Reviewed, UniProtKB/Swiss-Prot O76096 (CYTF_HUMAN)

Names and origin

Protein names

Recommended name:
    Cystatin-F
Alternative name(s):
    Leukocystatin
    Cystatin-7
    Cystatin-like metastasis-associated protein
      Short name=CMAP

Gene names

Name:

CST7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	145 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subcellular location	Secreted. Cytoplasm.
Tissue specificity	Primarily expressed in peripheral blood cells and spleen.
Sequence similarities	Belongs to the cystatin family.

Ontologies

Keywords
Cellular component	Cytoplasm Secreted
Domain	Signal
Molecular function	Protease inhibitor Thiol protease inhibitor
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	immune response Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cysteine protease inhibitor activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 145

126

Cystatin-F

PRO_0000006646

Regions

Motif

81 – 85

5

Secondary area of contact

Sites

Site

37

1

Reactive site

Amino acid modifications

Glycosylation

62

1

N-linked (GlcNAc...)

Glycosylation

115

1

N-linked (GlcNAc...)

Disulfide bond

26

Interchain (with C-63)

Disulfide bond

63

Interchain (with C-26)

Disulfide bond

99 ↔ 110

Disulfide bond

124 ↔ 144

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

145

Helix Strand Turn

Details...

Beta strand

28 – 34

7

Helix

47 – 63

17

Beta strand

67 – 100

34

Helix

107 – 109

3

Turn

116 – 118

3

Beta strand

121 – 131

11

Helix

132 – 134

3

Sequences

	Sequence		Length	Mass (Da)
	O76096-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: B2BCC4F76857CB0F	FASTA	145	16,454
	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

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

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.

RefSeq

NP_003641.2.

UniGene

Hs.143212

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CH9	X-ray	2.10	A	20-145	[»]

ModBase

Search...

Protein family/group databases

MEROPS

I25.007.

Genome annotation databases

Ensembl

ENSG00000077984. Homo sapiens. [Contig view]

GeneID

8530.

KEGG

hsa:8530.

Organism-specific databases

H-InvDB

HIX0015697.

HGNC

HGNC:2479. CST7.

MIM

603253. gene.

PharmGKB

PA26980.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

O76096.

HOVERGEN

O76096.

Gene expression databases

ArrayExpress

O76096.

CleanEx

HS_CST7.

GermOnline

ENSG00000077984. Homo sapiens.

Family and domain databases

InterPro

IPR000010. Prot_inh_cystat.
[Graphical view]

Pfam

PF00031. Cystatin. 1 hit.
[Graphical view]

ProDom

PD001231. Prot_inh_I25A_B. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00043. CY. 1 hit.
[Graphical view]

PROSITE

PS00287. CYSTATIN. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

31944.

SOURCE

Search...

Entry information

Entry name

CYTF_HUMAN

Accession

Primary (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 25, 2008
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)