CATR_MOUSE
ID CATR_MOUSE Reviewed; 334 AA.
AC Q9JIA9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cathepsin R;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=Ctsr; Synonyms=Catr;
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 DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=11004518; DOI=10.1016/s0167-4781(00)00114-7;
RA Sol-Church K., Frenck J., Bertenshaw G., Mason R.W.;
RT "Characterization of mouse cathepsin R, a new member of a family of
RT placentally expressed cysteine proteases (PECs).";
RL Biochim. Biophys. Acta 1492:488-492(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, and 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).
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Placenta. {ECO:0000269|PubMed:11004518}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult but not in embryo.
CC {ECO:0000269|PubMed:11004518}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; AF245399; AAF90051.1; -; mRNA.
DR EMBL; AY014778; AAK00507.1; -; mRNA.
DR EMBL; AK014432; BAB29345.1; -; mRNA.
DR EMBL; AK005429; BAB24023.1; -; mRNA.
DR CCDS; CCDS26585.1; -.
DR RefSeq; NP_064680.1; NM_020284.1.
DR AlphaFoldDB; Q9JIA9; -.
DR SMR; Q9JIA9; -.
DR STRING; 10090.ENSMUSP00000021889; -.
DR MEROPS; C01.042; -.
DR GlyGen; Q9JIA9; 1 site.
DR PaxDb; Q9JIA9; -.
DR PRIDE; Q9JIA9; -.
DR DNASU; 56835; -.
DR Ensembl; ENSMUST00000021889; ENSMUSP00000021889; ENSMUSG00000055679.
DR GeneID; 56835; -.
DR KEGG; mmu:56835; -.
DR UCSC; uc007qwe.1; mouse.
DR CTD; 56835; -.
DR MGI; MGI:1861723; Ctsr.
DR VEuPathDB; HostDB:ENSMUSG00000055679; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q9JIA9; -.
DR OMA; WETYKLE; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9JIA9; -.
DR TreeFam; TF313739; -.
DR BioGRID-ORCS; 56835; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ctsr; mouse.
DR PRO; PR:Q9JIA9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JIA9; protein.
DR Bgee; ENSMUSG00000055679; Expressed in placenta labyrinth and 14 other tissues.
DR ExpressionAtlas; Q9JIA9; baseline and differential.
DR Genevisible; Q9JIA9; MM.
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; ISA:MGI.
DR GO; GO:0005771; C:multivesicular body; 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; ISA: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:0030163; P:protein catabolic process; ISA: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; IPR033160; Cathepsin_R.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_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 PANTHER; PTHR12411:SF141; PTHR12411:SF141; 1.
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; 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..114
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026283"
FT CHAIN 115..334
FT /note="Cathepsin R"
FT /id="PRO_0000026284"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /evidence="ECO:0000250"
FT ACT_SITE 301
FT /evidence="ECO:0000250"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 136..179
FT /evidence="ECO:0000250"
FT DISULFID 170..212
FT /evidence="ECO:0000250"
FT DISULFID 270..323
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 37421 MW; D1F6F1953EF4B23D CRC64;
MAAVVFIAFL YLGVASGVPV LDSSLDAEWQ DWKIKYNKSY SLKEEKLKRV VWEEKLKMIK
LHNRENSLGK NGFTMKMNEF GDQTDEEFRK MMIEISVWTH REGKSIMKRE AGSILPKFVD
WRKKGYVTPV RRQGDCDACW AFAVTGAIEA QAIWQTGKLT PLSVQNLVDC SKPQGNNGCL
GGDTYNAFQY VLHNGGLESE ATYPYEGKDG PCRYNPKNSK AEITGFVSLP QSEDILMAAV
ATIGPITAGI DASHESFKNY KGGIYHEPNC SSDTVTHGVL VVGYGFKGIE TDGNHYWLIK
NSWGKRWGIR GYMKLAKDKN NHCGIASYAH YPTI
