HEPS_PONAB
ID HEPS_PONAB Reviewed; 417 AA.
AC Q5R5E8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Serine protease hepsin;
DE EC=3.4.21.106;
DE AltName: Full=Transmembrane protease serine 1;
DE Contains:
DE RecName: Full=Serine protease hepsin non-catalytic chain;
DE Contains:
DE RecName: Full=Serine protease hepsin catalytic chain;
GN Name=HPN; Synonyms=TMPRSS1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an essential role in cell growth and maintenance of
CC cell morphology. May mediate the activating cleavage of HGF and
CC MST1/HGFL. Plays a role in the proteolytic processing of ACE2 (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage after basic amino-acid residues, with Arg strongly
CC preferred to Lys.; EC=3.4.21.106;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; CR860913; CAH93018.1; -; mRNA.
DR RefSeq; NP_001126784.1; NM_001133312.1.
DR AlphaFoldDB; Q5R5E8; -.
DR SMR; Q5R5E8; -.
DR STRING; 9601.ENSPPYP00000011026; -.
DR MEROPS; S01.224; -.
DR GeneID; 100173788; -.
DR KEGG; pon:100173788; -.
DR CTD; 3249; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5R5E8; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0034769; P:basement membrane disassembly; ISS:UniProtKB.
DR GO; GO:0090103; P:cochlea morphogenesis; ISS:UniProtKB.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0097195; P:pilomotor reflex; ISS:UniProtKB.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; ISS:UniProtKB.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISS:UniProtKB.
DR GO; GO:2000611; P:positive regulation of thyroid hormone generation; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0097066; P:response to thyroid hormone; ISS:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.10.250.10; -; 1.
DR InterPro; IPR038957; Hepsin.
DR InterPro; IPR015352; Hepsin-SRCR_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24253:SF38; PTHR24253:SF38; 1.
DR Pfam; PF09272; Hepsin-SRCR; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..162
FT /note="Serine protease hepsin non-catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000285878"
FT CHAIN 163..417
FT /note="Serine protease hepsin catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000285879"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 54..151
FT /note="SRCR"
FT DOMAIN 163..405
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 257
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 353
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 90..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 119..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 153..277
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 188..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 291..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 322..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 349..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 417 AA; 45025 MW; BF879F6634DF4A4D CRC64;
MAQKEGGRTV PCCSRPKVAA LTAGTLLLLT AIGAASWAIV AVLLRSDQEP LYPVQVSSAD
ARLMVFDKTE GTWRLLCSSR SNARVAGLSC VEMGFLRALT HSELDVRTAG ANGTSGFFCV
DEGRLPHTQR LLEVISVCDC PRGRFLATIC QDCGRRKLPV DRIVGGRDTS LGRWPWQVSL
RYDGAHLCGG SLLSGDWVLT AAHCFPERNR VLSRWRVFAG AVAQASPHGL QLAVQAVVYH
GGYLPFRDPN SEENSNDIAL VHLSSPLPLT EYIQPVCLPA AGQALVDGKI CTVTGWGNTQ
YYGQQAGVLQ EARVPIISND VCNGADFYGN QIKPKMFCAG YPEGGIDACQ GDSGGPFVCE
DSISRTPRWR LCGIVSWGTG CALAQKPGVY TKVSDFREWI FQAIKTHSEA SGMVTQL
