P27321 (ICAL_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calpastatin

Alternative name(s):
Calpain inhibitor

Gene names

Name:

Cast

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	713 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Domain	Each of the four flexible inhibitory domains can inhibit one calcium-bound calpain molecule by occupying both sides of the active site. Ref.9
Sequence similarities	Belongs to the protease inhibitor I27 (calpastatin) family. [View classification]
Sequence caution	The sequence AAK29411.1 differs from that shown. Reason: Erroneous initiation. The sequence AAK29412.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA40053.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA40053.1 differs from that shown. Reason: Frameshift at positions 640 and 647. The sequence CAA73915.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA73916.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA73917.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Protease inhibitor Thiol protease inhibitor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	cysteine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P27321-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P27321-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     98-135: Missing.

Isoform 3 (identifier: P27321-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     166-188: Missing.

Isoform 4 (identifier: P27321-4)

The sequence of this isoform differs from the canonical sequence as follows:
     67-79: Missing.
     98-135: Missing.

Isoform 5 (identifier: P27321-5)

The sequence of this isoform differs from the canonical sequence as follows:
     98-135: Missing.
     166-188: Missing.

Isoform 6 (identifier: P27321-6)

The sequence of this isoform differs from the canonical sequence as follows:
     67-79: Missing.
     98-135: Missing.
     166-188: Missing.

Isoform 7 (identifier: P27321-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-177: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 713

713

Calpastatin

PRO_0000147635

Regions

Repeat

208 – 260

53

Inhibitory domain 1

Repeat

341 – 393

53

Inhibitory domain 2

Repeat

451 – 504

54

Inhibitory domain 3

Repeat

588 – 641

54

Inhibitory domain 4

Amino acid modifications

Modified residue

11

1

Phosphoserine By similarity

Modified residue

122

1

Phosphoserine By similarity

Modified residue

171

1

Phosphoserine By similarity

Modified residue

260

1

Phosphoserine Ref.7

Modified residue

281

1

Phosphoserine Ref.7

Modified residue

401

1

Phosphoserine By similarity

Modified residue

403

1

Phosphoserine By similarity

Modified residue

410

1

Phosphoserine By similarity

Modified residue

580

1

Phosphoserine By similarity

Modified residue

582

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 177

177

Missing in isoform 7.

VSP_026971

Alternative sequence

67 – 79

13

Missing in isoform 4 and isoform 6.

VSP_000753

Alternative sequence

98 – 135

38

Missing in isoform 2, isoform 4, isoform 5 and isoform 6.

VSP_000754

Alternative sequence

166 – 188

23

Missing in isoform 3, isoform 5 and isoform 6.

VSP_026972

Experimental info

Mutagenesis

613

1

G → A: 2.9-fold increase in the IC(50). Ref.9

Mutagenesis

613

1

G → FG: Turns CAST from an inhibitor into a substrate. Ref.9

Sequence conflict

161

1

K → E in CAA40053. Ref.1

Sequence conflict

161

1

K → E in AAK29411. Ref.5

Sequence conflict

209

1

N → S in CAA73917. Ref.4

Sequence conflict

314

1

K → E in AAK29412. Ref.5

Sequence conflict

463

1

V → G in ABA86879. Ref.1

Sequence conflict

463

1

V → G in ABA86880. Ref.1

Sequence conflict

463

1

V → G in ABA86881. Ref.1

Sequence conflict

463

1

V → G in ABA86882. Ref.1

Sequence conflict

463

1

V → G in ABA86883. Ref.1

Sequence conflict

463

1

V → G in ABA86884. Ref.1

Sequence conflict

463

1

V → G in ABB90254. Ref.1

Sequence conflict

463

1

V → G in CAA73916. Ref.4

Sequence conflict

481

1

T → A in CAA73917. Ref.4

Sequence conflict

518

1

D → G in CAA73917. Ref.4

Sequence conflict

611

1

K → R in CAA73915. Ref.4

Sequence conflict

646

1

L → P in AAH91239. Ref.2

Sequence conflict

646

1

L → P in CAA73915. Ref.4

Sequence conflict

646

1

L → P in CAA73917. Ref.4

Sequence conflict

646

1

L → P in AAK29411. Ref.5

Sequence conflict

646

1

L → P in AAK29412. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

713

Helix Strand Turn

Details...

