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 24-JAN-2024, entry version 150. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; O46427; 3 sites, No reported glycans. DR PaxDb; 9823-ENSSSCP00000001934; -. DR PeptideAtlas; O46427; -. DR Ensembl; ENSSSCT00000001983.4; ENSSSCP00000001934.1; ENSSSCG00000001770.5. DR Ensembl; ENSSSCT00025104075.1; ENSSSCP00025046196.1; ENSSSCG00025075350.1. DR Ensembl; ENSSSCT00035019633.1; ENSSSCP00035006994.1; ENSSSCG00035015394.1. DR Ensembl; ENSSSCT00045050141.1; ENSSSCP00045034889.1; ENSSSCG00045029217.1. DR Ensembl; ENSSSCT00065041570.1; ENSSSCP00065017623.1; ENSSSCG00065030727.1. 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; 5472948at2759; -. DR TreeFam; TF328985; -. DR Reactome; R-SSC-2132295; MHC class II antigen presentation. DR Reactome; R-SSC-5683826; Surfactant metabolism. DR Reactome; R-SSC-6798695; Neutrophil degranulation. DR SABIO-RK; O46427; -. DR EvolutionaryTrace; O46427; -. DR Proteomes; UP000008227; Chromosome 7. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000001770; Expressed in endocardial endothelium and 40 other cell types or tissues. DR ExpressionAtlas; O46427; baseline and differential. 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:0006955; P:immune response; IBA:GO_Central. 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; IBA:GO_Central. 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 Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A. DR InterPro; IPR000668; Peptidase_C1A_C. DR InterPro; IPR039417; Peptidase_C1A_papain-like. DR InterPro; IPR013201; Prot_inhib_I29. DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1. DR PANTHER; PTHR12411:SF642; PRO-CATHEPSIN H; 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; Cysteine proteinases; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. DR Genevisible; O46427; SS. 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 //