CATH_RAT
ID CATH_RAT Reviewed; 333 AA.
AC P00786;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Pro-cathepsin H;
DE Contains:
DE RecName: Full=Cathepsin H mini chain;
DE Contains:
DE RecName: Full=Cathepsin H;
DE EC=3.4.22.16;
DE Contains:
DE RecName: Full=Cathepsin H heavy chain;
DE Contains:
DE RecName: Full=Cathepsin H light chain;
DE Flags: Precursor;
GN Name=Ctsh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=3691815; DOI=10.1016/0014-5793(87)80545-8;
RA Ishidoh K., Imajoh S., Emori Y., Ohno S., Kawasaki H., Minami Y.,
RA Kominami E., Katunuma N., Suzuki K.;
RT "Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in
RT pro-peptide regions of cysteine proteinases.";
RL FEBS Lett. 226:33-37(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2759235; DOI=10.1016/0014-5793(89)80939-1;
RA Ishidoh K., Kominami E., Katunuma N., Suzuki K.;
RT "Gene structure of rat cathepsin H.";
RL FEBS Lett. 253:103-107(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-333.
RC TISSUE=Liver;
RX PubMed=2276418; DOI=10.1016/0020-711x(90)90237-w;
RA Qian F., Frankfater A., Miller R.V., Chan S.J., Steiner D.F.;
RT "Molecular cloning of rat precursor cathepsin H and the expression of five
RT lysosomal cathepsins in normal tissues and in a rat carcinosarcoma.";
RL Int. J. Biochem. 22:1457-1464(1990).
RN [5]
RP PROTEIN SEQUENCE OF 114-333.
RC TISSUE=Liver;
RX PubMed=6574504; DOI=10.1073/pnas.80.12.3666;
RA Takio K., Towatari T., Katunuma N., Teller D.C., Titani K.;
RT "Homology of amino acid sequences of rat liver cathepsins B and H with that
RT of papain.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3666-3670(1983).
CC -!- FUNCTION: Important for the overall degradation of proteins in
CC lysosomes.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably,
CC cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
CC -!- SUBUNIT: Composed of a mini chain and a large chain. The large chain
CC may be split into heavy and light chain. All chains are held together
CC by disulfide bonds.
CC -!- SUBCELLULAR LOCATION: Lysosome.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA63484.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y00708; CAA68699.1; -; mRNA.
DR EMBL; BC085352; AAH85352.1; -; mRNA.
DR EMBL; M38135; AAA63484.1; ALT_INIT; mRNA.
DR PIR; S00211; KHRTH.
DR RefSeq; NP_037071.1; NM_012939.1.
DR RefSeq; XP_008764662.1; XM_008766440.2.
DR AlphaFoldDB; P00786; -.
DR SMR; P00786; -.
DR STRING; 10116.ENSRNOP00000019285; -.
DR BindingDB; P00786; -.
DR ChEMBL; CHEMBL3308952; -.
DR MEROPS; C01.040; -.
DR MEROPS; I29.003; -.
DR GlyGen; P00786; 1 site.
DR iPTMnet; P00786; -.
DR PhosphoSitePlus; P00786; -.
DR PaxDb; P00786; -.
DR PRIDE; P00786; -.
DR Ensembl; ENSRNOT00000019285; ENSRNOP00000019285; ENSRNOG00000014064.
DR GeneID; 25425; -.
DR KEGG; rno:25425; -.
DR UCSC; RGD:2447; rat.
DR CTD; 1512; -.
DR RGD; 2447; Ctsh.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000160227; -.
DR HOGENOM; CLU_012184_1_1_1; -.
DR InParanoid; P00786; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; P00786; -.
DR TreeFam; TF328985; -.
DR BRENDA; 3.4.22.16; 5301.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P00786; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Genevisible; P00786; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0097208; C:alveolar lamellar body; IDA:RGD.
DR GO; GO:0005930; C:axoneme; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0001520; C:outer dense fiber; IDA:RGD.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:RGD.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:RGD.
DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR GO; GO:0030108; F:HLA-A specific activating MHC class I receptor activity; ISS:UniProtKB.
DR GO; GO:0030984; F:kininogen binding; IPI:RGD.
DR GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0043621; F:protein self-association; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; ISO:RGD.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:UniProtKB.
DR GO; GO:0060448; P:dichotomous subdivision of terminal units involved in lung branching; ISS:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0002764; P:immune response-regulating signaling pathway; ISS:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; ISS:UniProtKB.
DR GO; GO:0001656; P:metanephros development; IEP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010813; P:neuropeptide catabolic process; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0010952; P:positive regulation of peptidase activity; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:1990834; P:response to odorant; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0043129; P:surfactant homeostasis; ISS:UniProtKB.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Protease; Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..95
FT /note="Activation peptide"
FT /id="PRO_0000026224"
FT CHAIN 96..103
FT /note="Cathepsin H mini chain"
FT /id="PRO_0000026225"
FT PROPEP 104..113
FT /evidence="ECO:0000255"
FT /id="PRO_0000026226"
FT CHAIN 114..333
FT /note="Cathepsin H"
FT /id="PRO_0000026227"
FT CHAIN 114..290
FT /note="Cathepsin H heavy chain"
FT /id="PRO_0000026228"
FT CHAIN 291..333
FT /note="Cathepsin H light chain"
FT /id="PRO_0000026229"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /evidence="ECO:0000250"
FT ACT_SITE 299
FT /evidence="ECO:0000250"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6574504"
FT DISULFID 100..325
FT /evidence="ECO:0000250"
FT DISULFID 136..179
FT /evidence="ECO:0000250"
FT DISULFID 170..212
FT /evidence="ECO:0000250"
FT DISULFID 270..320
FT /evidence="ECO:0000250"
FT VARIANT 287
FT /note="G -> A"
SQ SEQUENCE 333 AA; 37104 MW; A90AC66338F0B744 CRC64;
MWTALPLLCA GAWLLSAGAT AELTVNAIEK FHFTSWMKQH QKTYSSREYS HRLQVFANNW
RKIQAHNQRN HTFKMGLNQF SDMSFAEIKH KYLWSEPQNC SATKSNYLRG TGPYPSSMDW
RKKGNVVSPV KNQGACGSCW TFSTTGALES AVAIASGKMM TLAEQQLVDC AQNFNNHGCQ
GGLPSQAFEY ILYNKGIMGE DSYPYIGKNG QCKFNPEKAV AFVKNVVNIT LNDEAAMVEA
VALYNPVSFA FEVTEDFMMY KSGVYSSNSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS
WGSNWGNNGY FLIERGKNMC GLAACASYPI PQV