Helix

195 – 199

5

Helix

236 – 238

3

Helix

241 – 247

7

Helix

271 – 274

4

Turn

275 – 277

3

Helix

573 – 581

9

Helix

616 – 618

3

Helix

621 – 627

7

Helix

652 – 659

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified July 24, 2007. Version 3. Checksum: 55505300F59A8DE3	FASTA	713	77,313
	10 20 30 40 50 60 MSRPGPKPAA SSRPRRGAAA SHTQEHVNEK NIGSSSKPAE KKGSDEVTAS SAATGTSPRM 70 80 90 100 110 120 STTGAKAVKI ESEKSQSSEP PVIHEKKPKG KPKEGSEPQT LPKHASDTGS KHAHKEKALS 130 140 150 160 170 180 RSNEQIVSEK SSESKTKFQD APSADGESVA GGVTVATASD KVVVKKKEKK SLTPTLPMES 190 200 210 220 230 240 TLNKLSDKSG VNAALDDLID TLGECEDTNK DDPPYTGPVV LDPMDSTYLE ALGIKEGTIP 250 260 270 280 290 300 PEYRKLLEKN EAITGPLPDS PKPMGIDHAI DALSSDFTCS SPTGKQTEKE KSTGESSKAQ 310 320 330 340 350 360 SAGVTRSAVP PQEKKRKVEE EVMNDQALQA LSDSLGTRQP DPQSHLRQAK QVKEAKAKEE 370 380 390 400 410 420 RQEKCGEDED TVPAEYRLKP AKDKDGKPLL PEPEETSKCL SESELIGELS ADFVQPTYQE 430 440 450 460 470 480 KPSMPAAKIK KGVVPDDAVE TLARSLGTRK EDPEDEKSLV DKVKEKAKEE DHEKLGEKEE 490 500 510 520 530 540 TIPPDYRLEI VKDKDGKPLL PKEAEEQLPP LSDDFLLDAL SQDFSSPANI LSLGFEDAKL 550 560 570 580 590 600 SAAVSETVSQ VPAPSNHTAA PPPGTERRDK ELDDALDELS DSLGQRQPDP DENKPLDDKV 610 620 630 640 650 660 KEKIKAEHSE KLGERDDTIP PEYRHLLDND GKDKPEKPLT KNTEKLGQDQ DPIDALSEDL 670 680 690 700 710 DSCPPTTETS QNTTKEKGKK TSSSKASKNE EKTKDSSKKT EEVPKPKVDE DAT
	Isoform 2 (B) [UniParc]. Checksum: D3514B481F47F5A1	FASTA	675	73,172
	10 20 30 40 50 60 MSRPGPKPAA SSRPRRGAAA SHTQEHVNEK NIGSSSKPAE KKGSDEVTAS SAATGTSPRM 70 80 90 100 110 120 STTGAKAVKI ESEKSQSSEP PVIHEKKPKG KPKEGSETKF QDAPSADGES VAGGVTVATA 130 140 150 160 170 180 SDKVVVKKKE KKSLTPTLPM ESTLNKLSDK SGVNAALDDL IDTLGECEDT NKDDPPYTGP 190 200 210 220 230 240 VVLDPMDSTY LEALGIKEGT IPPEYRKLLE KNEAITGPLP DSPKPMGIDH AIDALSSDFT 250 260 270 280 290 300 CSSPTGKQTE KEKSTGESSK AQSAGVTRSA VPPQEKKRKV EEEVMNDQAL QALSDSLGTR 310 320 330 340 350 360 QPDPQSHLRQ AKQVKEAKAK EERQEKCGED EDTVPAEYRL KPAKDKDGKP LLPEPEETSK 370 380 390 400 410 420 CLSESELIGE LSADFVQPTY QEKPSMPAAK IKKGVVPDDA VETLARSLGT RKEDPEDEKS 430 440 450 460 470 480 LVDKVKEKAK EEDHEKLGEK EETIPPDYRL EIVKDKDGKP LLPKEAEEQL PPLSDDFLLD 490 500 510 520 530 540 ALSQDFSSPA NILSLGFEDA KLSAAVSETV SQVPAPSNHT AAPPPGTERR DKELDDALDE 550 560 570 580 590 600 LSDSLGQRQP DPDENKPLDD KVKEKIKAEH SEKLGERDDT IPPEYRHLLD NDGKDKPEKP 610 620 630 640 650 660 LTKNTEKLGQ DQDPIDALSE DLDSCPPTTE TSQNTTKEKG KKTSSSKASK NEEKTKDSSK 670 KTEEVPKPKV DEDAT
