ID   CYTF_MOUSE              Reviewed;         144 AA.
AC   O89098;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 146.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=9632704; DOI=10.1074/jbc.273.26.16400;
RA   Halfon S., Ford J., Foster J., Dowling L., Lucian L., Sterling M., Xu Y.,
RA   Weiss M., Ikeda M., Liggett D., Helms A., Caux C., Lebecque S., Hannum C.,
RA   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).
CC   -!- FUNCTION: Inhibits papain and cathepsin L but with affinities lower
CC       than other cystatins. May play a role in immune regulation through
CC       inhibition of a unique target in the hematopoietic system.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR   EMBL; AF031826; AAC40140.1; -; Genomic_DNA.
DR   EMBL; AF031825; AAC40139.1; -; mRNA.
DR   CCDS; CCDS16857.2; -.
DR   RefSeq; NP_034107.2; NM_009977.3.
DR   AlphaFoldDB; O89098; -.
DR   SMR; O89098; -.
DR   IntAct; O89098; 1.
DR   MINT; O89098; -.
DR   STRING; 10090.ENSMUSP00000086606; -.
DR   MEROPS; I25.007; -.
DR   GlyGen; O89098; 1 site.
DR   PhosphoSitePlus; O89098; -.
DR   EPD; O89098; -.
DR   PaxDb; O89098; -.
DR   PRIDE; O89098; -.
DR   ProteomicsDB; 279258; -.
DR   Antibodypedia; 24951; 181 antibodies from 34 providers.
DR   DNASU; 13011; -.
DR   Ensembl; ENSMUST00000089200; ENSMUSP00000086606; ENSMUSG00000068129.
DR   GeneID; 13011; -.
DR   KEGG; mmu:13011; -.
DR   UCSC; uc008muc.2; mouse.
DR   CTD; 8530; -.
DR   MGI; MGI:1298217; Cst7.
DR   VEuPathDB; HostDB:ENSMUSG00000068129; -.
DR   eggNOG; ENOG502S5CP; Eukaryota.
DR   GeneTree; ENSGT00940000160277; -.
DR   HOGENOM; CLU_118168_1_0_1; -.
DR   InParanoid; O89098; -.
DR   OMA; VVPWLQH; -.
DR   OrthoDB; 1565344at2759; -.
DR   PhylomeDB; O89098; -.
DR   BioGRID-ORCS; 13011; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Cst7; mouse.
DR   PRO; PR:O89098; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; O89098; protein.
DR   Bgee; ENSMUSG00000068129; Expressed in bone marrow and 102 other tissues.
DR   Genevisible; O89098; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IMP:ARUK-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; IMP:ARUK-UCL.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:ARUK-UCL.
DR   GO; GO:0005770; C:late endosome; IMP:ARUK-UCL.
DR   GO; GO:0005764; C:lysosome; IMP:ARUK-UCL.
DR   GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IMP:MGI.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IDA:ARUK-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0097340; P:inhibition of cysteine-type endopeptidase activity; IMP:MGI.
DR   GO; GO:1903979; P:negative regulation of microglial cell activation; IMP:MGI.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IDA:ARUK-UCL.
DR   GO; GO:0031643; P:positive regulation of myelination; IMP:MGI.
DR   CDD; cd00042; CY; 1.
DR   InterPro; IPR042886; Cystatin-F.
DR   InterPro; IPR000010; Cystatin_dom.
DR   InterPro; IPR046350; Cystatin_sf.
DR   PANTHER; PTHR47141; PTHR47141; 1.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Signal; Thiol protease inhibitor.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..144
FT                   /note="Cystatin-F"
FT                   /id="PRO_0000006647"
FT   MOTIF           80..84
FT                   /note="Secondary area of contact"
FT   SITE            36
FT                   /note="Reactive site"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        98..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..143
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   144 AA;  16380 MW;  B5837334C1B4A89C CRC64;
     MWLAILLALC CLTSDTHGAR PPDFCSKDLI SSVKPGFPKT IETNNPGVLK AARHSVEKFN
     NCTNDIFLFK ESHVSKALVQ VVKGLKYMLE VKIGRTTCRK TMHHQLDNCD FQTNPALKRT
     LYCYSEVWVI PWLHSFEVPV LLCQ
//