="ECO:0007829|PDB:4PHN"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1ALV"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:4PHN"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:4PHN"
SQ SEQUENCE 266 AA; 28068 MW; 3FA81023EDC4141A CRC64;
MFLVNSFLKG GGGGGGGGGG LGGGLGNVLG GLISGAGGGG GGGGGGGGGG GGGGTAMRIL
GGVISAISEA AAQYNPEPPP PRTHYSNIEA NESEEVRQFR RLFAQLAGDD MEVSATELMN
ILNKVVTRHP DLKTDGFGID TCRSMVAVMD SDTTGKLGFE EFKYLWNNIK KWQAIYKQFD
VDRSGTIGSS ELPGAFEAAG FHLNEHLYSM IIRRYSDEGG NMDFDNFISC LVRLDAMFRA
FKSLDKDGTG QIQVNIQEWL QLTMYS
