CAT7_MOUSE
ID CAT7_MOUSE Reviewed; 331 AA.
AC Q91ZF2; Q9JI84;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cathepsin 7 {ECO:0000312|EMBL:AAH64740.1};
DE EC=3.4.22.-;
DE AltName: Full=Cathepsin 1 {ECO:0000312|EMBL:AAK00508.1};
DE Flags: Precursor;
GN Name=Cts7 {ECO:0000312|EMBL:AAH64740.1,
GN ECO:0000312|Ensembl:ENSMUSP00000021892, ECO:0000312|MGI:MGI:1860262};
GN Synonyms=Cts1 {ECO:0000312|EMBL:AAK00508.1},
GN Epcs24 {ECO:0000312|EMBL:AAF81274.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAK00508.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK00508.1};
RC TISSUE=Placenta {ECO:0000312|EMBL:AAK00508.1};
RX PubMed=11829493; DOI=10.1006/geno.2002.6696;
RA Deussing J., Kouadio M., Rehman S., Werber I., Schwinde A., Peters C.;
RT "Identification and characterization of a dense cluster of placenta-
RT specific cysteine peptidase genes and related genes on mouse chromosome
RT 13.";
RL Genomics 79:225-240(2002).
RN [2] {ECO:0000312|Ensembl:ENSMUSP00000021892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:EDL41318.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH64740.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH64740.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH64740.1};
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAF81274.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-329, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:10885754};
RC TISSUE=Placenta {ECO:0000269|PubMed:10885754};
RX PubMed=10885754; DOI=10.1006/dbio.2000.9705;
RA Hemberger M., Himmelbauer H., Ruschmann J., Zeitz C., Fundele R.;
RT "cDNA subtraction cloning reveals novel genes whose temporal and spatial
RT expression indicates association with trophoblast invasion.";
RL Dev. Biol. 222:158-169(2000).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=18776147; DOI=10.1242/dev.025627;
RA Screen M., Dean W., Cross J.C., Hemberger M.;
RT "Cathepsin proteases have distinct roles in trophoblast function and
RT vascular remodelling.";
RL Development 135:3311-3320(2008).
CC -!- FUNCTION: Involved in trophoblast cell proliferation and
CC differentiation probably by affecting mitotic cell cycle progression.
CC Proteolytic activity and nuclear localization are essential for its
CC role in cell cycle progression. {ECO:0000269|PubMed:18776147}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:18776147,
CC ECO:0000305}. Lysosome {ECO:0000269|PubMed:18776147, ECO:0000305}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:18776147}. Golgi
CC apparatus {ECO:0000269|PubMed:18776147, ECO:0000305}. Nucleus
CC {ECO:0000269|PubMed:18776147}. Secreted, extracellular space
CC {ECO:0000269|PubMed:18776147}.
CC -!- TISSUE SPECIFICITY: Expressed in placenta. Expressed in parietal and
CC spiral artery-associated trophoblast giant cells, most abundantly
CC during the phase of trophoblast invasion. From 14.5 dpc onwards,
CC expressed at lower levels in labyrinth trophoblast cells. Expressed in
CC trophoblast stem cells. Expressed in heart, liver and testis.
CC {ECO:0000269|PubMed:10885754, ECO:0000269|PubMed:11829493,
CC ECO:0000269|PubMed:18776147}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult but not in embryo. Expressed in
CC the placenta from early post-implantation (5.5 dpc) onwards. After 9.5
CC dpc expression declines. {ECO:0000269|PubMed:10885754,
CC ECO:0000269|PubMed:11829493, ECO:0000269|PubMed:18776147}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR EMBL; AY014779; AAK00508.1; -; mRNA.
DR EMBL; CT030645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466546; EDL41318.1; -; Genomic_DNA.
DR EMBL; BC064740; AAH64740.1; -; mRNA.
DR EMBL; AF250837; AAF81274.1; -; mRNA.
DR CCDS; CCDS26588.1; -.
DR RefSeq; NP_062412.1; NM_019539.3.
DR RefSeq; XP_006517360.1; XM_006517297.1.
DR AlphaFoldDB; Q91ZF2; -.
DR SMR; Q91ZF2; -.
DR STRING; 10090.ENSMUSP00000021892; -.
DR MEROPS; C01.016; -.
DR GlyGen; Q91ZF2; 1 site.
DR PaxDb; Q91ZF2; -.
DR PRIDE; Q91ZF2; -.
DR DNASU; 56092; -.
DR Ensembl; ENSMUST00000021892; ENSMUSP00000021892; ENSMUSG00000021440.
DR Ensembl; ENSMUST00000224986; ENSMUSP00000153603; ENSMUSG00000021440.
DR GeneID; 56092; -.
DR KEGG; mmu:56092; -.
DR UCSC; uc007qwi.1; mouse.
DR CTD; 56092; -.
DR MGI; MGI:1860262; Cts7.
DR VEuPathDB; HostDB:ENSMUSG00000021440; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q91ZF2; -.
DR OMA; LTEWEIW; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q91ZF2; -.
DR TreeFam; TF313739; -.
DR BioGRID-ORCS; 56092; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q91ZF2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q91ZF2; protein.
DR Bgee; ENSMUSG00000021440; Expressed in ectoplacental cone and 14 other tissues.
DR ExpressionAtlas; Q91ZF2; baseline and differential.
DR Genevisible; Q91ZF2; MM.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISA:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0097655; F:serpin family protein binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030574; P:collagen catabolic process; ISO:MGI.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; ISO:MGI.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; ISO:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:MGI.
DR GO; GO:0016540; P:protein autoprocessing; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISA:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:MGI.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Disulfide bond; Endosome;
KW Glycoprotein; Golgi apparatus; Hydrolase; Lysosome; Mitosis; Nucleus;
KW Protease; Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255, ECO:0000312|EMBL:AAK00508.1"
FT PROPEP 18..111
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT /id="PRO_0000415396"
FT CHAIN 112..331
FT /note="Cathepsin 7"
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT /id="PRO_5000088249"
FT MOTIF 33..50
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:18776147"
FT ACT_SITE 136
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT ACT_SITE 274
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT ACT_SITE 298
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..176
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT DISULFID 167..209
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT DISULFID 267..320
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT CONFLICT 329
FT /note="P -> L (in Ref. 5; AAF81274)"
FT /evidence="ECO:0000305|PubMed:10885754"
SQ SEQUENCE 331 AA; 37725 MW; 985E9FAF4F671FCA CRC64;
MTPTVFLSIL CLGVALAAPA PDYNLDAEWE EWKRSNDRTY SPEEEKQRRA VWEGNVKWIK
QHIMENGLWM NNFTIEMNEF GDMTGEEMKM LTESSSYPLR NGKHIQKRNP KIPPTLDWRK
EGYVTPVRRQ GSCGACWAFS VTACIEGQLF KKTGKLIPLS VQNLMDCSVS YGTKGCDGGR
PYDAFQYVKN NGGLEAEATY PYEAKAKHCR YRPERSVVKV NRFFVVPRNE EALLQALVTH
GPIAVAIDGS HASFHSYRGG IYHEPKCRKD TLDHGLLLVG YGYEGHESEN RKYWLLKNSH
GERWGENGYM KLPRGQNNYC GIASYAMYPA L
