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Calpain small subunit 1 (CSS1) (Calcium-activated neutral proteinase small subunit) (CANP small subunit) (Calcium-dependent protease small subunit) (CDPS) (Calcium-dependent protease small subunit 1) (Calpain regulatory subunit)

 CPNS1_RAT               Reviewed;         270 AA.
Q64537; P97572; Q4V795;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 3.
30-AUG-2017, entry version 146.
RecName: Full=Calpain small subunit 1;
Short=CSS1;
AltName: Full=Calcium-activated neutral proteinase small subunit;
Short=CANP small subunit;
AltName: Full=Calcium-dependent protease small subunit;
Short=CDPS;
AltName: Full=Calcium-dependent protease small subunit 1;
AltName: Full=Calpain regulatory subunit;
Name=Capns1; Synonyms=Capn4, Css1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-270.
PubMed=8950173; DOI=10.1016/S0167-4781(96)00135-2;
Sorimachi H., Amano S., Ishiura S., Suzuki K.;
"Primary sequences of rat mu-calpain large and small subunits are,
respectively, moderately and highly similar to those of human.";
Biochim. Biophys. Acta 1309:37-41(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 87-270, PARTIAL PROTEIN SEQUENCE,
DOMAIN, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 84-266.
PubMed=7982961;
Graham-Siegenthaler K., Gauthier S., Davies P.L., Elce J.S.;
"Active recombinant rat calpain II. Bacterially produced large and
small subunits associate both in vivo and in vitro.";
J. Biol. Chem. 269:30457-30460(1994).
[4]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 98-270 IN COMPLEX WITH
CALCIUM, SUBUNIT, AND DOMAIN.
PubMed=9228945; DOI=10.1038/nsb0797-532;
Blanchard H., Grochulski P., Li Y., Arthur J.S.C., Davies P.L.,
Elce J.S., Cygler M.;
"Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand
and Ca(2+)-induced conformational changes.";
Nat. Struct. Biol. 4:532-538(1997).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 91-249, DOMAIN, AND SUBUNIT.
PubMed=14579356; DOI=10.1002/prot.10453;
Leinala E.K., Arthur J.S., Grochulski P., Davies P.L., Elce J.S.,
Jia Z.;
"A second binding site revealed by C-terminal truncation of calpain
small subunit, a penta-EF-hand protein.";
Proteins 53:649-655(2003).
[6]
X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 88-270, AND SUBUNIT.
PubMed=15476820; DOI=10.1016/j.jmb.2004.08.073;
Hosfield C.M., Elce J.S., Jia Z.;
"Activation of calpain by Ca2+: roles of the large subunit N-terminal
and domain III-IV linker peptides.";
J. Mol. Biol. 343:1049-1053(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 88-270 IN COMPLEX WITH CAPN2
AND CALPASTATIN, CALCIUM-BINDING SITES, AND SUBUNIT.
PubMed=19020623; DOI=10.1038/nature07451;
Hanna R.A., Campbell R.L., Davies P.L.;
"Calcium-bound structure of calpain and its mechanism of inhibition by
calpastatin.";
Nature 456:409-412(2008).
[8]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 88-270 IN COMPLEX WITH CAPN2
AND CALPASTATIN, CALCIUM-BINDING SITES, AND SUBUNIT.
PubMed=19020622; DOI=10.1038/nature07353;
Moldoveanu T., Gehring K., Green D.R.;
"Concerted multi-pronged attack by calpastatin to occlude the
catalytic cleft of heterodimeric calpains.";
Nature 456:404-408(2008).
-!- FUNCTION: Regulatory subunit of the calcium-regulated non-
lysosomal thiol-protease which catalyzes limited proteolysis of
substrates involved in cytoskeletal remodeling and signal
transduction.
-!- SUBUNIT: Homodimer or heterodimer of a large (catalytic) and a
small (regulatory) subunit. In presence of calcium, the
heterodimer dissociates (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates
to the plasma membrane upon calcium binding (By similarity).
Allows the formation of the homodimer and also appears to mediate
the contact between the large catalytic subunit and small
regulatory subunit for the formation of the heterodimer.
{ECO:0000250}.
-!- DOMAIN: The contact of the 5th EF-hand domain from each monomer
allows the formation of the homodimer and also appears to mediate
the contact between the large catalytic subunit and small
regulatory subunit for the formation of the heterodimer.
-!- DOMAIN: EF-hand domains are paired. EF-hand 1 is paired with EF-
hand 2 and EF-hand 3 is paired with EF-hand 4. The fifth EF-hand
domain, left unpaired, does not bind the calcium but is
responsible of the dimerization by EF-embrace. The first four EF-
hand domains bind calcium, however it is not sure if the binding
of EF-hand 4 to calcium is physiologically relevant.
-----------------------------------------------------------------------
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EMBL; BC098068; AAH98068.1; -; mRNA.
EMBL; U53859; AAC53002.1; -; mRNA.
