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Protein
Submitted name:

Caspase 7

Gene

Casp7

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei144 – 1441UniRule annotation
Active sitei186 – 1861UniRule annotation

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • apoptotic process Source: RGD
  • execution phase of apoptosis Source: Ensembl
  • heart development Source: Ensembl
  • neuron apoptotic process Source: Ensembl
  • protein processing Source: Ensembl
  • proteolysis Source: RGD
  • response to UV Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol proteaseUniRule annotationSAAS annotation

Enzyme and pathway databases

ReactomeiR-RNO-111459. Activation of caspases through apoptosome-mediated cleavage.
R-RNO-111463. SMAC binds to IAPs.
R-RNO-111464. SMAC-mediated dissociation of IAP:caspase complexes.
R-RNO-111465. Apoptotic cleavage of cellular proteins.
R-RNO-264870. Caspase-mediated cleavage of cytoskeletal proteins.

Protein family/group databases

MEROPSiC14.004.

Names & Taxonomyi

Protein namesi
Submitted name:
Caspase 7Imported
Submitted name:
Caspase 7, isoform CRA_cImported
Submitted name:
Caspase-7Imported
Submitted name:
Protein Casp7Imported
Gene namesi
Name:Casp7Imported
ORF Names:rCG_57538Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620944. Casp7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
Complete GO annotation...

PTM / Processingi

Keywords - PTMi

ZymogenUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022693.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 190125CASPASE_P20InterPro annotationAdd
BLAST
Domaini209 – 30395CASPASE_P10InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C14A family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000231878.
HOVERGENiHBG050802.
KOiK04397.
TreeFamiTF102023.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR017350. Pept_C14A_CASP1-typ.
IPR015917. Pept_C14A_HD.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDDQDCAAE LEMADSSTED GVDAKPDRST IISSLLWKKK KNASMCPVST
60 70 80 90 100
TRDRVPTYLY RMDFEKMGKC IIINNKNFDK ATGMDVRNGT DKDAEALFKC
110 120 130 140 150
FRSLGFEVTV YNDCSCAKMQ DLLRRASEED HSNSACFACV LLSHGEENLI
160 170 180 190 200
YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL FFIQACRGTE LDDGIQADSG
210 220 230 240 250
PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRNPGKGSW FVQALCSILN
260 270 280 290 300
EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP RFNEKKQIPC MVSMLTKELY

FGR
Length:303
Mass (Da):34,324
Last modified:November 1, 1998 - v1
Checksum:iA71728754BF199DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07007019 Genomic DNA. No translation available.
AABR07007020 Genomic DNA. No translation available.
AABR07007021 Genomic DNA. No translation available.
AF072124 mRNA. Translation: AAC24011.1.
BC070936 mRNA. Translation: AAH70936.1.
CH473986 Genomic DNA. Translation: EDL94495.1.
RefSeqiNP_071596.1. NM_022260.3.
XP_008758768.1. XM_008760546.1.
UniGeneiRn.53995.

Genome annotation databases

EnsembliENSRNOT00000080511; ENSRNOP00000075193; ENSRNOG00000056216.
GeneIDi64026.
KEGGirno:64026.
UCSCiRGD:620944. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07007019 Genomic DNA. No translation available.
AABR07007020 Genomic DNA. No translation available.
AABR07007021 Genomic DNA. No translation available.
AF072124 mRNA. Translation: AAC24011.1.
BC070936 mRNA. Translation: AAH70936.1.
CH473986 Genomic DNA. Translation: EDL94495.1.
RefSeqiNP_071596.1. NM_022260.3.
XP_008758768.1. XM_008760546.1.
UniGeneiRn.53995.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022693.

Protein family/group databases

MEROPSiC14.004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000080511; ENSRNOP00000075193; ENSRNOG00000056216.
GeneIDi64026.
KEGGirno:64026.
UCSCiRGD:620944. rat.

Organism-specific databases

CTDi840.
RGDi620944. Casp7.

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000231878.
HOVERGENiHBG050802.
KOiK04397.
TreeFamiTF102023.

Enzyme and pathway databases

ReactomeiR-RNO-111459. Activation of caspases through apoptosome-mediated cleavage.
R-RNO-111463. SMAC binds to IAPs.
R-RNO-111464. SMAC-mediated dissociation of IAP:caspase complexes.
R-RNO-111465. Apoptotic cleavage of cellular proteins.
R-RNO-264870. Caspase-mediated cleavage of cytoskeletal proteins.

Miscellaneous databases

NextBioi612635.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR017350. Pept_C14A_CASP1-typ.
IPR015917. Pept_C14A_HD.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat caspase-7 sequence."
    Forghani F., Roy S.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: SpleenImported.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: LungImported.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  6. Ensembl
    Submitted (JUN-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiO88550_RAT
AccessioniPrimary (citable) accession number: O88550
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.