	Isoform 3 (C) [UniParc]. Checksum: 5FB95F6D6FAE3487	FASTA	690	74,714
	10 20 30 40 50 60 MSRPGPKPAA SSRPRRGAAA SHTQEHVNEK NIGSSSKPAE KKGSDEVTAS SAATGTSPRM 70 80 90 100 110 120 STTGAKAVKI ESEKSQSSEP PVIHEKKPKG KPKEGSEPQT LPKHASDTGS KHAHKEKALS 130 140 150 160 170 180 RSNEQIVSEK SSESKTKFQD APSADGESVA GGVTVATASD KVVVKSGVNA ALDDLIDTLG 190 200 210 220 230 240 ECEDTNKDDP PYTGPVVLDP MDSTYLEALG IKEGTIPPEY RKLLEKNEAI TGPLPDSPKP 250 260 270 280 290 300 MGIDHAIDAL SSDFTCSSPT GKQTEKEKST GESSKAQSAG VTRSAVPPQE KKRKVEEEVM 310 320 330 340 350 360 NDQALQALSD SLGTRQPDPQ SHLRQAKQVK EAKAKEERQE KCGEDEDTVP AEYRLKPAKD 370 380 390 400 410 420 KDGKPLLPEP EETSKCLSES ELIGELSADF VQPTYQEKPS MPAAKIKKGV VPDDAVETLA 430 440 450 460 470 480 RSLGTRKEDP EDEKSLVDKV KEKAKEEDHE KLGEKEETIP PDYRLEIVKD KDGKPLLPKE 490 500 510 520 530 540 AEEQLPPLSD DFLLDALSQD FSSPANILSL GFEDAKLSAA VSETVSQVPA PSNHTAAPPP 550 560 570 580 590 600 GTERRDKELD DALDELSDSL GQRQPDPDEN KPLDDKVKEK IKAEHSEKLG ERDDTIPPEY 610 620 630 640 650 660 RHLLDNDGKD KPEKPLTKNT EKLGQDQDPI DALSEDLDSC PPTTETSQNT TKEKGKKTSS 670 680 690 SKASKNEEKT KDSSKKTEEV PKPKVDEDAT
	Isoform 4 [UniParc]. Checksum: 184C191B609C0CD3	FASTA	662	71,769
	10 20 30 40 50 60 MSRPGPKPAA SSRPRRGAAA SHTQEHVNEK NIGSSSKPAE KKGSDEVTAS SAATGTSPRM 70 80 90 100 110 120 STTGAKPPVI HEKKPKGKPK EGSETKFQDA PSADGESVAG GVTVATASDK VVVKKKEKKS 130 140 150 160 170 180 LTPTLPMEST LNKLSDKSGV NAALDDLIDT LGECEDTNKD DPPYTGPVVL DPMDSTYLEA 190 200 210 220 230 240 LGIKEGTIPP EYRKLLEKNE AITGPLPDSP KPMGIDHAID ALSSDFTCSS PTGKQTEKEK 250 260 270 280 290 300 STGESSKAQS AGVTRSAVPP QEKKRKVEEE VMNDQALQAL SDSLGTRQPD PQSHLRQAKQ 310 320 330 340 350 360 VKEAKAKEER QEKCGEDEDT VPAEYRLKPA KDKDGKPLLP EPEETSKCLS ESELIGELSA 370 380 390 400 410 420 DFVQPTYQEK PSMPAAKIKK GVVPDDAVET LARSLGTRKE DPEDEKSLVD KVKEKAKEED 430 440 450 460 470 480 HEKLGEKEET IPPDYRLEIV KDKDGKPLLP KEAEEQLPPL SDDFLLDALS QDFSSPANIL 490 500 510 520 530 540 SLGFEDAKLS AAVSETVSQV PAPSNHTAAP PPGTERRDKE LDDALDELSD SLGQRQPDPD 550 560 570 580 590 600 ENKPLDDKVK EKIKAEHSEK LGERDDTIPP EYRHLLDNDG KDKPEKPLTK NTEKLGQDQD 610 620 630 640 650 660 PIDALSEDLD SCPPTTETSQ NTTKEKGKKT SSSKASKNEE KTKDSSKKTE EVPKPKVDED AT
	Isoform 5 [UniParc]. Checksum: 26A465A95B697D11	FASTA	652	70,573
