ID   CYTF_HUMAN              Reviewed;         145 AA.
AC   O76096; Q6FH95; Q7Z4J8; Q9UED4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   13-FEB-2019, entry version 154.
DE   RecName: Full=Cystatin-F;
DE   AltName: Full=Cystatin-7;
DE   AltName: Full=Cystatin-like metastasis-associated protein;
DE            Short=CMAP;
DE   AltName: Full=Leukocystatin;
DE   Flags: Precursor;
GN   Name=CST7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9632704; DOI=10.1074/jbc.273.26.16400;
RA   Halfon S., Ford J., Foster J., Dowling L., Lucian L., Sterling M.,
RA   Xu Y., Weiss M., Ikeda M., Liggett D., Helms A., Caux C., Lebecque S.,
RA   Hannum C., Menon S., McClanahan T., Gorman D., Zurawski G.;
RT   "Leukocystatin, a new class II cystatin expressed selectively by
RT   hematopoietic cells.";
RL   J. Biol. Chem. 273:16400-16408(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9733783; DOI=10.1074/jbc.273.38.24797;
RA   Ni J., Fernandez M.A., Danielsson L., Chillakuru R.A., Zhang J.,
RA   Grubb A., Su J., Gentz R., Abrahamson M.;
RT   "Cystatin F is a glycosylated human low molecular weight cysteine
RT   proteinase inhibitor.";
RL   J. Biol. Chem. 273:24797-24804(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10945474; DOI=10.1006/geno.2000.6237;
RA   Morita M., Hara Y., Tamai Y., Arakawa H., Nishimura S.;
RT   "Genomic construct and mapping of the gene for CMAP
RT   (leukocystatin/cystatin F, CST7) and identification of a proximal
RT   novel gene, BSCv (C20orf3).";
RL   Genomics 67:87-91(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC   TISSUE=Blood;
RX   PubMed=12423348; DOI=10.1046/j.1432-1033.2002.03252.x;
RA   Nathanson C.M., Wasselius J., Wallin H., Abrahamson M.;
RT   "Regulated expression and intracellular localization of cystatin F in
RT   human U937 cells.";
RL   Eur. J. Biochem. 269:5502-5511(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Morita M., Arakawa H., Yoshiuchi N.;
RT   "Human homologue of murine CMAP.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-19, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-145, SUBUNIT,
RP   GLYCOSYLATION AT ASN-62 AND ASN-115, AND DISULFIDE BONDS.
RX   PubMed=16601115; DOI=10.1074/jbc.M601033200;
RA   Schuettelkopf A.W., Hamilton G., Watts C., van Aalten D.M.F.;
RT   "Structural basis of reduction-dependent activation of human cystatin
RT   F.";
RL   J. Biol. Chem. 281:16570-16575(2006).
CC   -!- FUNCTION: Inhibits papain and cathepsin L but with affinities
CC       lower than other cystatins. May play a role in immune regulation
CC       through inhibition of a unique target in the hematopoietic system.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC       {ECO:0000269|PubMed:16601115}.
CC   -!- INTERACTION:
CC       P53634:CTSC; NbExp=2; IntAct=EBI-2807448, EBI-1047323;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12423348}.
CC       Cytoplasm {ECO:0000269|PubMed:12423348}.
CC   -!- TISSUE SPECIFICITY: Primarily expressed in peripheral blood cells
CC       and spleen.
CC   -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH15507.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAP88827.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAA34941.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAB11886.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR   EMBL; AF031824; AAC39788.1; -; mRNA.
DR   EMBL; AF036342; AAC35747.1; -; mRNA.
DR   EMBL; AB029636; BAB11886.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AJ510167; CAD52872.1; -; Genomic_DNA.
DR   EMBL; AJ510168; CAD52872.1; JOINED; Genomic_DNA.
DR   EMBL; AJ510169; CAD52872.1; JOINED; Genomic_DNA.
DR   EMBL; AJ510170; CAD52872.1; JOINED; Genomic_DNA.
DR   EMBL; AB015225; BAA34941.1; ALT_INIT; mRNA.
DR   EMBL; BT009825; AAP88827.1; ALT_INIT; mRNA.
DR   EMBL; CR541860; CAG46658.1; -; mRNA.
DR   EMBL; CR541878; CAG46676.1; -; mRNA.
DR   EMBL; AL035661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC015507; AAH15507.1; ALT_INIT; mRNA.
DR   CCDS; CCDS13165.2; -.
DR   RefSeq; NP_003641.3; NM_003650.3.
DR   UniGene; Hs.143212; -.
DR   PDB; 2CH9; X-ray; 2.10 A; A=20-145.
DR   PDBsum; 2CH9; -.
DR   ProteinModelPortal; O76096; -.
DR   SMR; O76096; -.
DR   BioGrid; 114100; 9.
DR   IntAct; O76096; 3.
DR   MINT; O76096; -.
DR   STRING; 9606.ENSP00000420384; -.
DR   MEROPS; I25.007; -.
DR   iPTMnet; O76096; -.
DR   PhosphoSitePlus; O76096; -.
DR   BioMuta; CST7; -.
DR   EPD; O76096; -.
DR   jPOST; O76096; -.
DR   PaxDb; O76096; -.
DR   PeptideAtlas; O76096; -.
DR   PRIDE; O76096; -.
DR   ProteomicsDB; 50415; -.
DR   DNASU; 8530; -.
DR   Ensembl; ENST00000480798; ENSP00000420384; ENSG00000077984.
DR   GeneID; 8530; -.
DR   KEGG; hsa:8530; -.
DR   UCSC; uc002wtx.2; human.
DR   CTD; 8530; -.
DR   DisGeNET; 8530; -.
DR   EuPathDB; HostDB:ENSG00000077984.5; -.
DR   GeneCards; CST7; -.
DR   HGNC; HGNC:2479; CST7.
DR   HPA; HPA040442; -.
DR   MIM; 603253; gene.
DR   neXtProt; NX_O76096; -.
DR   OpenTargets; ENSG00000077984; -.
DR   PharmGKB; PA26980; -.
DR   eggNOG; ENOG410J26J; Eukaryota.
DR   eggNOG; ENOG41121KX; LUCA.
DR   GeneTree; ENSGT00940000160277; -.
DR   HOGENOM; HOG000112134; -.
DR   HOVERGEN; HBG009556; -.
DR   InParanoid; O76096; -.
DR   KO; K13903; -.
DR   OMA; DNCDFQT; -.
DR   OrthoDB; 1565344at2759; -.
DR   PhylomeDB; O76096; -.
DR   ChiTaRS; CST7; human.
DR   EvolutionaryTrace; O76096; -.
DR   GeneWiki; CST7_(gene); -.
DR   GenomeRNAi; 8530; -.
DR   PRO; PR:O76096; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; ENSG00000077984; Expressed in 122 organ(s), highest expression level in blood.
DR   Genevisible; O76096; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:ProtInc.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   CDD; cd00042; CY; 1.
DR   InterPro; IPR027214; Cystatin.
DR   InterPro; IPR000010; Cystatin_dom.
DR   PANTHER; PTHR11413; PTHR11413; 1.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Disulfide bond;
KW   Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Signal; Thiol protease inhibitor.
FT   SIGNAL        1     19       {ECO:0000244|PubMed:25944712,
FT                                ECO:0000255}.
FT   CHAIN        20    145       Cystatin-F.
FT                                /FTId=PRO_0000006646.
FT   MOTIF        81     85       Secondary area of contact.
FT   SITE         37     37       Reactive site.
FT   CARBOHYD     62     62       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16601115}.
FT   CARBOHYD    115    115       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16601115}.
FT   DISULFID     26     26       Interchain (with C-63).
FT                                {ECO:0000269|PubMed:16601115}.
FT   DISULFID     63     63       Interchain (with C-26).
FT                                {ECO:0000269|PubMed:16601115}.
FT   DISULFID     99    110       {ECO:0000269|PubMed:16601115}.
FT   DISULFID    124    144       {ECO:0000269|PubMed:16601115}.
FT   HELIX        47     63       {ECO:0000244|PDB:2CH9}.
FT   STRAND       67    100       {ECO:0000244|PDB:2CH9}.
FT   HELIX       107    109       {ECO:0000244|PDB:2CH9}.
FT   TURN        116    118       {ECO:0000244|PDB:2CH9}.
FT   STRAND      121    131       {ECO:0000244|PDB:2CH9}.
FT   HELIX       132    134       {ECO:0000244|PDB:2CH9}.
FT   STRAND      136    145       {ECO:0000244|PDB:2CH9}.
SQ   SEQUENCE   145 AA;  16454 MW;  B2BCC4F76857CB0F CRC64;
     MRAAGTLLAF CCLVLSTTGG PSPDTCSQDL NSRVKPGFPK TIKTNDPGVL QAARYSVEKF
     NNCTNDMFLF KESRITRALV QIVKGLKYML EVEIGRTTCK KNQHLRLDDC DFQTNHTLKQ
     TLSCYSEVWV VPWLQHFEVP VLRCH
//