CATJ_RAT
ID CATJ_RAT Reviewed; 334 AA.
AC Q63088; Q920D9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cathepsin J;
DE EC=3.4.22.-;
DE AltName: Full=Cathepsin L-related protein;
DE AltName: Full=Cathepsin P;
DE AltName: Full=Catlrp-p;
DE Flags: Precursor;
GN Name=Ctsj; Synonyms=Ctsp;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Sol-Church K.;
RT "PECs, a multigene family of proteases expressed in rodent placenta.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 97-334, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Placenta;
RX PubMed=7766407; DOI=10.1002/mrd.1080400203;
RA Conliffe P.R., Ogilvie S., Simmen R.C.M., Michel F.J., Saunders P.,
RA Shiverick K.T.;
RT "Cloning and expression of a rat placental cDNA encoding a novel cathepsin
RT L-related protein.";
RL Mol. Reprod. Dev. 40:146-156(1995).
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in placenta.
CC {ECO:0000269|PubMed:7766407}.
CC -!- DEVELOPMENTAL STAGE: Highest expression on 18 dpc.
CC {ECO:0000269|PubMed:7766407}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; AF310623; AAL26793.2; -; mRNA.
DR EMBL; BC097263; AAH97263.1; -; mRNA.
DR EMBL; L14776; AAC42066.1; -; mRNA.
DR PIR; I58002; I58002.
DR RefSeq; NP_058817.1; NM_017121.1.
DR AlphaFoldDB; Q63088; -.
DR SMR; Q63088; -.
DR STRING; 10116.ENSRNOP00000035908; -.
DR ChEMBL; CHEMBL3308940; -.
DR MEROPS; C01.038; -.
DR GlyGen; Q63088; 4 sites.
DR PaxDb; Q63088; -.
DR Ensembl; ENSRNOT00000038758; ENSRNOP00000035908; ENSRNOG00000046476.
DR GeneID; 29174; -.
DR KEGG; rno:29174; -.
DR CTD; 26898; -.
DR RGD; 69241; Ctsj.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q63088; -.
DR OMA; TCGSNTQ; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q63088; -.
DR PRO; PR:Q63088; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Genevisible; Q63088; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
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; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..113
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026232"
FT CHAIN 114..334
FT /note="Cathepsin J"
FT /id="PRO_0000026233"
FT ACT_SITE 138
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /evidence="ECO:0000250"
FT ACT_SITE 300
FT /evidence="ECO:0000250"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 269..322
FT /evidence="ECO:0000250"
FT CONFLICT 97
FT /note="I -> N (in Ref. 3; AAC42066)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..153
FT /note="FS -> SL (in Ref. 3; AAC42066)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..179
FT /note="CSKSEGNNGCR -> TKSEGIGLP (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36783 MW; 7599D47A435A39ED CRC64;
MTPAVFLVIL CFGVASGAPA RDPNLDAEWQ DWKTKYAKSY SPVEEELKRA VWEENLKMIQ
LHNKENGLGK NGFTMEMNAF ADTTGEEFRK SLSDILIPAA VTNPSAQKQV SIGLPNFKDW
RKEGYVTPVR NQGKCGSCWA FAAVGAIEGQ MFSKTGNLTP LSVQNLLDCS KSEGNNGCRW
GTAHQAFNYV LKNKGLEAEA TYPYEGKDGP CRYHSENASA NITGFVNLPP NELYLWVAVA
SIGPVSAAID ASHDSFRFYS GGVYHEPNCS SYVVNHAVLV VGYGFEGNET DGNNYWLIKN
SWGEEWGING FMKIAKDRNN HCGIASQASF PDIF