	10 20 30 40 50 60 MSRPGPKPAA SSRPRRGAAA SHTQEHVNEK NIGSSSKPAE KKGSDEVTAS SAATGTSPRM 70 80 90 100 110 120 STTGAKAVKI ESEKSQSSEP PVIHEKKPKG KPKEGSETKF QDAPSADGES VAGGVTVATA 130 140 150 160 170 180 SDKVVVKSGV NAALDDLIDT LGECEDTNKD DPPYTGPVVL DPMDSTYLEA LGIKEGTIPP 190 200 210 220 230 240 EYRKLLEKNE AITGPLPDSP KPMGIDHAID ALSSDFTCSS PTGKQTEKEK STGESSKAQS 250 260 270 280 290 300 AGVTRSAVPP QEKKRKVEEE VMNDQALQAL SDSLGTRQPD PQSHLRQAKQ VKEAKAKEER 310 320 330 340 350 360 QEKCGEDEDT VPAEYRLKPA KDKDGKPLLP EPEETSKCLS ESELIGELSA DFVQPTYQEK 370 380 390 400 410 420 PSMPAAKIKK GVVPDDAVET LARSLGTRKE DPEDEKSLVD KVKEKAKEED HEKLGEKEET 430 440 450 460 470 480 IPPDYRLEIV KDKDGKPLLP KEAEEQLPPL SDDFLLDALS QDFSSPANIL SLGFEDAKLS 490 500 510 520 530 540 AAVSETVSQV PAPSNHTAAP PPGTERRDKE LDDALDELSD SLGQRQPDPD ENKPLDDKVK 550 560 570 580 590 600 EKIKAEHSEK LGERDDTIPP EYRHLLDNDG KDKPEKPLTK NTEKLGQDQD PIDALSEDLD 610 620 630 640 650 SCPPTTETSQ NTTKEKGKKT SSSKASKNEE KTKDSSKKTE EVPKPKVDED AT
	Isoform 6 [UniParc]. Checksum: 777B3D8554E57AE7	FASTA	639	69,170
	10 20 30 40 50 60 MSRPGPKPAA SSRPRRGAAA SHTQEHVNEK NIGSSSKPAE KKGSDEVTAS SAATGTSPRM 70 80 90 100 110 120 STTGAKPPVI HEKKPKGKPK EGSETKFQDA PSADGESVAG GVTVATASDK VVVKSGVNAA 130 140 150 160 170 180 LDDLIDTLGE CEDTNKDDPP YTGPVVLDPM DSTYLEALGI KEGTIPPEYR KLLEKNEAIT 190 200 210 220 230 240 GPLPDSPKPM GIDHAIDALS SDFTCSSPTG KQTEKEKSTG ESSKAQSAGV TRSAVPPQEK 250 260 270 280 290 300 KRKVEEEVMN DQALQALSDS LGTRQPDPQS HLRQAKQVKE AKAKEERQEK CGEDEDTVPA 310 320 330 340 350 360 EYRLKPAKDK DGKPLLPEPE ETSKCLSESE LIGELSADFV QPTYQEKPSM PAAKIKKGVV 370 380 390 400 410 420 PDDAVETLAR SLGTRKEDPE DEKSLVDKVK EKAKEEDHEK LGEKEETIPP DYRLEIVKDK 430 440 450 460 470 480 DGKPLLPKEA EEQLPPLSDD FLLDALSQDF SSPANILSLG FEDAKLSAAV SETVSQVPAP 490 500 510 520 530 540 SNHTAAPPPG TERRDKELDD ALDELSDSLG QRQPDPDENK PLDDKVKEKI KAEHSEKLGE 550 560 570 580 590 600 RDDTIPPEYR HLLDNDGKDK PEKPLTKNTE KLGQDQDPID ALSEDLDSCP PTTETSQNTT 610 620 630 KEKGKKTSSS KASKNEEKTK DSSKKTEEVP KPKVDEDAT
	Isoform 7 [UniParc]. Checksum: D9BA9EB299CA6BCB	FASTA	536	58,859
	10 20 30 40 50 60 MESTLNKLSD KSGVNAALDD LIDTLGECED TNKDDPPYTG PVVLDPMDST YLEALGIKEG 70 80 90 100 110 120 TIPPEYRKLL EKNEAITGPL PDSPKPMGID HAIDALSSDF TCSSPTGKQT EKEKSTGESS 130 140 150 160 170 180 KAQSAGVTRS AVPPQEKKRK VEEEVMNDQA LQALSDSLGT RQPDPQSHLR QAKQVKEAKA 190 200 210 220 230 240 KEERQEKCGE DEDTVPAEYR LKPAKDKDGK PLLPEPEETS KCLSESELIG ELSADFVQPT 250 260 270 280 290 300 YQEKPSMPAA KIKKGVVPDD AVETLARSLG TRKEDPEDEK SLVDKVKEKA KEEDHEKLGE 310 320 330 340 350 360 KEETIPPDYR LEIVKDKDGK PLLPKEAEEQ LPPLSDDFLL