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Protein

Cystatin-D

Gene

CST5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B.1 Publication

Temperature dependencei

Thermostable.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei32 – 321Reactive siteBy similarity

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Thiol protease inhibitor

Protein family/group databases

MEROPSiI25.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystatin-D
Alternative name(s):
Cystatin-5
Gene namesi
Name:CST5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:2477. CST5.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26978.

Polymorphism and mutation databases

BioMutaiCST5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 142122Cystatin-DPRO_0000006645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi95 ↔ 105
Disulfide bondi119 ↔ 139

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP28325.
PeptideAtlasiP28325.
PRIDEiP28325.

Expressioni

Tissue specificityi

Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in parotid gland but not in seminal vesicle, prostate, epididymis, testis, ovary, placenta, thyroid, gastric corpus, small intestine, liver, or gall bladder tissue.1 Publication

Gene expression databases

BgeeiP28325.
CleanExiHS_CST5.
GenevisibleiP28325. HS.

Organism-specific databases

HPAiCAB024944.
HPA061449.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi107855. 8 interactions.
STRINGi9606.ENSP00000307132.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374Combined sources
Helixi42 – 5716Combined sources
Beta strandi63 – 7816Combined sources
Beta strandi81 – 9616Combined sources
Turni111 – 1133Combined sources
Beta strandi117 – 12610Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 14111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RN7X-ray2.50A21-142[»]
1ROAX-ray1.80A21-142[»]
ProteinModelPortaliP28325.
SMRiP28325. Positions 31-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28325.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi70 – 745Secondary area of contact

Sequence similaritiesi

Belongs to the cystatin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410KIFQ. Eukaryota.
ENOG4110QA3. LUCA.
GeneTreeiENSGT00840000129787.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP28325.
KOiK13901.
OMAiDNCPFND.
OrthoDBiEOG7M98J9.
PhylomeDBiP28325.

Family and domain databases

InterProiIPR027214. Cystatin.
IPR000010. Cystatin_dom.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PANTHERiPTHR11413. PTHR11413. 1 hit.
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 1 hit.
[Graphical view]
PROSITEiPS00287. CYSTATIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMWPMHTPLL LLTALMVAVA GSASAQSRTL AGGIHATDLN DKSVQCALDF
60 70 80 90 100
AISEYNKVIN KDEYYSRPLQ VMAAYQQIVG GVNYYFNVKF GRTTCTKSQP
110 120 130 140
NLDNCPFNDQ PKLKEEEFCS FQINEVPWED KISILNYKCR KV
Length:142
Mass (Da):16,080
Last modified:December 1, 1992 - v1
Checksum:iCEFA89BA87A0DA68
GO

Mass spectrometryi

Molecular mass is 13154.4675±0.0101 Da from positions 29 - 142. Determined by ESI. Variant Arg-46.1 Publication
Molecular mass is 13596.7015±0.0049 Da from positions 25 - 142. Determined by ESI. Variant Arg-46.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461C → R in 45% of the population. 1 Publication
Corresponds to variant rs1799841 [ dbSNP | Ensembl ].
VAR_002208

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59964 Genomic DNA. Translation: CAA42590.1.
X70377 mRNA. Translation: CAA49838.1.
AL591074 Genomic DNA. Translation: CAI23644.1.
BC062678 mRNA. Translation: AAH62678.1.
BC069514 mRNA. Translation: AAH69514.1.
CCDSiCCDS13162.1.
PIRiA47142.
RefSeqiNP_001891.2. NM_001900.4.
UniGeneiHs.121489.

