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O76096 (CYTF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Cystatin-F
Alternative name(s):
Cystatin-7
Cystatin-like metastasis-associated protein
Short name=CMAP
Leukocystatin
Gene names
Name:CST7
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homodimer; disulfide-linked. Ref.10

Subcellular location

Secreted. Cytoplasm Ref.4.

Tissue specificity

Primarily expressed in peripheral blood cells and spleen.

Sequence similarities

Belongs to the cystatin family.

Sequence caution

The sequence AAH15507.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAP88827.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA34941.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB11886.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB75498.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
Secreted
   DomainSignal
   Molecular functionProtease inhibitor
Thiol protease inhibitor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processimmune response

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type endopeptidase inhibitor activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 145126Cystatin-F
PRO_0000006646

Regions

Motif81 – 855Secondary area of contact

Sites

Site371Reactive site

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Ref.10
Glycosylation1151N-linked (GlcNAc...) Ref.10
Disulfide bond26Interchain (with C-63) Ref.10
Disulfide bond63Interchain (with C-26) Ref.10
Disulfide bond99 ↔ 110 Ref.10
Disulfide bond124 ↔ 144 Ref.10

Secondary structure

.............. 145
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O76096 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: B2BCC4F76857CB0F

FASTA14516,454
        10         20         30         40         50         60 
MRAAGTLLAF CCLVLSTTGG PSPDTCSQDL NSRVKPGFPK TIKTNDPGVL QAARYSVEKF 

        70         80         90        100        110        120 
NNCTNDMFLF KESRITRALV QIVKGLKYML EVEIGRTTCK KNQHLRLDDC DFQTNHTLKQ 

       130        140 
TLSCYSEVWV VPWLQHFEVP VLRCH 

« Hide

References

« Hide 'large scale' references
[1]"Leukocystatin, a new class II cystatin expressed selectively by hematopoietic cells."
Halfon S., Ford J., Foster J., Dowling L., Lucian L., Sterling M., Xu Y., Weiss M., Ikeda M., Liggett D., Helms A., Caux C., Lebecque S., Hannum C., Menon S., McClanahan T., Gorman D., Zurawski G.
J. Biol. Chem. 273:16400-16408(1998) [PubMed: 9632704] [Abstract]
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: 9733783] [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: 10945474] [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: 12423348] [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. expand/collapse author list , 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: 11780052] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[10]"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: 16601115] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-145, SUBUNIT, GLYCOSYLATION AT ASN-62 AND ASN-115, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031824 mRNA. Translation: AAC39788.1.
AF036342 mRNA. Translation: AAC35747.1.
AB029636 Genomic DNA. Translation: BAB11886.1. Different initiation.
AJ510167 expand/collapse EMBL AC list , 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.
IPIIPI00216569.
RefSeqNP_003641.3. NM_003650.3.
UniGeneHs.143212.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CH9X-ray2.10A20-145[»]
ProteinModelPortalO76096.
SMRO76096. Positions 25-144.
ModBaseSearch...

Protein-protein interaction databases

IntActO76096. 1 interaction.
MINTMINT-6179682.
STRINGO76096.

Protein family/group databases

MEROPSI25.007.

Proteomic databases

PRIDEO76096.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376835; ENSP00000366031; ENSG00000077984.
ENST00000480798; ENSP00000420384; ENSG00000077984.
GeneID8530.
KEGGhsa:8530.
UCSCuc002wtx.1. human.

Organism-specific databases

CTD8530.
GeneCardsGC20P024924.
HGNCHGNC:2479. CST7.
MIM603253. gene.
neXtProtNX_O76096.
PharmGKBPA26980.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16003.
GeneTreeENSGT00600000084460.
HOGENOMHBG717109.
HOVERGENHBG009556.
InParanoidO76096.
OrthoDBEOG4KH2WN.

Gene expression databases

ArrayExpressO76096.
BgeeO76096.
CleanExHS_CST7.
GenevestigatorO76096.
GermOnlineENSG00000077984. Homo sapiens.

Family and domain databases

InterProIPR000010. Prot_inh_cystat.
[Graphical view]
KOK13903.
PfamPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTSM00043. CY. 1 hit.
[Graphical view]
PROSITEPS00287. CYSTATIN. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio31944.
SOURCESearch...

Entry information

Entry nameCYTF_HUMAN
AccessionPrimary (citable) accession number: O76096
Secondary accession number(s): Q6FH95, Q7Z4J8, Q9UED4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: November 16, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families