CPNS1_BOVIN
ID CPNS1_BOVIN Reviewed; 263 AA.
AC P13135; A1YVU9; Q1JQC3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2551902; DOI=10.1016/s0021-9258(18)71512-3;
RA McClelland P., Lash J.A., Hathaway D.R.;
RT "Identification of major autolytic cleavage sites in the regulatory subunit
RT of vascular calpain II. A comparison of partial amino-terminal sequences to
RT deduced sequence from complementary DNA.";
RL J. Biol. Chem. 264:17428-17431(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Juszczuk-Kubiak E., Rosochacki S., Wycinska K.;
RT "A novel RFLP/MboII polymorphism of the small subunit bovine calcium-
RT activated protease (CAPNS1) and its association with carcass and meat
RT quality traits of Polish-Black-and-White cattle.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 {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. {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.
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DR EMBL; J05065; AAA30422.1; -; mRNA.
DR EMBL; EF139087; ABL75413.1; -; Genomic_DNA.
DR EMBL; BC116060; AAI16061.1; -; mRNA.
DR PIR; A34466; A34466.
DR RefSeq; NP_776686.1; NM_174261.1.
DR AlphaFoldDB; P13135; -.
DR SMR; P13135; -.
DR CORUM; P13135; -.
DR STRING; 9913.ENSBTAP00000019803; -.
DR PaxDb; P13135; -.
DR PeptideAtlas; P13135; -.
DR PRIDE; P13135; -.
DR Ensembl; ENSBTAT00000019803; ENSBTAP00000019803; ENSBTAG00000014872.
DR GeneID; 281664; -.
DR KEGG; bta:281664; -.
DR CTD; 826; -.
DR VEuPathDB; HostDB:ENSBTAG00000014872; -.
DR VGNC; VGNC:52184; CAPNS1.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000155478; -.
DR HOGENOM; CLU_051357_2_0_1; -.
DR InParanoid; P13135; -.
DR OrthoDB; 1330600at2759; -.
DR TreeFam; TF314682; -.
DR BRENDA; 3.4.22.B24; 908.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000014872; Expressed in spermatocyte and 105 other tissues.
DR ExpressionAtlas; P13135; baseline and differential.
DR GO; GO:0110158; C:calpain complex; IBA:GO_Central.
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; ISS:AgBase.
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 2: Evidence at transcript level;
KW Acetylation; Calcium; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..263
FT /note="Calpain small subunit 1"
FT /id="PRO_0000073712"
FT DOMAIN 91..125
FT /note="EF-hand 1; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 134..167
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 164..199
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 200..228
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT DOMAIN 229..263
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
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 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q64537"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
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 153
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 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 181
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 183
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 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 220
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 174
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04632"
SQ SEQUENCE 263 AA; 27931 MW; 9427925D5284CE1A CRC64;
MFLVNSFLKG GGGGGGGGGL GGGLGNVLGG LISGAGGGGG GGGGGGGGGG GTAMRILGGV
ISAISEAAAQ YNPEPVPPRT HYSNIEANES EEVRQFRRLF AQLAGDDMEV SATELMNILN
KVVTRHPDLK TDGFGIDTCR SMVAVMDSDT TGKLGFEEFK YLWNNIKKWQ AVYKQFDVDR
SGTIGSSELP GAFEAAGFRL NEHLYNMIIR RYSDEGGNMD FDNFISCLVR LDAMFRAFKS
LDKDGTGQIQ VNIQEWLQLT MYS
