HEPS_HUMAN
ID HEPS_HUMAN Reviewed; 417 AA.
AC P05981; B2RDS4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Serine protease hepsin;
DE EC=3.4.21.106 {ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933, ECO:0000305|PubMed:26673890};
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 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=Liver;
RX PubMed=2835076; DOI=10.1021/bi00403a032;
RA Leytus S.P., Loeb K.R., Hagen F.S., Kurachi K., Davie E.W.;
RT "A novel trypsin-like serine protease (hepsin) with a putative
RT transmembrane domain expressed by human liver and hepatoma cells.";
RL Biochemistry 27:1067-1074(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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 SUBCELLULAR LOCATION.
RX PubMed=1885621; DOI=10.1016/s0021-9258(18)55395-3;
RA Tsuji A., Torres-Rosado A., Arai T., le Beau M.M., Lemons R.S., Chou S.H.,
RA Kurachi K.;
RT "Hepsin, a cell membrane-associated protease. Characterization, tissue
RT distribution, and gene localization.";
RL J. Biol. Chem. 266:16948-16953(1991).
RN [5]
RP FUNCTION.
RX PubMed=8346233; DOI=10.1073/pnas.90.15.7181;
RA Torres-Rosado A., O'Shea K.S., Tsuji A., Chou S.-H., Kurachi K.;
RT "Hepsin, a putative cell-surface serine protease, is required for mammalian
RT cell growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7181-7185(1993).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=21875933; DOI=10.1158/1541-7786.mcr-11-0004;
RA Ganesan R., Kolumam G.A., Lin S.J., Xie M.H., Santell L., Wu T.D.,
RA Lazarus R.A., Chaudhuri A., Kirchhofer D.;
RT "Proteolytic activation of pro-macrophage-stimulating protein by hepsin.";
RL Mol. Cancer Res. 9:1175-1186(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP FUNCTION.
RX PubMed=24227843; DOI=10.1128/jvi.02202-13;
RA Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O.,
RA Poehlmann S.;
RT "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by
RT TMPRSS2 augments entry driven by the severe acute respiratory syndrome
RT coronavirus spike protein.";
RL J. Virol. 88:1293-1307(2014).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=26673890; DOI=10.7554/elife.08887;
RA Brunati M., Perucca S., Han L., Cattaneo A., Consolato F., Andolfo A.,
RA Schaeffer C., Olinger E., Peng J., Santambrogio S., Perrier R., Li S.,
RA Bokhove M., Bachi A., Hummler E., Devuyst O., Wu Q., Jovine L.,
RA Rampoldi L.;
RT "The serine protease hepsin mediates urinary secretion and polymerisation
RT of Zona Pellucida domain protein uromodulin.";
RL Elife 4:0-0(2015).
RN [11] {ECO:0007744|PDB:1P57}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 46-417, DISULFIDE BONDS, ACTIVE
RP SITE, AND DOMAIN.
RX PubMed=12962630; DOI=10.1016/s0969-2126(03)00148-5;
RA Somoza J.R., Ho J.D., Luong C., Ghate M., Sprengeler P.A., Mortara K.,
RA Shrader W.D., Sperandio D., Chan H., McGrath M.E., Katz B.A.;
RT "The structure of the extracellular region of human hepsin reveals a serine
RT protease domain and a novel scavenger receptor cysteine-rich (SRCR)
RT domain.";
RL Structure 11:1123-1131(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 46-417, DISULFIDE BONDS,
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=15839837; DOI=10.1042/bj20041955;
RA Herter S., Piper D.E., Aaron W., Gabriele T., Cutler G., Cao P.,
RA Bhatt A.S., Choe Y., Craik C.S., Walker N., Meininger D., Hoey T.,
RA Austin R.J.;
RT "Hepatocyte growth factor is a preferred in vitro substrate for human
RT hepsin, a membrane-anchored serine protease implicated in prostate and
RT ovarian cancers.";
RL Biochem. J. 390:125-136(2005).
