CATH_PIG
ID CATH_PIG Reviewed; 335 AA.
AC O46427;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RC TISSUE=Peripheral blood, and Spleen;
RX PubMed=9493267; DOI=10.1016/s0969-2126(98)00007-0;
RA Guncar G., Podobnik M., Pungercar J., Strukelj B., Turk V., Turk D.;
RT "Crystal structure of porcine cathepsin H determined at 2.1-A resolution:
RT location of the mini-chain C-terminal carboxyl group defines cathepsin H
RT aminopeptidase function.";
RL Structure 6:51-61(1998).
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 cathepsin H and mini chain; disulfide-linked.
CC Cathepsin H may be split into heavy and light chain. All chains are
CC held together 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}.
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DR EMBL; AF001169; AAB93957.1; -; mRNA.
DR RefSeq; NP_999094.1; NM_213929.2.
DR PDB; 1NB3; X-ray; 2.80 A; A/B/C/D=116-334, P/R/S/T=98-105.
DR PDB; 1NB5; X-ray; 2.40 A; A/B/C/D=116-334, P/R/S/T=98-105.
DR PDB; 8PCH; X-ray; 2.10 A; A=116-334, P=98-105.
DR PDBsum; 1NB3; -.
DR PDBsum; 1NB5; -.
DR PDBsum; 8PCH; -.
DR AlphaFoldDB; O46427; -.
DR SMR; O46427; -.
DR IntAct; O46427; 2.
DR STRING; 9823.ENSSSCP00000001934; -.
DR MEROPS; C01.040; -.
DR PaxDb; O46427; -.
DR PeptideAtlas; O46427; -.
DR Ensembl; ENSSSCT00000001983; ENSSSCP00000001934; ENSSSCG00000001770.
DR Ensembl; ENSSSCT00025104075; ENSSSCP00025046196; ENSSSCG00025075350.
DR Ensembl; ENSSSCT00035019633; ENSSSCP00035006994; ENSSSCG00035015394.
DR Ensembl; ENSSSCT00045050141; ENSSSCP00045034889; ENSSSCG00045029217.
DR Ensembl; ENSSSCT00065041570; ENSSSCP00065017623; ENSSSCG00065030727.
DR GeneID; 396969; -.
DR KEGG; ssc:396969; -.
DR CTD; 1512; -.
DR VGNC; VGNC:87077; CTSH.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000160227; -.
DR HOGENOM; CLU_012184_1_1_1; -.
DR InParanoid; O46427; -.
DR OMA; AYNNFGC; -.
DR OrthoDB; 1275401at2759; -.
DR TreeFam; TF328985; -.
DR Reactome; R-SSC-2132295; MHC class II antigen presentation.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR SABIO-RK; O46427; -.
DR EvolutionaryTrace; O46427; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000001770; Expressed in endocardial endothelium and 40 other tissues.
DR ExpressionAtlas; O46427; baseline and differential.
DR Genevisible; O46427; SS.
DR GO; GO:0097208; C:alveolar lamellar body; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0030108; F:HLA-A specific activating MHC class I receptor activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
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; ISS: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; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
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 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..97
FT /evidence="ECO:0000255"
FT /id="PRO_0000026218"
FT PEPTIDE 98..105
FT /note="Cathepsin H mini chain"
FT /id="PRO_0000026219"
FT PROPEP 107..115
FT /id="PRO_0000026220"
FT CHAIN 116..335
FT /note="Cathepsin H"
FT /id="PRO_0000026221"
FT CHAIN 116..292
FT /note="Cathepsin H heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026222"
FT CHAIN 293..335
FT /note="Cathepsin H light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026223"
FT ACT_SITE 141
FT ACT_SITE 281
FT ACT_SITE 301
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..327
FT DISULFID 138..181
FT DISULFID 172..214
FT DISULFID 272..322
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:8PCH"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:8PCH"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:8PCH"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:8PCH"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:8PCH"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:8PCH"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:8PCH"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:8PCH"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:8PCH"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1NB5"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:8PCH"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:1NB3"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:8PCH"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:8PCH"
SQ SEQUENCE 335 AA; 37455 MW; F728EB45292C3B55 CRC64;
MWAVLSLLCA GAWLLGPPAC GASNLAVSSF EKLHFKSWMV QHQKKYSLEE YHHRLQVFVS
NWRKINAHNA GNHTFKLGLN QFSDMSFDEI RHKYLWSEPQ NCSATKGNYL RGTGPYPPSM
DWRKKGNFVS PVKNQGSCGS CWTFSTTGAL ESAVAIATGK MLSLAEQQLV DCAQNFNNHG
CQGGLPSQAF EYIRYNKGIM GEDTYPYKGQ DDHCKFQPDK AIAFVKDVAN ITMNDEEAMV
EAVALYNPVS FAFEVTNDFL MYRKGIYSST SCHKTPDKVN HAVLAVGYGE ENGIPYWIVK
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV
