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Protein

Cystatin-F

Gene

CST7

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

Functioni

Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei37 – 371Reactive site

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity Source: ProtInc
  • endopeptidase inhibitor activity Source: ProtInc

GO - Biological processi

  • immune response Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Thiol protease inhibitor

Protein family/group databases

MEROPSiI25.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystatin-F
Alternative name(s):
Cystatin-7
Cystatin-like metastasis-associated protein
Short name:
CMAP
Leukocystatin
Gene namesi
Name:CST7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:2479. CST7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26980.

Polymorphism and mutation databases

BioMutaiCST7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisCombined sourcesAdd
BLAST
Chaini20 – 145126Cystatin-FPRO_0000006646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 – 26Interchain (with C-63)1 Publication
Glycosylationi62 – 621N-linked (GlcNAc...)1 Publication
Disulfide bondi63 – 63Interchain (with C-26)1 Publication
Disulfide bondi99 ↔ 1101 Publication
Glycosylationi115 – 1151N-linked (GlcNAc...)1 Publication
Disulfide bondi124 ↔ 1441 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiO76096.
PaxDbiO76096.
PeptideAtlasiO76096.
PRIDEiO76096.

PTM databases

iPTMnetiO76096.

Expressioni

Tissue specificityi

Primarily expressed in peripheral blood cells and spleen.

Gene expression databases

BgeeiO76096.
CleanExiHS_CST7.
GenevisibleiO76096. HS.

Organism-specific databases

HPAiHPA040442.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CTSCP536342EBI-2807448,EBI-1047323

Protein-protein interaction databases

BioGridi114100. 8 interactions.
IntActiO76096. 2 interactions.
MINTiMINT-6179682.
STRINGi9606.ENSP00000420384.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 6317Combined sources
Beta strandi67 – 10034Combined sources
Helixi107 – 1093Combined sources
Turni116 – 1183Combined sources
Beta strandi121 – 13111Combined sources
Helixi132 – 1343Combined sources
Beta strandi136 – 14510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CH9X-ray2.10A20-145[»]
ProteinModelPortaliO76096.
SMRiO76096. Positions 25-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO76096.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi81 – 855Secondary area of contact

Sequence similaritiesi

Belongs to the cystatin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J26J. Eukaryota.
ENOG41121KX. LUCA.
GeneTreeiENSGT00840000129890.
HOGENOMiHOG000112134.
HOVERGENiHBG009556.
InParanoidiO76096.
KOiK13903.
OMAiDNCDFQT.
OrthoDBiEOG7M98J9.
PhylomeDBiO76096.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

O76096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAAGTLLAF CCLVLSTTGG PSPDTCSQDL NSRVKPGFPK TIKTNDPGVL
60 70 80 90 100
QAARYSVEKF NNCTNDMFLF KESRITRALV QIVKGLKYML EVEIGRTTCK
110 120 130 140
KNQHLRLDDC DFQTNHTLKQ TLSCYSEVWV VPWLQHFEVP VLRCH
Length:145
Mass (Da):16,454
Last modified:November 1, 1998 - v1
Checksum:iB2BCC4F76857CB0F
GO

Sequence cautioni

The sequence AAH15507.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAP88827.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA34941.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB11886.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAB75498.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031824 mRNA. Translation: AAC39788.1.
AF036342 mRNA. Translation: AAC35747.1.
AB029636 Genomic DNA. Translation: BAB11886.1. Different initiation.
AJ510167
, AJ510168, AJ510169, AJ510170 Genomic DNA. Translation: CAD52872.1.
AB015225 mRNA. Translation: BAA34941.1. Different initiation.
BT009825 mRNA. Translation: AAP88827.1. Different initiation.
CR541860 mRNA. Translation: CAG46658.1.
CR541878 mRNA. Translation: CAG46676.1.
AL035661 Genomic DNA. Translation: CAB75498.2. Different initiation.
BC015507 mRNA. Translation: AAH15507.1. Different initiation.
CCDSiCCDS13165.2.
RefSeqiNP_003641.3. NM_003650.3.
UniGeneiHs.143212.

Genome annotation databases

EnsembliENST00000480798; ENSP00000420384; ENSG00000077984.
GeneIDi8530.
KEGGihsa:8530.
UCSCiuc002wtx.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031824 mRNA. Translation: AAC39788.1.
AF036342 mRNA. Translation: AAC35747.1.
AB029636 Genomic DNA. Translation: BAB11886.1. Different initiation.
AJ510167
, AJ510168, AJ510169, AJ510170 Genomic DNA. Translation: CAD52872.1.
AB015225 mRNA. Translation: BAA34941.1. Different initiation.
BT009825 mRNA. Translation: AAP88827.1. Different initiation.
CR541860 mRNA. Translation: CAG46658.1.
CR541878 mRNA. Translation: CAG46676.1.
AL035661 Genomic DNA. Translation: CAB75498.2. Different initiation.
BC015507 mRNA. Translation: AAH15507.1. Different initiation.
CCDSiCCDS13165.2.
RefSeqiNP_003641.3. NM_003650.3.
UniGeneiHs.143212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CH9X-ray2.10A20-145[»]
ProteinModelPortaliO76096.
SMRiO76096. Positions 25-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114100. 8 interactions.
IntActiO76096. 2 interactions.
MINTiMINT-6179682.
STRINGi9606.ENSP00000420384.

Protein family/group databases

MEROPSiI25.007.

PTM databases

iPTMnetiO76096.

Polymorphism and mutation databases

BioMutaiCST7.

Proteomic databases

EPDiO76096.
PaxDbiO76096.
PeptideAtlasiO76096.
PRIDEiO76096.

Protocols and materials databases

DNASUi8530.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000480798; ENSP00000420384; ENSG00000077984.
GeneIDi8530.
KEGGihsa:8530.
UCSCiuc002wtx.2. human.

Organism-specific databases

CTDi8530.
GeneCardsiCST7.
HGNCiHGNC:2479. CST7.
HPAiHPA040442.
MIMi603253. gene.
neXtProtiNX_O76096.
PharmGKBiPA26980.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J26J. Eukaryota.
ENOG41121KX. LUCA.
GeneTreeiENSGT00840000129890.
HOGENOMiHOG000112134.
HOVERGENiHBG009556.
InParanoidiO76096.
KOiK13903.
OMAiDNCDFQT.
OrthoDBiEOG7M98J9.
PhylomeDBiO76096.

Miscellaneous databases

ChiTaRSiCST7. human.
EvolutionaryTraceiO76096.
GeneWikiiCST7_(gene).
GenomeRNAii8530.
PROiO76096.
SOURCEiSearch...

Gene expression databases

BgeeiO76096.
CleanExiHS_CST7.
GenevisibleiO76096. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor."
    Ni J., Fernandez M.A., Danielsson L., Chillakuru R.A., Zhang J., Grubb A., Su J., Gentz R., Abrahamson M.
    J. Biol. Chem. 273:24797-24804(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Genomic construct and mapping of the gene for CMAP (leukocystatin/cystatin F, CST7) and identification of a proximal novel gene, BSCv (C20orf3)."
    Morita M., Hara Y., Tamai Y., Arakawa H., Nishimura S.
    Genomics 67:87-91(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Regulated expression and intracellular localization of cystatin F in human U937 cells."
    Nathanson C.M., Wasselius J., Wallin H., Abrahamson M.
    Eur. J. Biochem. 269:5502-5511(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    Tissue: Blood.
  5. "Human homologue of murine CMAP."
    Morita M., Arakawa H., Yoshiuchi N.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "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].
  9. "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].
    Tissue: Lung.
  10. Cited for: CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural basis of reduction-dependent activation of human cystatin F."
    Schuettelkopf A.W., Hamilton G., Watts C., van Aalten D.M.F.
    J. Biol. Chem. 281:16570-16575(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-145, SUBUNIT, GLYCOSYLATION AT ASN-62 AND ASN-115, DISULFIDE BONDS.

Entry informationi

Entry nameiCYTF_HUMAN
AccessioniPrimary (citable) accession number: O76096
Secondary accession number(s): Q6FH95, Q7Z4J8, Q9UED4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 135 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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