CPNS1_RAT
ID CPNS1_RAT Reviewed; 270 AA.
AC Q64537; P97572; Q4V795;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 172.
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, Css1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-270.
RX PubMed=8950173; DOI=10.1016/s0167-4781(96)00135-2;
RA Sorimachi H., Amano S., Ishiura S., Suzuki K.;
RT "Primary sequences of rat mu-calpain large and small subunits are,
RT respectively, moderately and highly similar to those of human.";
RL Biochim. Biophys. Acta 1309:37-41(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-270, PARTIAL PROTEIN SEQUENCE, DOMAIN,
RP SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 84-266.
RX PubMed=7982961; DOI=10.1016/s0021-9258(18)43835-5;
RA Graham-Siegenthaler K., Gauthier S., Davies P.L., Elce J.S.;
RT "Active recombinant rat calpain II. Bacterially produced large and small
RT subunits associate both in vivo and in vitro.";
RL J. Biol. Chem. 269:30457-30460(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 98-270 IN COMPLEX WITH CALCIUM,
RP SUBUNIT, AND DOMAIN.
RX PubMed=9228945; DOI=10.1038/nsb0797-532;
RA Blanchard H., Grochulski P., Li Y., Arthur J.S.C., Davies P.L., Elce J.S.,
RA Cygler M.;
RT "Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and
RT Ca(2+)-induced conformational changes.";
RL Nat. Struct. Biol. 4:532-538(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 91-249, DOMAIN, AND SUBUNIT.
RX PubMed=14579356; DOI=10.1002/prot.10453;
RA Leinala E.K., Arthur J.S., Grochulski P., Davies P.L., Elce J.S., Jia Z.;
RT "A second binding site revealed by C-terminal truncation of calpain small
RT subunit, a penta-EF-hand protein.";
RL Proteins 53:649-655(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 88-270, AND SUBUNIT.
RX PubMed=15476820; DOI=10.1016/j.jmb.2004.08.073;
RA Hosfield C.M., Elce J.S., Jia Z.;
RT "Activation of calpain by Ca2+: roles of the large subunit N-terminal and
RT domain III-IV linker peptides.";
RL J. Mol. Biol. 343:1049-1053(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 88-270 IN COMPLEX WITH CAPN2 AND
RP CALPASTATIN, CALCIUM-BINDING SITES, AND SUBUNIT.
RX PubMed=19020623; DOI=10.1038/nature07451;
RA Hanna R.A., Campbell R.L., Davies P.L.;
RT "Calcium-bound structure of calpain and its mechanism of inhibition by
RT calpastatin.";
RL Nature 456:409-412(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 88-270 IN COMPLEX WITH CAPN2 AND
RP CALPASTATIN, CALCIUM-BINDING SITES, AND SUBUNIT.
RX PubMed=19020622; DOI=10.1038/nature07353;
RA Moldoveanu T., Gehring K., Green D.R.;
RT "Concerted multi-pronged attack by calpastatin to occlude the catalytic
RT cleft of heterodimeric calpains.";
RL Nature 456:404-408(2008).
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 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q64537; Q07009: Capn2; NbExp=8; IntAct=EBI-918712, EBI-1040438;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to
CC the plasma membrane upon calcium binding (By similarity). Allows the
CC 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: 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; BC098068; AAH98068.1; -; mRNA.
DR EMBL; U53859; AAC53002.1; -; mRNA.
DR EMBL; U10861; AAA64828.1; -; mRNA.
DR PIR; A55143; A55143.
DR RefSeq; NP_058814.1; NM_017118.1.
DR RefSeq; XP_017445520.1; XM_017590031.1.
DR PDB; 1AJ5; X-ray; 2.30 A; A/B=98-270.
DR PDB; 1DF0; X-ray; 2.60 A; B=88-270.
DR PDB; 1DVI; X-ray; 2.30 A; A/B=88-270.
DR PDB; 1NP8; X-ray; 2.00 A; A/B=91-249.
DR PDB; 1QXP; X-ray; 2.80 A; A/B=88-270.
DR PDB; 1U5I; X-ray; 2.86 A; B=88-270.
DR PDB; 3BOW; X-ray; 2.40 A; B=88-270.
