CATW_HUMAN
ID CATW_HUMAN Reviewed; 376 AA.
AC P56202; Q86VT4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cathepsin W;
DE EC=3.4.22.-;
DE AltName: Full=Lymphopain;
DE Flags: Precursor;
GN Name=CTSW;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT GLY-139.
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 [MRNA], AND VARIANT GLY-139.
RX PubMed=9108299; DOI=10.1016/s0014-5793(97)00118-x;
RA Linnevers C., Smeekens S.P., Broemme D.;
RT "Human cathepsin W, a putative cysteine protease predominantly expressed in
RT CD8+ T-lymphocytes.";
RL FEBS Lett. 405:253-259(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-139.
RX PubMed=9675123; DOI=10.1006/bbrc.1998.8954;
RA Wex T., Levy B., Smeekens S.P., Ansorge S., Desnick R.J., Bromme D.;
RT "Genomic structure, chromosomal localization, and expression of human
RT cathepsin W.";
RL Biochem. Biophys. Res. Commun. 248:255-261(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-139.
RC TISSUE=Pancreas;
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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11490002; DOI=10.4049/jimmunol.167.4.2172;
RA Wex T., Buehling F., Wex H., Guenther D., Malfertheiner P., Weber E.,
RA Broemme D.;
RT "Human cathepsin W, a cysteine protease predominantly expressed in NK
RT cells, is mainly localized in the endoplasmic reticulum.";
RL J. Immunol. 167:2172-2178(2001).
RN [7]
RP PROTEIN SEQUENCE OF 22-36.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RX PubMed=26060270; DOI=10.1128/mbio.00297-15;
RA Edinger T.O., Pohl M.O., Yangueez E., Stertz S.;
RT "Cathepsin W Is Required for Escape of Influenza A Virus from Late
RT Endosomes.";
RL MBio 6:E00297-E00297(2015).
CC -!- FUNCTION: May have a specific function in the mechanism or regulation
CC of T-cell cytolytic activity.
CC -!- FUNCTION: (Microbial infection) Plays a role during influenza virus
CC infection in lungs cells ex vivo. Acts at the level of virus entering
CC host cytoplasm from late endosome. {ECO:0000269|PubMed:15340161}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:11490002}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in natural killer cells,
CC and in cytotoxic T cells. {ECO:0000269|PubMed:11490002}.
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; AF013611; AAB82449.1; -; mRNA.
DR EMBL; AF015954; AAB82457.1; -; Genomic_DNA.
DR EMBL; AF055903; AAC32181.1; -; Genomic_DNA.
DR EMBL; AP001201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048255; AAH48255.1; -; mRNA.
DR CCDS; CCDS8117.1; -.
DR RefSeq; NP_001326.2; NM_001335.3.
DR AlphaFoldDB; P56202; -.
DR SMR; P56202; -.
DR BioGRID; 107901; 2.
DR IntAct; P56202; 2.
DR MINT; P56202; -.
DR STRING; 9606.ENSP00000311300; -.
DR MEROPS; C01.037; -.
DR GlyGen; P56202; 2 sites.
DR iPTMnet; P56202; -.
DR PhosphoSitePlus; P56202; -.
DR BioMuta; CTSW; -.
DR DMDM; 259016196; -.
DR EPD; P56202; -.
DR MassIVE; P56202; -.
DR MaxQB; P56202; -.
DR PaxDb; P56202; -.
DR PeptideAtlas; P56202; -.
DR PRIDE; P56202; -.
DR ProteomicsDB; 56904; -.
DR Antibodypedia; 4281; 99 antibodies from 23 providers.
DR DNASU; 1521; -.
DR Ensembl; ENST00000307886.8; ENSP00000311300.3; ENSG00000172543.9.
DR GeneID; 1521; -.
DR KEGG; hsa:1521; -.
DR MANE-Select; ENST00000307886.8; ENSP00000311300.3; NM_001335.4; NP_001326.3.
DR UCSC; uc001ogc.2; human.
DR CTD; 1521; -.
DR DisGeNET; 1521; -.
DR GeneCards; CTSW; -.
DR HGNC; HGNC:2546; CTSW.
DR HPA; ENSG00000172543; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 602364; gene.
DR neXtProt; NX_P56202; -.
DR OpenTargets; ENSG00000172543; -.
DR PharmGKB; PA27042; -.
DR VEuPathDB; HostDB:ENSG00000172543; -.
DR eggNOG; KOG1542; Eukaryota.
DR GeneTree; ENSGT00940000161630; -.
DR HOGENOM; CLU_012184_4_1_1; -.
DR InParanoid; P56202; -.
DR OMA; NTCGITR; -.
DR OrthoDB; 1264766at2759; -.
DR PhylomeDB; P56202; -.
DR TreeFam; TF337736; -.
DR PathwayCommons; P56202; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; P56202; -.
DR BioGRID-ORCS; 1521; 14 hits in 1068 CRISPR screens.
DR ChiTaRS; CTSW; human.
DR GeneWiki; Cathepsin_W; -.
DR GenomeRNAi; 1521; -.
DR Pharos; P56202; Tbio.
DR PRO; PR:P56202; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P56202; protein.
DR Bgee; ENSG00000172543; Expressed in granulocyte and 101 other tissues.
DR ExpressionAtlas; P56202; baseline and differential.
DR Genevisible; P56202; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15340161"
FT PROPEP 22..127
FT /evidence="ECO:0000255"
FT /id="PRO_0000026327"
FT CHAIN 128..376
FT /note="Cathepsin W"
FT /id="PRO_0000026328"
FT ACT_SITE 153
FT /evidence="ECO:0000250"
FT ACT_SITE 291
FT /evidence="ECO:0000250"
FT ACT_SITE 331
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..191
FT /evidence="ECO:0000250"
FT DISULFID 184..226
FT /evidence="ECO:0000250"
FT DISULFID 284..352
FT /evidence="ECO:0000250"
FT VARIANT 139
FT /note="S -> G (in dbSNP:rs604630)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9108299, ECO:0000269|PubMed:9675123,
FT ECO:0000269|PubMed:9823953"
FT /id="VAR_058847"
FT VARIANT 218
FT /note="Q -> R (in dbSNP:rs606830)"
FT /id="VAR_057041"
FT CONFLICT 179
FT /note="Q -> H (in Ref. 1; AAB82449/AAB82457 and 3;
FT AAC32181)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42120 MW; D2956524D17B593A CRC64;
MALTAHPSCL LALLVAGLAQ GIRGPLRAQD LGPQPLELKE AFKLFQIQFN RSYLSPEEHA
HRLDIFAHNL AQAQRLQEED LGTAEFGVTP FSDLTEEEFG QLYGYRRAAG GVPSMGREIR
SEEPEESVPF SCDWRKVASA ISPIKDQKNC NCCWAMAAAG NIETLWRISF WDFVDVSVQE
LLDCGRCGDG CHGGFVWDAF ITVLNNSGLA SEKDYPFQGK VRAHRCHPKK YQKVAWIQDF
IMLQNNEHRI AQYLATYGPI TVTINMKPLQ LYRKGVIKAT PTTCDPQLVD HSVLLVGFGS
VKSEEGIWAE TVSSQSQPQP PHPTPYWILK NSWGAQWGEK GYFRLHRGSN TCGITKFPLT
ARVQKPDMKP RVSCPP