EMBL; U10861; AAA64828.1; -; mRNA.
PIR; A55143; A55143.
RefSeq; NP_058814.1; NM_017118.1.
RefSeq; XP_017445520.1; XM_017590031.1.
UniGene; Rn.3430; -.
PDB; 1AJ5; X-ray; 2.30 A; A/B=98-270.
PDB; 1DF0; X-ray; 2.60 A; B=88-270.
PDB; 1DVI; X-ray; 2.30 A; A/B=88-270.
PDB; 1NP8; X-ray; 2.00 A; A/B=91-249.
PDB; 1U5I; X-ray; 2.86 A; B=88-270.
PDB; 3BOW; X-ray; 2.40 A; B=88-270.
PDB; 3DF0; X-ray; 2.95 A; B=87-270.
PDBsum; 1AJ5; -.
PDBsum; 1DF0; -.
PDBsum; 1DVI; -.
PDBsum; 1NP8; -.
PDBsum; 1U5I; -.
PDBsum; 3BOW; -.
PDBsum; 3DF0; -.
ProteinModelPortal; Q64537; -.
SMR; Q64537; -.
DIP; DIP-6140N; -.
IntAct; Q64537; 2.
MINT; MINT-112921; -.
STRING; 10116.ENSRNOP00000067513; -.
iPTMnet; Q64537; -.
PhosphoSitePlus; Q64537; -.
PaxDb; Q64537; -.
PRIDE; Q64537; -.
GeneID; 100912380; -.
GeneID; 29156; -.
KEGG; rno:100912380; -.
KEGG; rno:29156; -.
UCSC; RGD:2270; rat.
CTD; 826; -.
RGD; 2270; Capns1.
eggNOG; KOG0037; Eukaryota.
eggNOG; ENOG410YKQK; LUCA.
HOGENOM; HOG000063658; -.
HOVERGEN; HBG004492; -.
InParanoid; Q64537; -.
KO; K08583; -.
PhylomeDB; Q64537; -.
BRENDA; 3.4.22.B24; 5301.
EvolutionaryTrace; Q64537; -.
PRO; PR:Q64537; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; TAS:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0006508; P:proteolysis; IMP:RGD.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13833; EF-hand_8; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Cell membrane; Complete proteome;
Cytoplasm; Direct protein sequencing; Membrane; Metal-binding;
Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 270 Calpain small subunit 1.
/FTId=PRO_0000073717.
DOMAIN 98 132 EF-hand 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00448}.
DOMAIN 141 174 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 171 206 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 207 235 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 236 270 EF-hand 5. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 110 121 1. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
CA_BIND 154 165 2. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
CA_BIND 184 195 3. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
COMPBIAS 1 66 Gly-rich (hydrophobic).
COMPBIAS 10 25 Poly-Gly.
COMPBIAS 37 58 Poly-Gly.
COMPBIAS 80 85 Poly-Pro.
METAL 111 111 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 114 114 Calcium 1. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 116 116 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 121 121 Calcium 1. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 139 139 Calcium 4. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 154 154 Calcium 2. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 156 156 Calcium 2. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 158 158 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 160 160 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 165 165 Calcium 2. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 184 184 Calcium 3. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 186 186 Calcium 3. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 188 188 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 190 190 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 195 195 Calcium 3. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
METAL 227 227 Calcium 4. {ECO:0000244|PDB:1DVI,
ECO:0000244|PDB:3BOW,
ECO:0000244|PDB:3DF0,
ECO:0000269|PubMed:19020622,
ECO:0000269|PubMed:19020623,
ECO:0000269|PubMed:9228945}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P04632}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:P04632}.
MOD_RES 181 181 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04632}.
CONFLICT 87 87 S -> M (in Ref. 3; AAA64828).
{ECO:0000305}.
HELIX 98 111 {ECO:0000244|PDB:1NP8}.
HELIX 112 114 {ECO:0000244|PDB:1NP8}.
HELIX 119 132 {ECO:0000244|PDB:1NP8}.
TURN 134 136 {ECO:0000244|PDB:1AJ5}.
HELIX 143 153 {ECO:0000244|PDB:1NP8}.
STRAND 158 161 {ECO:0000244|PDB:1NP8}.
HELIX 163 183 {ECO:0000244|PDB:1NP8}.
STRAND 188 191 {ECO:0000244|PDB:1NP8}.
TURN 193 195 {ECO:0000244|PDB:1NP8}.
HELIX 196 202 {ECO:0000244|PDB:1NP8}.
HELIX 209 219 {ECO:0000244|PDB:1NP8}.
STRAND 224 226 {ECO:0000244|PDB:1DVI}.
HELIX 228 243 {ECO:0000244|PDB:1NP8}.
TURN 248 251 {ECO:0000244|PDB:1DF0}.
STRAND 253 258 {ECO:0000244|PDB:1DVI}.
HELIX 260 268 {ECO:0000244|PDB:1AJ5}.
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


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