CPNS1_RABIT
ID CPNS1_RABIT Reviewed; 266 AA.
AC P06813;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3013892; DOI=10.1016/s0021-9258(18)67680-x;
RA Emori Y., Kawasaki H., Imajoh S., Kawashima S., Suzuki K.;
RT "Isolation and sequence analysis of cDNA clones for the small subunit of
RT rabbit calcium-dependent protease.";
RL J. Biol. Chem. 261:9472-9476(1986).
RN [2]
RP CALCIUM-BINDING, AND DOMAIN.
RX PubMed=3038855; DOI=10.1093/oxfordjournals.jbchem.a121956;
RA Minami Y., Emori Y., Kawasaki H., Suzuki K.;
RT "E-F hand structure-domain of calcium-activated neutral protease (CANP) can
RT bind Ca2+ ions.";
RL J. Biochem. 101:889-895(1987).
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 -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to
CC the plasma membrane upon calcium binding. Allows the formation of the
CC homodimer and also appears to mediate the contact between the large
CC catalytic subunit and small regulatory subunit for the formation of the
CC 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. {ECO:0000250}.
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. {ECO:0000269|PubMed:3038855}.
CC -!- PTM: The N-terminus is blocked.
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DR EMBL; M13364; AAA81565.1; -; mRNA.
DR PIR; A24816; CIRBL.
DR RefSeq; NP_001075733.1; NM_001082264.1.
DR AlphaFoldDB; P06813; -.
DR SMR; P06813; -.
DR STRING; 9986.ENSOCUP00000011273; -.
DR PRIDE; P06813; -.
DR Ensembl; ENSOCUT00000013092; ENSOCUP00000011273; ENSOCUG00000013093.
DR GeneID; 100009090; -.
DR KEGG; ocu:100009090; -.
DR CTD; 826; -.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000155478; -.
DR HOGENOM; CLU_051357_2_0_1; -.
DR InParanoid; P06813; -.
DR OMA; MCRAFQT; -.
DR OrthoDB; 1330600at2759; -.
DR TreeFam; TF314682; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000013093; Expressed in aorta and 15 other tissues.
DR GO; GO:0110158; C:calpain complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IEA:Ensembl.
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 Acetylation; Calcium; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..266
FT /note="Calpain small subunit 1"
FT /id="PRO_0000073716"
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"
SQ 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
