CAT7_RAT
ID CAT7_RAT Reviewed; 331 AA.
AC D3ZZ07;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cathepsin 7 {ECO:0000312|EMBL:EDL93846.1};
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=Cts7 {ECO:0000312|Ensembl:ENSRNOP00000051349};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:EDL93846.1}
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.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q91ZF2}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q91ZF2}. Lysosome
CC {ECO:0000250|UniProtKB:Q91ZF2}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q91ZF2}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q91ZF2}. Nucleus {ECO:0000250|UniProtKB:Q91ZF2}.
CC Secreted, extracellular space {ECO:0000250|UniProtKB:Q91ZF2}.
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; CH474032; EDL93846.1; -; Genomic_DNA.
DR RefSeq; NP_001099569.1; NM_001106099.1.
DR AlphaFoldDB; D3ZZ07; -.
DR SMR; D3ZZ07; -.
DR STRING; 10116.ENSRNOP00000051349; -.
DR MEROPS; C01.016; -.
DR GlyGen; D3ZZ07; 1 site.
DR PaxDb; D3ZZ07; -.
DR Ensembl; ENSRNOT00000043686; ENSRNOP00000051349; ENSRNOG00000033540.
DR GeneID; 290970; -.
DR KEGG; rno:290970; -.
DR UCSC; RGD:1309226; rat.
DR CTD; 56092; -.
DR RGD; 1309226; Cts7.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; D3ZZ07; -.
DR OMA; LTEWEIW; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; D3ZZ07; -.
DR TreeFam; TF313739; -.
DR PRO; PR:D3ZZ07; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
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 3: Inferred from homology;
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"
FT PROPEP 18..111
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT /id="PRO_0000415397"
FT CHAIN 112..331
FT /note="Cathepsin 7"
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT /id="PRO_0000415398"
FT MOTIF 33..50
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q91ZF2"
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"
SQ SEQUENCE 331 AA; 37868 MW; 280B8F8ADD27E26F CRC64;
MTVAVFLAIL CLRAALAAPR PDYSLDAEWE EWKRNNAKTY SPEEEKQRRA VWEENVKMIK
WHTMQNGLWM NNFTIEMNEF GDMTGEEMRM MTDSSALTLR NGKHIQKRNV KIPKTLDWRD
TGCVAPVRSQ GGCGACWAFS VAASIESQLF KKTGKLIPLS VQNLIDCTVT YGNNDCSGGK
PYTAFQYVKN NGGLEAEATY PYEAKLRHCR YRPERSVVKI ARFFVVPRNE EALMQALVTY
GPIAVAIDGS HASFKRYRGG IYHEPKCRRD TLDHGLLLVG YGYEGHESEN RKYWLLKNSH
GEQWGERGYM KLPRDQNNYC GIASYAMYPL L