CC -!- FUNCTION: Serine protease that cleaves extracellular substrates, and
CC contributes to the proteolytic processing of growth factors, such as
CC HGF and MST1/HGFL (PubMed:21875933, PubMed:15839837). Plays a role in
CC cell growth and maintenance of cell morphology (PubMed:8346233,
CC PubMed:21875933). Plays a role in the proteolytic processing of ACE2
CC (PubMed:24227843). Mediates the proteolytic cleavage of urinary UMOD
CC that is required for UMOD polymerization (PubMed:26673890).
CC {ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933,
CC ECO:0000269|PubMed:24227843, ECO:0000269|PubMed:26673890,
CC ECO:0000269|PubMed:8346233}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage after basic amino-acid residues, with Arg strongly
CC preferred to Lys.; EC=3.4.21.106;
CC Evidence={ECO:0000269|PubMed:15839837, ECO:0000269|PubMed:21875933,
CC ECO:0000305|PubMed:26673890};
CC -!- INTERACTION:
CC P05981; Q12983: BNIP3; NbExp=3; IntAct=EBI-12816745, EBI-749464;
CC P05981; P11686: SFTPC; NbExp=3; IntAct=EBI-12816745, EBI-10197617;
CC P05981; O00526: UPK2; NbExp=3; IntAct=EBI-12816745, EBI-10179682;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1885621};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:1885621}.
CC Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in liver and kidney.
CC {ECO:0000269|PubMed:21875933}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; M18930; AAA36013.1; -; mRNA.
DR EMBL; X07732; CAA30558.1; -; mRNA.
DR EMBL; X07002; CAA30058.1; -; mRNA.
DR EMBL; AK315655; BAG38021.1; -; mRNA.
DR EMBL; BC025716; AAH25716.1; -; mRNA.
DR CCDS; CCDS32993.1; -.
DR PIR; S00845; S00845.
DR RefSeq; NP_002142.1; NM_002151.2.
DR RefSeq; NP_892028.1; NM_182983.2.
DR RefSeq; XP_005258895.2; XM_005258838.4.
DR RefSeq; XP_006723244.2; XM_006723181.3.
DR RefSeq; XP_016882220.1; XM_017026731.1.
DR PDB; 1O5E; X-ray; 1.75 A; H=163-417, L=46-159.
DR PDB; 1O5F; X-ray; 1.78 A; H=163-417, L=46-159.
DR PDB; 1P57; X-ray; 1.75 A; A=46-159, B=163-417.
DR PDB; 1Z8G; X-ray; 1.55 A; A=46-417.
DR PDB; 3T2N; X-ray; 2.55 A; A/B=46-417.
DR PDB; 5CE1; X-ray; 2.50 A; A=46-417.
DR PDBsum; 1O5E; -.
DR PDBsum; 1O5F; -.
DR PDBsum; 1P57; -.
DR PDBsum; 1Z8G; -.
DR PDBsum; 3T2N; -.
DR PDBsum; 5CE1; -.
DR AlphaFoldDB; P05981; -.
DR SMR; P05981; -.
DR BioGRID; 109486; 116.
DR IntAct; P05981; 3.
DR STRING; 9606.ENSP00000262626; -.
DR BindingDB; P05981; -.
DR ChEMBL; CHEMBL2079849; -.
DR DrugBank; DB03865; 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine.
DR DrugBank; DB00522; Bentiromide.
DR DrugBank; DB03297; Benzylsulfonic acid.
DR DrugBank; DB03643; CRA_1144.
DR DrugCentral; P05981; -.
DR MEROPS; S01.224; -.
DR TCDB; 8.A.131.1.12; the transmembrane protease serine 3 (tmprss3) family.
DR GlyGen; P05981; 1 site.
DR iPTMnet; P05981; -.
DR PhosphoSitePlus; P05981; -.
DR BioMuta; HPN; -.
DR DMDM; 123057; -.
