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P04988 (CYSP1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine proteinase 1

EC=3.4.22.-
Gene names
Name:cprA
Synonyms:CP1
ORF Names:DDB_G0290957
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cysteine proteinases 1 and 2 are believed to participate in the breakdown of protein during differentiation of Dictyostelium as a response to starvation.

Subcellular location

Lysosome.

Post-translational modification

Phosphoglycosylated, contains GlcNAc-alpha-1-P-Ser residues. Ref.3

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhyperosmotic response

Inferred from expression pattern PubMed 17517120. Source: dictyBase

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 11799Activation peptide
PRO_0000026358
Chain118 – 343226Cysteine proteinase 1
PRO_0000026359

Sites

Active site1421 By similarity
Active site2861 By similarity
Active site3111 By similarity

Amino acid modifications

Disulfide bond139 ↔ 190 By similarity
Disulfide bond173 ↔ 224 By similarity
Disulfide bond279 ↔ 332 By similarity

Experimental info

Sequence conflict231L → P in CAA26255. Ref.1
Sequence conflict1841Q → E in CAA26255. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P04988 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: 8F70D4907C891021

FASTA34338,510
        10         20         30         40         50         60 
MKVILLFVLA VFTVFVSSRG IPLEEQSQFL EFQDKFNKKY SHEEYLERFE IFKSNLGKIE 

        70         80         90        100        110        120 
ELNLIAINHK ADTKFGVNKF ADLSSDEFKN YYLNNKEAIF TDDLPVADYL DDEFINSIPT 

       130        140        150        160        170        180 
AFDWRTRGAV TPVKNQGQCG SCWSFSTTGN VEGQHFISQN KLVSLSEQNL VDCDHECMEY 

       190        200        210        220        230        240 
EGEQACDEGC NGGLQPNAYN YIIKNGGIQT ESSYPYTAET GTQCNFNSAN IGAKISNFTM 

       250        260        270        280        290        300 
IPKNETVMAG YIVSTGPLAI AADAVEWQFY IGGVFDIPCN PNSLDHGILI VGYSAKNTIF 

       310        320        330        340 
RKNMPYWIVK NSWGADWGEQ GYIYLRRGKN TCGVSNFVST SII 

« Hide

References

« Hide 'large scale' references
[1]"A developmentally regulated cysteine proteinase in Dictyostelium discoideum."
Williams J.G., North M.J., Mahbubani H.M.
EMBO J. 4:999-1006(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[3]"A lysosomal cysteine proteinase from Dictyostelium discoideum contains N-acetylglucosamine-1-phosphate bound to serine but not mannose-6-phosphate on N-linked oligosaccharides."
Mehta D.P., Ichikawa M., Salimath P.V., Etchison J.R., Haak R., Manzi A., Freeze H.H.
J. Biol. Chem. 271:10897-10903(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02407 mRNA. Translation: CAA26255.1.
AAFI02000174 Genomic DNA. Translation: EAL61909.1.
PIRKHDO. A22827.

3D structure databases

ProteinModelPortalP04988.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC01.022.

PTM databases

UniCarbKBP04988.

2D gel databases

SWISS-2DPAGEP04988.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0201647; DDB0201647; DDB_G0290957.
KEGGddi:DDB_G0290957.

Organism-specific databases

dictyBaseDDB_G0290957. cprA.

Phylogenomic databases

eggNOGCOG4870.
KOK01376.
OMAWMQTYIG.
PhylomeDBP04988.
ProtClustDBCLSZ2429603.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSP1_DICDI
AccessionPrimary (citable) accession number: P04988
Secondary accession number(s): Q54FC0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 4, 2007
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase