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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_RABIT             Reviewed;         266 AA.
P06813;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
30-AUG-2017, entry version 124.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3013892;
Emori Y., Kawasaki H., Imajoh S., Kawashima S., Suzuki K.;
"Isolation and sequence analysis of cDNA clones for the small subunit
of rabbit calcium-dependent protease.";
J. Biol. Chem. 261:9472-9476(1986).
[2]
CALCIUM-BINDING, AND DOMAIN.
PubMed=3038855;
Minami Y., Emori Y., Kawasaki H., Suzuki K.;
"E-F hand structure-domain of calcium-activated neutral protease
(CANP) can bind Ca2+ ions.";
J. Biochem. 101:889-895(1987).
-!- 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. 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.
{ECO:0000250}.
-!- 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.
{ECO:0000269|PubMed:3038855}.
-!- PTM: The N-terminus is blocked.
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EMBL; M13364; AAA81565.1; -; mRNA.
PIR; A24816; CIRBL.
RefSeq; NP_001075733.1; NM_001082264.1.
UniGene; Ocu.2040; -.
ProteinModelPortal; P06813; -.
SMR; P06813; -.
STRING; 9986.ENSOCUP00000011273; -.
PRIDE; P06813; -.
Ensembl; ENSOCUT00000013092; ENSOCUP00000011273; ENSOCUG00000013093.
GeneID; 100009090; -.
KEGG; ocu:100009090; -.
CTD; 826; -.
eggNOG; KOG0037; Eukaryota.
eggNOG; ENOG410YKQK; LUCA.
GeneTree; ENSGT00620000087734; -.
HOGENOM; HOG000063658; -.
HOVERGEN; HBG004492; -.
InParanoid; P06813; -.
KO; K08583; -.
OMA; SDEGGNM; -.
OrthoDB; EOG091G0ISY; -.
TreeFam; TF314682; -.
Proteomes; UP000001811; Unplaced.
Bgee; ENSOCUG00000013093; -.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13202; EF-hand_5; 1.
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;
Acetylation; Calcium; Cell membrane; Complete proteome; Cytoplasm;
Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 266 Calpain small subunit 1.
/FTId=PRO_0000073716.
DOMAIN 94 128 EF-hand 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00448}.
DOMAIN 137 170 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 167 202 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 203 231 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 232 266 EF-hand 5. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 106 117 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 150 161 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 180 191 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
COMPBIAS 1 64 Gly-rich (hydrophobic).
COMPBIAS 10 25 Poly-Gly.
COMPBIAS 34 54 Poly-Gly.
COMPBIAS 76 81 Poly-Pro.
METAL 107 107 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q64537}.
METAL 110 110 Calcium 1.
{ECO:0000250|UniProtKB:Q64537}.
METAL 112 112 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q64537}.
METAL 117 117 Calcium 1.
{ECO:0000250|UniProtKB:Q64537}.
METAL 135 135 Calcium 4.
{ECO:0000250|UniProtKB:Q64537}.
METAL 150 150 Calcium 2.
{ECO:0000250|UniProtKB:Q64537}.
METAL 152 152 Calcium 2.
{ECO:0000250|UniProtKB:Q64537}.
METAL 154 154 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q64537}.
METAL 156 156 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q64537}.
METAL 161 161 Calcium 2.
{ECO:0000250|UniProtKB:Q64537}.
METAL 180 180 Calcium 3.
{ECO:0000250|UniProtKB:Q64537}.
METAL 182 182 Calcium 3.
{ECO:0000250|UniProtKB:Q64537}.
METAL 184 184 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q64537}.
METAL 186 186 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q64537}.
METAL 191 191 Calcium 3.
{ECO:0000250|UniProtKB:Q64537}.
METAL 223 223 Calcium 4.
{ECO:0000250|UniProtKB:Q64537}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P04632}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:P04632}.
MOD_RES 177 177 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04632}.
SEQUENCE 266 AA; 28239 MW; 1D7FE31989F70B03 CRC64;
MFLVNSFLKG GGGGGGGGGL GGGLGNVLGG LISGAGGGGG GGGGGGGGGA GGGGTAMRIL
GGVISAISEA AAQYNPEPPP PRTHYSNIEA NESEEVRQFR RLFAQLAGDD MEVSATELMN
ILNKVVTRHP DLKTDGFGLD TCRSMVAVMD SDTTGKLGFE EFKYLWNNIK KWQAIYKQFD
VDRSGTICSR ELPGAFEAAG FHLNEHLYNM IIRRYSDEAG NMDFDNFISC LVRLDAMFRA
FKSLDKDGTG QIQVNIQEWL QLTMYS


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