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Protein

Calpastatin

Gene

CAST

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.

GO - Molecular functioni

GO - Biological processi

  • protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Thiol protease inhibitor

Protein family/group databases

MEROPSiI27.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpastatin
Alternative name(s):
Calpain inhibitor
Gene namesi
Name:CAST
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713CalpastatinPRO_0000147634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki32 – 32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei50 – 501N6-acetyllysineBy similarity
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei134 – 1341PhosphoserineBy similarity
Modified residuei136 – 1361PhosphothreonineBy similarity
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei367 – 3671PhosphoserineBy similarity
Modified residuei369 – 3691PhosphoserineBy similarity
Modified residuei376 – 3761PhosphoserineBy similarity
Modified residuei441 – 4411PhosphoserineBy similarity
Modified residuei517 – 5171PhosphoserineBy similarity
Modified residuei528 – 5281PhosphoserineBy similarity
Modified residuei575 – 5751PhosphoserineBy similarity
Modified residuei577 – 5771PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP12675.

Expressioni

Gene expression databases

GenevisibleiP12675. SS.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015070.

Structurei

Secondary structure

1
713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi232 – 2398Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NX0X-ray2.30C/D231-241[»]
1NX1X-ray2.00C/D231-241[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati171 – 22353Inhibitory domain 1Add
BLAST
Repeati307 – 35953Inhibitory domain 2Add
BLAST
Repeati447 – 50054Inhibitory domain 3Add
BLAST
Repeati583 – 63654Inhibitory domain 4Add
BLAST

Domaini

Each of the four flexible inhibitory domains can inhibit one calcium-bound calpain molecule by occupying both sides of the active site.By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IFF9. Eukaryota.
ENOG4111YF0. LUCA.
HOVERGENiHBG000183.
InParanoidiP12675.

Family and domain databases

InterProiIPR026998. Calpastatin.
IPR001259. Prot_inh_calpain.
[Graphical view]
PANTHERiPTHR10077. PTHR10077. 1 hit.
PfamiPF00748. Calpain_inhib. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPTETKAIP VSKQLEGPHS PNKKRHKKQA VKTEPEKKSQ STKPSVVHEK
60 70 80 90 100
KTQEVKPKEH PEPKSLPTHS ADAGSKRAHK EKAVSRSNEQ PTSEKSTKPK
110 120 130 140 150
AKPQDPTPSD GKLSVTGVSA ASGKPAETKK DDKSLTSSVP AESKSSKPSG
160 170 180 190 200
KSDMDAALDD LIDTLGGPEE TEEDNTTYTG PEVLDPMSST YIEELGKREV
210 220 230 240 250
TLPPKYRELL DKKEGIPVPP PDTSKPLGPD DAIDALSLDL TCSSPTADGK
260 270 280 290 300
KTEKEKSTGE VLKAQSVGVI KSAAAPPHEK KRRVEEDTMS DQALEALSAS
310 320 330 340 350
LGSRKSEPEL DLSSIKEIDE AKAKEEKLKK CGEDDETVPP EYRLKPAMDK
360 370 380 390 400
DGKPLLPEAE EKPKPLSESE LIDELSEDFD QSKRKEKQSK PTEKTKESQA
410 420 430 440 450
TAPTPVGEAV SRTSLCCVQS APPKPATGMV PDDAVEALAG SLGKKEADPE
460 470 480 490 500
DGKPVEDKVK EKAKEEDREK LGEKEETIPP DYRLEEVKDK DGKTLPHKDP
510 520 530 540 550
KEPVLPLSED FVLDALSQDF AGPPAASSLF EDAKLSAAVS EVVSQTSAPT
560 570 580 590 600
THSAGPPPDT VSDDKKLDDA LDQLSDSLGQ RQPDPDENKP IEDKVKEKAE
610 620 630 640 650
AEHRDKLGER DDTIPPEYRH LLDKDEEGKS TKPPTKKPEA PKKPEAAQDP
660 670 680 690 700
IDALSGDFDR CPSTTETSEN TTKDKDKKTA SKSKAPKNGG KAKDSTKAKE
710
ETSKQKSDGK STS
Length:713
Mass (Da):77,124
Last modified:October 1, 1989 - v1
Checksum:iABD4E8F119CE97B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti328 – 3281L → V in AAA31009 (PubMed:3780962).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20160 mRNA. Translation: AAA31012.1.
AY372988 mRNA. Translation: AAR27961.1.
M27969 mRNA. Translation: AAA31009.1.
PIRiA24627.
A28706.
UniGeneiSsc.31703.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20160 mRNA. Translation: AAA31012.1.
AY372988 mRNA. Translation: AAR27961.1.
M27969 mRNA. Translation: AAA31009.1.
PIRiA24627.
A28706.
UniGeneiSsc.31703.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NX0X-ray2.30C/D231-241[»]
1NX1X-ray2.00C/D231-241[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015070.

Protein family/group databases

MEROPSiI27.001.

Proteomic databases

PaxDbiP12675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IFF9. Eukaryota.
ENOG4111YF0. LUCA.
HOVERGENiHBG000183.
InParanoidiP12675.

Gene expression databases

GenevisibleiP12675. SS.

Family and domain databases

InterProiIPR026998. Calpastatin.
IPR001259. Prot_inh_calpain.
[Graphical view]
PANTHERiPTHR10077. PTHR10077. 1 hit.
PfamiPF00748. Calpain_inhib. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis."
    Takano E., Maki M., Mori H., Hatanaka M., Marti T., Titani K., Kannagi R., Ooi T., Murachi T.
    Biochemistry 27:1964-1972(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Involvement of calpain-calpastatin in cigarette smoke-induced inhibition of lung endothelial nitric oxide synthase."
    Cui Z., Han Z., Li Z., Hu H., Patel J.M., Antony V., Block E.R., Su Y.
    Am. J. Respir. Cell Mol. Biol. 33:513-520(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Evidence for the repetitive domain structure of pig calpastatin as demonstrated by cloning of complementary DNA."
    Takano E., Maki M., Hatanaka M., Mori H., Zenita K., Sakihama T., Kannagi R., Marti T., Titani K., Murachi T.
    FEBS Lett. 208:199-202(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 304-554.

Entry informationi

Entry nameiICAL_PIG
AccessioniPrimary (citable) accession number: P12675
Secondary accession number(s): Q3ZTQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 17, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.