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CATO_HUMAN
ID   CATO_HUMAN              Reviewed;         321 AA.
AC   P43234;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Cathepsin O;
DE            EC=3.4.22.42;
DE   Flags: Precursor;
GN   Name=CTSO; Synonyms=CTSO1;
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 [MRNA].
RC   TISSUE=Mammary carcinoma;
RX   PubMed=7929457; DOI=10.1016/s0021-9258(18)47135-9;
RA   Velasco G., Ferrando A.A., Puente X.S., Sanchez L.M., Lopez-Otin C.;
RT   "Human cathepsin O. Molecular cloning from a breast carcinoma, production
RT   of the active enzyme in Escherichia coli, and expression analysis in human
RT   tissues.";
RL   J. Biol. Chem. 269:27136-27142(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   -!- FUNCTION: Proteolytic enzyme possibly involved in normal cellular
CC       protein degradation and turnover.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The recombinant human enzyme hydrolyzes synthetic
CC         endopeptidase substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-
CC         NHMec.; EC=3.4.22.42;
CC   -!- INTERACTION:
CC       P43234; Q92993: KAT5; NbExp=3; IntAct=EBI-2874283, EBI-399080;
CC       P43234; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2874283, EBI-11742507;
CC       P43234; P17252: PRKCA; NbExp=3; IntAct=EBI-2874283, EBI-1383528;
CC       P43234; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2874283, EBI-9090795;
CC       P43234; P61981: YWHAG; NbExp=3; IntAct=EBI-2874283, EBI-359832;
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined. High levels seen
CC       in the ovary, kidney and placenta while low levels seen in thymus and
CC       skeletal muscle.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR   EMBL; X77383; CAA54562.1; -; mRNA.
DR   EMBL; BC049206; AAH49206.1; -; mRNA.
DR   CCDS; CCDS3794.1; -.
DR   PIR; A55090; A55090.
DR   RefSeq; NP_001325.1; NM_001334.2.
DR   AlphaFoldDB; P43234; -.
DR   SMR; P43234; -.
DR   BioGRID; 107899; 21.
DR   IntAct; P43234; 9.
DR   STRING; 9606.ENSP00000414904; -.
DR   MEROPS; C01.035; -.
DR   GlyGen; P43234; 2 sites.
DR   iPTMnet; P43234; -.
DR   PhosphoSitePlus; P43234; -.
DR   BioMuta; CTSO; -.
DR   DMDM; 1168795; -.
DR   EPD; P43234; -.
DR   jPOST; P43234; -.
DR   MassIVE; P43234; -.
DR   PaxDb; P43234; -.
DR   PeptideAtlas; P43234; -.
DR   PRIDE; P43234; -.
DR   ProteomicsDB; 55597; -.
DR   Antibodypedia; 48148; 135 antibodies from 26 providers.
DR   DNASU; 1519; -.
DR   Ensembl; ENST00000433477.4; ENSP00000414904.3; ENSG00000256043.5.
DR   Ensembl; ENST00000573499.1; ENSP00000460395.1; ENSG00000263238.1.
DR   GeneID; 1519; -.
DR   KEGG; hsa:1519; -.
DR   MANE-Select; ENST00000433477.4; ENSP00000414904.3; NM_001334.3; NP_001325.1.
DR   UCSC; uc003ipg.4; human.
DR   CTD; 1519; -.
DR   DisGeNET; 1519; -.
DR   GeneCards; CTSO; -.
DR   HGNC; HGNC:2542; CTSO.
DR   HPA; ENSG00000256043; Low tissue specificity.
DR   MIM; 600550; gene.
DR   neXtProt; NX_P43234; -.
DR   OpenTargets; ENSG00000256043; -.
DR   PharmGKB; PA27040; -.
DR   VEuPathDB; HostDB:ENSG00000256043; -.
DR   eggNOG; KOG1542; Eukaryota.
DR   GeneTree; ENSGT00940000159253; -.
DR   HOGENOM; CLU_012184_1_3_1; -.
DR   InParanoid; P43234; -.
DR   OMA; QNGLCRY; -.
DR   OrthoDB; 1275401at2759; -.
DR   PhylomeDB; P43234; -.
DR   TreeFam; TF331594; -.
DR   PathwayCommons; P43234; -.
DR   Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR   SignaLink; P43234; -.
DR   BioGRID-ORCS; 1519; 9 hits in 1067 CRISPR screens.
DR   ChiTaRS; CTSO; human.
DR   GeneWiki; Cathepsin_O; -.
DR   GenomeRNAi; 1519; -.
DR   Pharos; P43234; Tbio.
DR   PRO; PR:P43234; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P43234; protein.
DR   Bgee; ENSG00000256043; Expressed in calcaneal tendon and 99 other tissues.
DR   Genevisible; P43234; HS.
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:0006508; P:proteolysis; TAS:ProtInc.
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; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW   Reference proteome; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..107
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026321"
FT   CHAIN           108..321
FT                   /note="Cathepsin O"
FT                   /id="PRO_0000026322"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        129..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        163..204
FT                   /evidence="ECO:0000250"
FT   DISULFID        262..310
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  35958 MW;  F48011ECA9E0BC45 CRC64;
     MDVRALPWLP WLLWLLCRGG GDADSRAPFT PTWPRSRERE AAAFRESLNR HRYLNSLFPS
     ENSTAFYGIN QFSYLFPEEF KAIYLRSKPS KFPRYSAEVH MSIPNVSLPL RFDWRDKQVV
     TQVRNQQMCG GCWAFSVVGA VESAYAIKGK PLEDLSVQQV IDCSYNNYGC NGGSTLNALN
     WLNKMQVKLV KDSEYPFKAQ NGLCHYFSGS HSGFSIKGYS AYDFSDQEDE MAKALLTFGP
     LVVIVDAVSW QDYLGGIIQH HCSSGEANHA VLITGFDKTG STPYWIVRNS WGSSWGVDGY
     AHVKMGSNVC GIADSVSSIF V
 
 
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