CATJ_MOUSE
ID CATJ_MOUSE Reviewed; 334 AA.
AC Q9R014; Q564D9; Q91XK6; Q9WV51;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 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 [MRNA], TISSUE SPECIFICITY, AND VARIANT LYS-43 DEL.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=10526153; DOI=10.1016/s0014-5793(99)01263-6;
RA Tisljar K., Deussing J., Peters C.;
RT "Cathepsin J, a novel murine cysteine protease of the papain family with a
RT placenta-restricted expression.";
RL FEBS Lett. 459:299-304(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RA Sol-Church K., Frenck J., Troeber D., Mason R.W.;
RT "Cloning of a mouse cysteine protease.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-43 DEL.
RC STRAIN=129/SvEvTacfBr;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in placenta.
CC {ECO:0000269|PubMed:10526153}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF136272; AAF13142.1; -; mRNA.
DR EMBL; AF158182; AAD41898.1; -; mRNA.
DR EMBL; AY034579; AAK58455.1; -; Genomic_DNA.
DR EMBL; AK005526; BAB24099.1; -; mRNA.
DR EMBL; AK131661; BAE20748.1; -; mRNA.
DR EMBL; BC103769; AAI03770.1; -; mRNA.
DR CCDS; CCDS88467.1; -.
DR RefSeq; NP_036137.1; NM_012007.1.
DR RefSeq; XP_006517318.1; XM_006517255.1.
DR AlphaFoldDB; Q9R014; -.
DR SMR; Q9R014; -.
DR STRING; 10090.ENSMUSP00000071457; -.
DR MEROPS; C01.038; -.
DR GlyGen; Q9R014; 4 sites.
DR PaxDb; Q9R014; -.
DR PeptideAtlas; Q9R014; -.
DR PRIDE; Q9R014; -.
DR ProteomicsDB; 279920; -.
DR DNASU; 26898; -.
DR Ensembl; ENSMUST00000224224; ENSMUSP00000153389; ENSMUSG00000055298.
DR GeneID; 26898; -.
DR KEGG; mmu:26898; -.
DR UCSC; uc007qwa.1; mouse.
DR CTD; 26898; -.
DR MGI; MGI:1349426; Ctsj.
DR VEuPathDB; HostDB:ENSMUSG00000055298; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR InParanoid; Q9R014; -.
DR OMA; TCGSNTQ; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9R014; -.
DR TreeFam; TF313739; -.
DR BRENDA; 3.4.22.B65; 3474.
DR BioGRID-ORCS; 26898; 0 hits in 58 CRISPR screens.
DR PRO; PR:Q9R014; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9R014; protein.
DR Bgee; ENSMUSG00000055298; Expressed in placenta labyrinth and 9 other tissues.
DR ExpressionAtlas; Q9R014; baseline and differential.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0097655; F:serpin family protein binding; ISO:MGI.
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:0016540; P:protein autoprocessing; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO: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: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; 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 /id="PRO_0000026230"
FT CHAIN 114..334
FT /note="Cathepsin J"
FT /id="PRO_0000026231"
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 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 DISULFID 135..178
FT /evidence="ECO:0000250"
FT DISULFID 169..211
FT /evidence="ECO:0000250"
FT DISULFID 269..322
FT /evidence="ECO:0000250"
FT VARIANT 43
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:10526153,
FT ECO:0000269|PubMed:11829493"
SQ SEQUENCE 334 AA; 37276 MW; A422B7679E76DD7C CRC64;
MTPTVLLLIL CFGVASGAQA HDPKLDAEWK DWKTKYAKSY SPKEEALRRA VWEENMRMIK
LHNKENSLGK NNFTMKMNKF GDQTSEEFRK SIDNIPIPAA MTDPHAQNHV SIGLPDYKDW
REEGYVTPVR NQGKCGSCWA FAAAGAIEGQ MFWKTGNLTP LSVQNLLDCS KTVGNKGCQS
GTAHQAFEYV LKNKGLEAEA TYPYEGKDGP CRYRSENASA NITDYVNLPP NELYLWVAVA
SIGPVSAAID ASHDSFRFYN GGIYYEPNCS SYFVNHAVLV VGYGSEGDVK DGNNYWLIKN
SWGEEWGMNG YMQIAKDHNN HCGIASLASY PNIF