DALSQDFSSP ANILSLGFED 370 380 390 400 410 420 AKLSAAVSET VSQVPAPSNH TAAPPPGTER RDKELDDALD ELSDSLGQRQ PDPDENKPLD 430 440 450 460 470 480 DKVKEKIKAE HSEKLGERDD TIPPEYRHLL DNDGKDKPEK PLTKNTEKLG QDQDPIDALS 490 500 510 520 530 EDLDSCPPTT ETSQNTTKEK GKKTSSSKAS KNEEKTKDSS KKTEEVPKPK VDEDAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple rat brain calpastatin forms are produced by distinct starting points and alternative splicing of the N-terminal exons." De Tullio R., Averna M., Stifanese R., Parr T., Bardsley R.G., Pontremoli S., Melloni E. Arch. Biochem. Biophys. 465:148-156(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7). Strain: Sprague-Dawley.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Liver.
[3]	"Rat calpastatin has diverged primary sequence from other mammalian calpastatins but retains functionally important sequences." Ishida S., Emori Y., Suzuki K. Biochim. Biophys. Acta 1088:436-438(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-713 (ISOFORM 1). Tissue: Liver.
[4]	"Rat brain contains multiple mRNAs for calpastatin." De Tullio R., Sparatore B., Salamino F., Melloni E., Pontremoli S. FEBS Lett. 422:113-117(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-713 (ISOFORMS 1; 2 AND 5). Strain: Sprague-Dawley. Tissue: Brain.
[5]	"Hypoxic induction of two rat cardiac calpastatin cDNAs." Risbood M.P., Lin H., Lee T. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-713 (ISOFORMS 1 AND 5). Strain: Sprague-Dawley. Tissue: Heart.
[6]	"Multiple forms of rat calpastatin cDNA in the coding region of functionally unknown amino-terminal domain." Lee W.J., Hatanaka M., Maki M. Biochim. Biophys. Acta 1129:251-253(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-188 (ISOFORMS 1; 2 AND 4). Strain: Fischer.
[7]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-281, MASS SPECTROMETRY. Tissue: Renal collecting duct.
[8]	"Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains." Moldoveanu T., Gehring K., Green D.R. Nature 456:404-408(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 193-278 IN COMPLEX WITH CAPN2 AND CAPNS1.
[9]	"Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin." Hanna R.A., Campbell R.L., Davies P.L. Nature 456:409-412(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 571-664 IN COMPLEX WITH CAPN2 AND CAPNS1, INHIBITORY DOMAINS, MUTAGENESIS OF GLY-613.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

