ICAL_BOVIN
ID ICAL_BOVIN Reviewed; 705 AA.
AC P20811;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Calpastatin;
DE AltName: Full=Calpain inhibitor;
GN Name=CAST;
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].
RC TISSUE=Longissimus muscle;
RX PubMed=8181976; DOI=10.2527/1994.723606x;
RA Killefer J., Koohmaraie M.;
RT "Bovine skeletal muscle calpastatin: cloning, sequence analysis, and
RT steady-state mRNA expression.";
RL J. Anim. Sci. 72:606-614(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-15 AND 33-45.
RC TISSUE=Heart;
RX PubMed=2804140; DOI=10.1016/0167-4838(89)90032-0;
RA Mellgren R.L., Lane R.D., Mericle M.T.;
RT "The binding of large calpastatin to biologic membranes is mediated in part
RT by interaction of an amino terminal region with acidic phospholipids.";
RL Biochim. Biophys. Acta 999:71-77(1989).
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; L14450; AAA19643.1; -; mRNA.
DR AlphaFoldDB; P20811; -.
DR SMR; P20811; -.
DR MEROPS; I27.001; -.
DR MEROPS; I27.002; -.
DR MEROPS; I27.003; -.
DR MEROPS; I27.004; -.
DR PeptideAtlas; P20811; -.
DR PRIDE; P20811; -.
DR eggNOG; ENOG502RHIZ; Eukaryota.
DR InParanoid; P20811; -.
DR Proteomes; UP000009136; Unplaced.
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 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 Acetylation; Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Repeat; Thiol protease inhibitor;
KW Ubl conjugation.
FT CHAIN 1..705
FT /note="Calpastatin"
FT /id="PRO_0000147630"
FT REPEAT 149..202
FT /note="Inhibitory domain 1"
FT REPEAT 292..344
FT /note="Inhibitory domain 2"
FT REPEAT 434..487
FT /note="Inhibitory domain 3"
FT REPEAT 571..624
FT /note="Inhibitory domain 4"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27321"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT CONFLICT 2
FT /note="N -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 9..15
FT /note="VKTEPEK -> IPGSKQL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 705 AA; 75843 MW; A6C816E052816794 CRC64;
MNPTEAKAVK TEPEKKPQSS KPSVVHEKKT QEVKPKEHTE PKSLPKHSSD TGVKHAPKEK
AVSKSSEQPP SEKSTKPKTK SQDKISGGGK STVPAAAAAA SAEPADKNKE NKLLTSAVPA
ESKPSKPSGK SDMDTALDDL IDTLGEPEEM KEDNTTYTGP EVSDPMSSTY IEELGKREST
PPPKYKELLN KEEGIAGPPP DSLKPLGPND AIDALSSDFT CSSLQLTTCS PTADGKETEK
EKSTEEALKA QSAGVIRSAA PPKEKRRKVE EDTMTEQALQ ALSASLGTRK PEPELDPSSI
REVDEAKAKE EKVKKCGEDE ETVPSEYRLK PATDKDGKPL LPEAEEKPKP LSESELIDEL
SEDFDQSKPT EKQSKPTEKT EASPAAAPYP VAEDVPRTSM CSLQSAPPTA APAKGMVPDD
AVEALAGSLP KKEADPEDGK PVEDKVKEKA KEEDRENFGE KEETIPPDYR LEEAKDKDGK
PLLPKEVKEP LPPLSEDVLL DALSKDFTVP SDTSSPQFED AKLSAVVSEV VSQTPAPTTQ
AAGPPPDCAR DNKELDDALD QLSDTLGQRQ PDPDENKPVE DKVKEKAKAE HRDKLGERDD
TIPPKYQHLL DDNKEGTPGK PKDQRAQGIR NCGEKPAGAQ DPIDALSGDF DSCPSTTETS
TDTPKDKDKK PASVPKHLGN GGKAKDSTKA KEETSKPKAD GKSTS
