ICAL_CHLAE
ID ICAL_CHLAE Reviewed; 283 AA.
AC P49342;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Calpastatin;
DE AltName: Full=Calpain inhibitor;
DE Flags: Fragment;
GN Name=CAST;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1569094; DOI=10.1016/s0021-9258(18)42463-5;
RA Lee W.J., Ma H., Takano E., Yang H.Q., Hatanaka M., Maki M.;
RT "Molecular diversity in amino-terminal domains of human calpastatin by exon
RT skipping.";
RL J. Biol. Chem. 267:8437-8442(1992).
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; M86248; AAA52753.1; -; mRNA.
DR AlphaFoldDB; P49342; -.
DR BMRB; P49342; -.
DR IntAct; P49342; 1.
DR EvolutionaryTrace; P49342; -.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR026998; Calpastatin.
DR InterPro; IPR001259; Prot_inh_calpain.
DR PANTHER; PTHR10077; PTHR10077; 1.
DR Pfam; PF00748; Calpain_inhib; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Phosphoprotein; Protease inhibitor; Repeat;
KW Thiol protease inhibitor; Ubl conjugation.
FT CHAIN 1..>283
FT /note="Calpastatin"
FT /id="PRO_0000147631"
FT REPEAT 170..222
FT /note="Inhibitory domain 1"
FT REGION 1..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..283
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 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 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27321"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 243
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 NON_TER 283
SQ SEQUENCE 283 AA; 30170 MW; 02743390B5D6F0F8 CRC64;
MNPTETKAIP VSQQMEGPHL PNKKKHKKQA VKTEPEKKSQ STKLSVVHEK KSQEGKPKEH
TEQKSLPKPA SDTGSKDAHN KKAVSRSAEQ QPSEKSTEPK TEPQDMVSAG GESVAGVAAT
SGKPGDKKKE KKSLTPAVPV ESKPDKPSGK SGMDAALDDL IDTLGGPEEI EEENTTYTGP
EVSDPMSSTY IEELGKREVT IPPKYRELLA KNEGITGPPA DSSKPVGPDD AIDALSSDFT
CGSPTAAGKK TEKEESTEVL KAQSAGTVRS AAPPQEKKRK VEK