DQ186624 mRNA. Translation: ABA86879.1.
DQ186625 mRNA. Translation: ABA86880.1.
DQ186626 mRNA. Translation: ABA86881.1.
DQ186627 mRNA. Translation: ABA86882.1.
DQ186628 mRNA. Translation: ABA86883.1.
DQ186629 mRNA. Translation: ABA86884.1.
DQ287975 mRNA. Translation: ABB90254.1.
BC091239 mRNA. Translation: AAH91239.1.
X56729 mRNA. Translation: CAA40053.1. Sequence problems.
Y13587 mRNA. Translation: CAA73915.1. Different initiation.
Y13588 mRNA. Translation: CAA73916.1. Different initiation.
Y13589 mRNA. Translation: CAA73917.1. Different initiation.
AF346597 mRNA. Translation: AAK29411.1. Different initiation.
AF346598 mRNA. Translation: AAK29412.1. Different initiation.
X62520 mRNA. Translation: CAA44386.1.

IPI

IPI00195926.
IPI00368326.
IPI00555292.
IPI00782263.
IPI00855218.
IPI00855234.
IPI00858353.

PIR

S15074.
S20611.

RefSeq

NP_001028887.1. NM_001033715.1.
NP_001028888.1. NM_001033716.1.
NP_445747.2. NM_053295.2.

UniGene

Rn.17481.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BOW	X-ray	2.40	C	571-664	[»]
3DF0	X-ray	2.95	C	193-278	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44338N.

MINT

MINT-4820577.

Protein family/group databases

MEROPS

I27.001.

PTM databases

PhosphoSite

P27321.

Proteomic databases

PaxDb

P27321.

PRIDE

P27321.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000062054; ENSRNOP00000058758; ENSRNOG00000010286.

GeneID

25403.

KEGG

rno:25403.

Organism-specific databases

CTD

831.

RGD

2278. Cast.

Phylogenomic databases

eggNOG

NOG25116.

GeneTree

ENSGT00390000002993.

HOVERGEN

HBG000183.

KO

K04281.

OrthoDB

EOG4H463V.

Gene expression databases

ArrayExpress

P27321.

Genevestigator

P27321.

GermOnline

ENSRNOG00000010286. Rattus norvegicus.

Family and domain databases

InterPro

IPR026998. Calpastatin.
IPR001259. Prot_inh_calpain.
[Graphical view]

PANTHER

PTHR10077. PTHR10077. 1 hit.

Pfam

PF00748. Calpain_inhib. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P27321.

NextBio

606501.

Entry information

Entry name

ICAL_RAT

Accession

Primary (citable) accession number: P27321
Secondary accession number(s): A5GXY4 , A5GXY5, A5GXY6, A5GXY7, A5GXY8, A5GXY9, A5GXZ7, O55151, O55152, O55153, Q5BK19, Q99MG1, Q99MG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	July 24, 2007
Last modified:	April 3, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program