ICAL_PIG
ID ICAL_PIG Reviewed; 713 AA.
AC P12675; Q3ZTQ5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Calpastatin;
DE AltName: Full=Calpain inhibitor;
GN Name=CAST;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=2837276; DOI=10.1021/bi00406a024;
RA Takano E., Maki M., Mori H., Hatanaka M., Marti T., Titani K., Kannagi R.,
RA Ooi T., Murachi T.;
RT "Pig heart calpastatin: identification of repetitive domain structures and
RT anomalous behavior in polyacrylamide gel electrophoresis.";
RL Biochemistry 27:1964-1972(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16100081; DOI=10.1165/rcmb.2005-0046oc;
RA Cui Z., Han Z., Li Z., Hu H., Patel J.M., Antony V., Block E.R., Su Y.;
RT "Involvement of calpain-calpastatin in cigarette smoke-induced inhibition
RT of lung endothelial nitric oxide synthase.";
RL Am. J. Respir. Cell Mol. Biol. 33:513-520(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 304-554.
RX PubMed=3780962; DOI=10.1016/0014-5793(86)81017-1;
RA Takano E., Maki M., Hatanaka M., Mori H., Zenita K., Sakihama T.,
RA Kannagi R., Marti T., Titani K., Murachi T.;
RT "Evidence for the repetitive domain structure of pig calpastatin as
RT demonstrated by cloning of complementary DNA.";
RL FEBS Lett. 208:199-202(1986).
CC -!- FUNCTION: Specific inhibition of calpain (calcium-dependent cysteine
CC protease). Plays a key role in postmortem tenderization of meat and
CC have been proposed to be involved in muscle protein degradation in
CC living tissue.
CC -!- DOMAIN: Each of the four flexible inhibitory domains can inhibit one
CC calcium-bound calpain molecule by occupying both sides of the active
CC site. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I27 (calpastatin) family.
CC {ECO:0000305}.
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DR EMBL; M20160; AAA31012.1; -; mRNA.
DR EMBL; AY372988; AAR27961.1; -; mRNA.
DR EMBL; M27969; AAA31009.1; -; mRNA.
DR PIR; A24627; A24627.
DR PIR; A28706; A28706.
DR PDB; 1NX0; X-ray; 2.30 A; C/D=231-241.
DR PDB; 1NX1; X-ray; 2.00 A; C/D=231-241.
DR PDBsum; 1NX0; -.
DR PDBsum; 1NX1; -.
DR AlphaFoldDB; P12675; -.
DR SMR; P12675; -.
DR STRING; 9823.ENSSSCP00000015070; -.
DR MEROPS; I27.001; -.
DR PaxDb; P12675; -.
DR PeptideAtlas; P12675; -.
DR PRIDE; P12675; -.
DR Ensembl; ENSSSCT00070019868; ENSSSCP00070016515; ENSSSCG00070009854.
DR eggNOG; ENOG502RHIZ; Eukaryota.
DR InParanoid; P12675; -.
DR Reactome; R-SSC-1474228; Degradation of the extracellular matrix.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 2.
DR Genevisible; P12675; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010859; F:calcium-dependent cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0097340; P:inhibition of cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR InterPro; IPR026998; Calpastatin.
DR InterPro; IPR001259; Prot_inh_calpain.
DR PANTHER; PTHR10077; PTHR10077; 1.
DR Pfam; PF00748; Calpain_inhib; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Repeat; Thiol protease inhibitor;
KW Ubl conjugation.
FT CHAIN 1..713
FT /note="Calpastatin"
FT /id="PRO_0000147634"
FT REPEAT 171..223
FT /note="Inhibitory domain 1"
FT REPEAT 307..359
FT /note="Inhibitory domain 2"
FT REPEAT 447..500
FT /note="Inhibitory domain 3"
FT REPEAT 583..636
FT /note="Inhibitory domain 4"
FT REGION 1..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27321"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT CONFLICT 328
FT /note="L -> V (in Ref. 3; AAA31009)"
FT /evidence="ECO:0000305"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:1NX1"
SQ SEQUENCE 713 AA; 77124 MW; ABD4E8F119CE97B5 CRC64;
MNPTETKAIP VSKQLEGPHS PNKKRHKKQA VKTEPEKKSQ STKPSVVHEK KTQEVKPKEH
PEPKSLPTHS ADAGSKRAHK EKAVSRSNEQ PTSEKSTKPK AKPQDPTPSD GKLSVTGVSA
ASGKPAETKK DDKSLTSSVP AESKSSKPSG KSDMDAALDD LIDTLGGPEE TEEDNTTYTG
PEVLDPMSST YIEELGKREV TLPPKYRELL DKKEGIPVPP PDTSKPLGPD DAIDALSLDL
TCSSPTADGK KTEKEKSTGE VLKAQSVGVI KSAAAPPHEK KRRVEEDTMS DQALEALSAS
LGSRKSEPEL DLSSIKEIDE AKAKEEKLKK CGEDDETVPP EYRLKPAMDK DGKPLLPEAE
EKPKPLSESE LIDELSEDFD QSKRKEKQSK PTEKTKESQA TAPTPVGEAV SRTSLCCVQS
APPKPATGMV PDDAVEALAG SLGKKEADPE DGKPVEDKVK EKAKEEDREK LGEKEETIPP
DYRLEEVKDK DGKTLPHKDP KEPVLPLSED FVLDALSQDF AGPPAASSLF EDAKLSAAVS
EVVSQTSAPT THSAGPPPDT VSDDKKLDDA LDQLSDSLGQ RQPDPDENKP IEDKVKEKAE
AEHRDKLGER DDTIPPEYRH LLDKDEEGKS TKPPTKKPEA PKKPEAAQDP IDALSGDFDR
CPSTTETSEN TTKDKDKKTA SKSKAPKNGG KAKDSTKAKE ETSKQKSDGK STS