DR PDB; 3DF0; X-ray; 2.95 A; B=87-270.
DR PDBsum; 1AJ5; -.
DR PDBsum; 1DF0; -.
DR PDBsum; 1DVI; -.
DR PDBsum; 1NP8; -.
DR PDBsum; 1QXP; -.
DR PDBsum; 1U5I; -.
DR PDBsum; 3BOW; -.
DR PDBsum; 3DF0; -.
DR AlphaFoldDB; Q64537; -.
DR SMR; Q64537; -.
DR DIP; DIP-6140N; -.
DR IntAct; Q64537; 4.
DR MINT; Q64537; -.
DR STRING; 10116.ENSRNOP00000064489; -.
DR iPTMnet; Q64537; -.
DR PhosphoSitePlus; Q64537; -.
DR jPOST; Q64537; -.
DR PaxDb; Q64537; -.
DR PRIDE; Q64537; -.
DR GeneID; 29156; -.
DR KEGG; rno:29156; -.
DR UCSC; RGD:2270; rat.
DR CTD; 826; -.
DR RGD; 2270; Capns1.
DR eggNOG; KOG0037; Eukaryota.
DR InParanoid; Q64537; -.
DR OrthoDB; 1330600at2759; -.
DR PhylomeDB; Q64537; -.
DR BRENDA; 3.4.22.B24; 5301.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR EvolutionaryTrace; Q64537; -.
DR PRO; PR:Q64537; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0110158; C:calpain complex; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; TAS:RGD.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0030163; P:protein catabolic process; IMP:RGD.
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 3D-structure; Acetylation; Calcium; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..270
FT /note="Calpain small subunit 1"
FT /id="PRO_0000073717"
FT DOMAIN 98..132
FT /note="EF-hand 1; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 141..174
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 171..206
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 207..235
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT DOMAIN 236..270
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19020622,
FT ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945,
FT ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW,
FT ECO:0007744|PDB:3DF0"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19020622,
FT ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945,
FT ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW,
FT ECO:0007744|PDB:3DF0"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19020622,
FT ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945,
FT ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW,
FT ECO:0007744|PDB:3DF0"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19020622,
FT ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945,
FT ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW,
FT ECO:0007744|PDB:3DF0"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:19020622,
FT ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945,
FT ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW,
FT ECO:0007744|PDB:3DF0"
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 ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
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 ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:19020622, ECO:0000269|PubMed:19020623,
FT ECO:0000269|PubMed:9228945, ECO:0007744|PDB:1DVI,
FT ECO:0007744|PDB:3BOW, ECO:0007744|PDB:3DF0"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:19020622,
FT ECO:0000269|PubMed:19020623, ECO:0000269|PubMed:9228945,
FT ECO:0007744|PDB:1DVI, ECO:0007744|PDB:3BOW,
FT ECO:0007744|PDB:3DF0"
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 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04632"
FT CONFLICT 87
FT /note="S -> M (in Ref. 3; AAA64828)"
FT /evidence="ECO:0000305"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:1NP8"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1NP8"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:1NP8"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1AJ5"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:1NP8"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1NP8"
FT HELIX 163..183
FT /evidence="ECO:0007829|PDB:1NP8"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1NP8"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1NP8"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:1NP8"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:1NP8"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1DVI"
FT HELIX 228..243
FT /evidence="ECO:0007829|PDB:1NP8"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:1DF0"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:1DVI"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:1AJ5"
SQ SEQUENCE 270 AA; 28570 MW; 63609614CD4D3EB7 CRC64;
MFLVNSFLKG GGGGGGGGGL GGGLGNVLGG LISGAAGGGG GGGGGGGMGL GGGGGGGGTA
MRILGGVISA ISEAAAQYNP EPPPPRSHYS NIEANESEEE RQFRKLFVQL AGDDMEVSAT
ELMNILNKVV TRHPDLKTDG FGIDTCRSMV AVMDSDTTGK LGFEEFKYLW NNIKKWQGIY
KRFDTDRSGT IGSNELPGAF EAAGFHLNQH IYSMIIRRYS DETGNMDFDN FISCLVRLDA
MFRAFRSLDK NGTGQIQVNI QEWLQLTMYS