Genome annotation databases

EnsembliENST00000304710; ENSP00000307132; ENSG00000170367.
GeneIDi1473.
KEGGihsa:1473.
UCSCiuc002wtr.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59964 Genomic DNA. Translation: CAA42590.1.
X70377 mRNA. Translation: CAA49838.1.
AL591074 Genomic DNA. Translation: CAI23644.1.
BC062678 mRNA. Translation: AAH62678.1.
BC069514 mRNA. Translation: AAH69514.1.
CCDSiCCDS13162.1.
PIRiA47142.
RefSeqiNP_001891.2. NM_001900.4.
UniGeneiHs.121489.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RN7X-ray2.50A21-142[»]
1ROAX-ray1.80A21-142[»]
ProteinModelPortaliP28325.
SMRiP28325. Positions 31-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107855. 8 interactions.
STRINGi9606.ENSP00000307132.

Protein family/group databases

MEROPSiI25.005.

Polymorphism and mutation databases

BioMutaiCST5.

Proteomic databases

PaxDbiP28325.
PeptideAtlasiP28325.
PRIDEiP28325.

Protocols and materials databases

DNASUi1473.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304710; ENSP00000307132; ENSG00000170367.
GeneIDi1473.
KEGGihsa:1473.
UCSCiuc002wtr.2. human.

Organism-specific databases

CTDi1473.
GeneCardsiCST5.
HGNCiHGNC:2477. CST5.
HPAiCAB024944.
HPA061449.
MIMi123858. gene.
neXtProtiNX_P28325.
PharmGKBiPA26978.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KIFQ. Eukaryota.
ENOG4110QA3. LUCA.
GeneTreeiENSGT00840000129787.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP28325.
KOiK13901.
OMAiDNCPFND.
OrthoDBiEOG7M98J9.
PhylomeDBiP28325.

Miscellaneous databases

EvolutionaryTraceiP28325.
GeneWikiiCST5.
GenomeRNAii1473.
PROiP28325.
SOURCEiSearch...

Gene expression databases

BgeeiP28325.
CleanExiHS_CST5.
GenevisibleiP28325. HS.

Family and domain databases

InterProiIPR027214. Cystatin.
IPR000010. Cystatin_dom.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PANTHERiPTHR11413. PTHR11413. 1 hit.
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 1 hit.
[Graphical view]
PROSITEiPS00287. CYSTATIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of the gene encoding cystatin D, a novel human cysteine proteinase inhibitor."
    Freije J.P., Abrahamson M., Olafssonn I., Velasco G., Grubb A., Lopez-Otin C.
    J. Biol. Chem. 266:20538-20543(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Leukocyte.
  2. "Human cystatin D. cDNA cloning, characterization of the Escherichia coli expressed inhibitor, and identification of the native protein in saliva."
    Freije J.P., Balbin M., Abrahamson M., Velasco G., Dalboge H., Grubb A., Lopez-Otin C.
    J. Biol. Chem. 268:15737-15744(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Parotid gland.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases."
    Balbin M., Hall A., Grubb A., Mason R.W., Lopez-Otin C., Abrahamson M.
    J. Biol. Chem. 269:23156-23162(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-38, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  6. "Confident assignment of intact mass tags to human salivary cystatins using top-down Fourier-transform ion cyclotron resonance mass spectrometry."
    Ryan C.M., Souda P., Halgand F., Wong D.T., Loo J.A., Faull K.F., Whitelegge J.P.
    J. Am. Soc. Mass Spectrom. 21:908-917(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
    Tissue: Saliva.
  7. "Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile."
    Alvarez-Fernandez M., Liang Y.H., Abrahamson M., Su X.D.
    J. Biol. Chem. 280:18221-18228(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-142, DISULFIDE BONDS.
  8. "A sequence variation in the human cystatin D gene resulting in an amino acid (Cys/Arg) polymorphism at the protein level."
    Balbin M., Freije J.P., Abrahamson M., Velasco G., Lopez-Otin C.
    Hum. Genet. 90:668-669(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-46.

Entry informationi

Entry nameiCYTD_HUMAN
AccessioniPrimary (citable) accession number: P28325
Secondary accession number(s): Q5JRF5, Q9UCA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 6, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

The truncated forms found may result from N-terminal proteolysis.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.