ICAL_RABIT
ID ICAL_RABIT Reviewed; 718 AA.
AC P08855;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Calpastatin;
DE AltName: Full=Calpain inhibitor;
DE Contains:
DE RecName: Full=Erythrocyte calpastatin;
GN Name=CAST;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=3035539; DOI=10.1073/pnas.84.11.3590;
RA Emori Y., Kawasaki H., Imajoh S., Imahori K., Suzuki K.;
RT "Endogenous inhibitor for calcium-dependent cysteine protease contains four
RT internal repeats that could be responsible for its multiple reactive
RT sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3590-3594(1987).
RN [2]
RP PROTEIN SEQUENCE OF 290-718.
RC TISSUE=Erythrocyte;
RX PubMed=3039985; DOI=10.1016/0006-291x(87)90575-4;
RA Imajoh S., Kawasaki H., Emori Y., Suzuki K.;
RT "Calcium-activated neutral protease inhibitor from rabbit erythrocytes
RT lacks the N-terminal region of the liver inhibitor but retains three
RT inhibitory units.";
RL Biochem. Biophys. Res. Commun. 146:630-637(1987).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Erythrocyte;
RX PubMed=3034666; DOI=10.1016/0014-5793(87)80161-8;
RA Imajoh S., Kawasaki H., Emori Y., Ishiura S., Minami Y., Sugita H.,
RA Imahori K., Suzuki K.;
RT "A fragment of an endogenous inhibitor produced in Escherichia coli for
RT calcium-activated neutral protease (CANP) retains an inhibitory activity.";
RL FEBS Lett. 215:274-278(1987).
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 -!- MISCELLANEOUS: In erythrocytes the protein lacks the N-terminal region
CC of the liver inhibitor but retains three inhibitory units.
CC -!- SIMILARITY: Belongs to the protease inhibitor I27 (calpastatin) family.
CC {ECO:0000305}.
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DR EMBL; M16476; AAA31186.1; -; mRNA.
DR PIR; A26615; A26615.
DR RefSeq; NP_001075739.1; NM_001082270.1.
DR AlphaFoldDB; P08855; -.
DR STRING; 9986.ENSOCUP00000006752; -.
DR MEROPS; I27.001; -.
DR MEROPS; I27.002; -.
DR MEROPS; I27.003; -.
DR MEROPS; I27.004; -.
DR PRIDE; P08855; -.
DR GeneID; 100009098; -.
DR KEGG; ocu:100009098; -.
DR CTD; 831; -.
DR eggNOG; ENOG502RHIZ; Eukaryota.
DR InParanoid; P08855; -.
DR OrthoDB; 203890at2759; -.
DR Proteomes; UP000001811; 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 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..718
FT /note="Calpastatin"
FT /id="PRO_0000004168"
FT CHAIN 290..718
FT /note="Erythrocyte calpastatin"
FT /id="PRO_0000004169"
FT REPEAT 170..222
FT /note="Inhibitory domain 1"
FT REPEAT 307..359
FT /note="Inhibitory domain 2"
FT REPEAT 450..503
FT /note="Inhibitory domain 3"
FT REPEAT 587..640
FT /note="Inhibitory domain 4"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..185
FT /note="Polar 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 320..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 86
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 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51125"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 290
FT /note="Blocked amino end (Ser); in form erythrocyte"
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 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20810"
FT MOD_RES 581
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 718 AA; 76965 MW; B57F2B85D386A6BA CRC64;
MNPAEAKAVP ISKEMEGPHP HSKKRHRRQD AKTEPEKSQS TKPPVDHEKK AQEGKPKEHT
KPKSTHKHAS DGEGKHGRNE KTASRSKEPV TPAKRTEPET KPQDTKPAGG KSVAAGTTAA
PGKAGDPKKE KKSLPAAALA EPKPDEPSGK SGMDAALDDL IDTLGEPSET QEDSTAYTGP
EISDPMSSTY IEELGKREVT IPPKYRELLE KKTGVAGPPP DSVTPLGPDD AIDALSSDFT
CSSPVASGKE AGKEAAKSAG EVLEAESAKV MRAAAPPQEK KRKVEEDAMS DQALEALSAS
LGTRMAEPEL DLSSIKEVAE AKRKEEKVEK CGEDDETVPA EYRLKPATDK DGKPLLPEPA
EKPKPRSESE LIDELSKDFS QAKSNEKQPK PTGKTEESKA AVPAPVAEAV PRTSMCSIQP
VPPKPASLQK STVPDDAVEA LAGSLGRKEA DPEEGKPVAD KIKEKSKEEE REKLGEKEET
IPPDYRLEEA KDKDGKPLLP SEPTAQLPAL SEDLLLDALS EDFSGPSSAS SLKFDDAMLS
AAVSEVVSQS PASITRATAP PPDTRPSNKE LDDALDKLSD SLGQRQPDPD ENKPMEDKVK
ERAKKEHKDK LGERDDTIPP EYRHLLDQGE QDKPEKPPTK KSKEIKKPAG DQDPIDALSG
DLDSCPPAAE TSQATEKDKS KTTTASSSKA AKHGDKAKDS AQTTEETSKP KANEKNAS
