ICAL_SHEEP
ID ICAL_SHEEP Reviewed; 723 AA.
AC Q95208;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Calpastatin;
DE AltName: Full=Calpain inhibitor;
GN Name=CAST;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Mainelli K., Sugimoto J., Fishkin A., Knezetic J.;
RT "Sequence analysis of ovine myocardial calpastatin mRNA transcripts.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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; U66320; AAB07483.1; -; mRNA.
DR RefSeq; NP_001009788.1; NM_001009788.1.
DR AlphaFoldDB; Q95208; -.
DR SMR; Q95208; -.
DR MEROPS; I27.001; -.
DR MEROPS; I27.002; -.
DR MEROPS; I27.003; -.
DR MEROPS; I27.004; -.
DR GeneID; 443364; -.
DR KEGG; oas:443364; -.
DR CTD; 831; -.
DR OrthoDB; 203890at2759; -.
DR Proteomes; UP000002356; Unplaced.
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; 4.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Phosphoprotein; Protease inhibitor;
KW Reference proteome; Repeat; Thiol protease inhibitor; Ubl conjugation.
FT CHAIN 1..723
FT /note="Calpastatin"
FT /id="PRO_0000147636"
FT REPEAT 171..224
FT /note="Inhibitory domain 1"
FT REPEAT 307..359
FT /note="Inhibitory domain 2"
FT REPEAT 449..502
FT /note="Inhibitory domain 3"
FT REPEAT 586..642
FT /note="Inhibitory domain 4"
FT REGION 1..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
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 445..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..723
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 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27321"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 245
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 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 580
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"
SQ SEQUENCE 723 AA; 78999 MW; 251EA851D50B8F00 CRC64;
MNPTEAKAIP GSKQLEGPHS PNKKRHKKQA VKTEPEKKSQ STKPSVVHEK KTQEVKPKEH
TEPKSQPKHP SDTRSKHAPK EKAVSKSSEQ PPSEKSTKPK TKSQDEISGG GKSAVPAVAA
AASAEPADKN KESKLLTSAV PVESKPSKPS AKSDMDTALD DLIDTLGEPE ETKEDTTTYT
GPEVSDPMSS TYIEELGKRE VTLPPKYREL LNKEEGIAGP PPDSSKPLGP NDAIDALSSD
FTCSSPTADA KKTEKEKSTE EALKAQSAGV IRSAAPPKEK RRKVEEDTMT EQALEALSAS
LGTRKPRPEL DPSSIKEVDE AKAKEEKVKK CGEDEERVPS EYRLKPATDK DGKPLLPEAE
EKPKPLSESE LIDELSEDFD RSKCKEKQSK PTEKNRGIPG RCPRACARGC ASDLHVFCAV
SSTHSSSSEG MVPDDAVEAL AGSLGKKEAD PEDGKPVEDK VKEKAKEEDR EKLGEREETI
PPDYRLEEAK DKDGKPLPPK EVKEPLPPLS EDFLLDALSK DFTVPSDTSS PQFEDAKLSV
VVSEVVSQTP APTTQAAGPP RDSARDNKEL DDALDQLSDS LGQRQPDPDE HKPVEDKVKE
KAKAEHRDKL GERDDTIPPK YQHLLDDNKE GTPGKPKRSE SPRHQRSPRH QRNLQVPRTP
LTPSQGTWTA VPQLQKPQQT QQRTKTRSLL PSDKAPRNGG KAKDSTKAKE ETSKPKADGK
STS
