CATW_MOUSE
ID CATW_MOUSE Reviewed; 371 AA.
AC P56203;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cathepsin W;
DE EC=3.4.22.-;
DE AltName: Full=Lymphopain;
DE Flags: Precursor;
GN Name=Ctsw;
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].
RX PubMed=9823953; DOI=10.1038/sj.leu.2401164;
RA Brown J., Matutes E., Singleton A., Price C., Molgaard H., Buttle D.,
RA Enver T.;
RT "Lymphopain, a cytotoxic T and natural killer cell-associated cysteine
RT proteinase.";
RL Leukemia 12:1771-1781(1998).
RN [2]
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).
CC -!- FUNCTION: May have a specific function in the mechanism or regulation
CC of T-cell cytolytic activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P56202}.
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; AF014941; AAB82455.1; -; mRNA.
DR EMBL; AC122861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS29465.1; -.
DR RefSeq; NP_034115.2; NM_009985.5.
DR AlphaFoldDB; P56203; -.
DR SMR; P56203; -.
DR BioGRID; 198977; 1.
DR STRING; 10090.ENSMUSP00000025844; -.
DR MEROPS; C01.037; -.
DR GlyGen; P56203; 4 sites.
DR PhosphoSitePlus; P56203; -.
DR EPD; P56203; -.
DR PaxDb; P56203; -.
DR PRIDE; P56203; -.
DR ProteomicsDB; 279924; -.
DR Antibodypedia; 4281; 99 antibodies from 23 providers.
DR DNASU; 13041; -.
DR Ensembl; ENSMUST00000025844; ENSMUSP00000025844; ENSMUSG00000024910.
DR GeneID; 13041; -.
DR KEGG; mmu:13041; -.
DR UCSC; uc008gdk.2; mouse.
DR CTD; 1521; -.
DR MGI; MGI:1338045; Ctsw.
DR VEuPathDB; HostDB:ENSMUSG00000024910; -.
DR eggNOG; KOG1542; Eukaryota.
DR GeneTree; ENSGT00940000161630; -.
DR HOGENOM; CLU_012184_4_1_1; -.
DR InParanoid; P56203; -.
DR OMA; NTCGITR; -.
DR OrthoDB; 1264766at2759; -.
DR PhylomeDB; P56203; -.
DR TreeFam; TF337736; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 13041; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Ctsw; mouse.
DR PRO; PR:P56203; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P56203; protein.
DR Bgee; ENSMUSG00000024910; Expressed in peripheral lymph node and 80 other tissues.
DR ExpressionAtlas; P56203; baseline and differential.
DR Genevisible; P56203; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR033158; Cathepsin_W.
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:SF101; PTHR12411:SF101; 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; Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..125
FT /evidence="ECO:0000255"
FT /id="PRO_0000026329"
FT CHAIN 126..371
FT /note="Cathepsin W"
FT /id="PRO_0000026330"
FT ACT_SITE 151
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT ACT_SITE 326
FT /evidence="ECO:0000250"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 148..189
FT /evidence="ECO:0000250"
FT DISULFID 182..224
FT /evidence="ECO:0000250"
FT DISULFID 282..347
FT /evidence="ECO:0000250"
SQ SEQUENCE 371 AA; 42120 MW; 1192C3D0C607DDB7 CRC64;
MTLTAHLSYF LVLLLAGQGL SDSLLTKDAG PRPLELKEVF KLFQIRFNRS YWNPAEYTRR
LSIFAHNLAQ AQRLQQEDLG TAEFGETPFS DLTEEEFGQL YGQERSPERT PNMTKKVESN
TWGESVPRTC DWRKAKNIIS SVKNQGSCKC CWAMAAADNI QALWRIKHQQ FVDVSVQELL
DCERCGNGCN GGFVWDAYLT VLNNSGLASE KDYPFQGDRK PHRCLAKKYK KVAWIQDFTM
LSNNEQAIAH YLAVHGPITV TINMKLLQHY QKGVIKATPS SCDPRQVDHS VLLVGFGKEK
EGMQTGTVLS HSRKRRHSSP YWILKNSWGA HWGEKGYFRL YRGNNTCGVT KYPFTAQVDS
PVKKARTSCP P