DR EPD; P05981; -.
DR jPOST; P05981; -.
DR MassIVE; P05981; -.
DR MaxQB; P05981; -.
DR PaxDb; P05981; -.
DR PeptideAtlas; P05981; -.
DR PRIDE; P05981; -.
DR ProteomicsDB; 51865; -.
DR ABCD; P05981; 2 sequenced antibodies.
DR Antibodypedia; 1718; 185 antibodies from 33 providers.
DR DNASU; 3249; -.
DR Ensembl; ENST00000262626.6; ENSP00000262626.2; ENSG00000105707.15.
DR Ensembl; ENST00000392226.5; ENSP00000376060.1; ENSG00000105707.15.
DR Ensembl; ENST00000672452.2; ENSP00000500664.1; ENSG00000105707.15.
DR Ensembl; ENST00000673426.1; ENSP00000500909.1; ENSG00000105707.15.
DR GeneID; 3249; -.
DR KEGG; hsa:3249; -.
DR MANE-Select; ENST00000672452.2; ENSP00000500664.1; NM_001384133.1; NP_001371062.1.
DR UCSC; uc002nxq.3; human.
DR CTD; 3249; -.
DR DisGeNET; 3249; -.
DR GeneCards; HPN; -.
DR HGNC; HGNC:5155; HPN.
DR HPA; ENSG00000105707; Tissue enhanced (kidney, liver, pancreas).
DR MIM; 142440; gene.
DR neXtProt; NX_P05981; -.
DR OpenTargets; ENSG00000105707; -.
DR PharmGKB; PA29425; -.
DR VEuPathDB; HostDB:ENSG00000105707; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159697; -.
DR HOGENOM; CLU_006842_19_2_1; -.
DR InParanoid; P05981; -.
DR OMA; GQTVPCC; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P05981; -.
DR TreeFam; TF351678; -.
DR BRENDA; 3.4.21.106; 2681.
DR PathwayCommons; P05981; -.
DR Reactome; R-HSA-6806942; MET Receptor Activation.
DR Reactome; R-HSA-8852405; Signaling by MST1.
DR SignaLink; P05981; -.
DR SIGNOR; P05981; -.
DR BioGRID-ORCS; 3249; 18 hits in 1079 CRISPR screens.
DR ChiTaRS; HPN; human.
DR EvolutionaryTrace; P05981; -.
DR GeneWiki; HPN_(gene); -.
DR GenomeRNAi; 3249; -.
DR Pharos; P05981; Tchem.
DR PRO; PR:P05981; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P05981; protein.
DR Bgee; ENSG00000105707; Expressed in right lobe of liver and 110 other tissues.
DR ExpressionAtlas; P05981; baseline and differential.
DR Genevisible; P05981; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0034769; P:basement membrane disassembly; IDA: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; IDA:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0097195; P:pilomotor reflex; ISS:UniProtKB.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IDA:UniProtKB.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IDA: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; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP: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; IPR017448; SRCR-like_dom.
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; SM00202; SR; 1.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW Membrane; Protease; Reference proteome; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..162
FT /note="Serine protease hepsin non-catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027841"
FT CHAIN 163..417
FT /note="Serine protease hepsin catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027842"
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:0000305|PubMed:12962630,
FT ECO:0000305|PubMed:15839837"
FT ACT_SITE 257
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:12962630,
FT ECO:0000305|PubMed:15839837"
FT ACT_SITE 353
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:12962630,
FT ECO:0000305|PubMed:15839837"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 77..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:12962630, ECO:0000269|PubMed:15839837,
FT ECO:0007744|PDB:1O5E, ECO:0007744|PDB:1O5F,
FT ECO:0007744|PDB:1P57, ECO:0007744|PDB:1Z8G"
FT DISULFID 90..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:12962630, ECO:0000269|PubMed:15839837,
FT ECO:0007744|PDB:1O5E, ECO:0007744|PDB:1O5F,
FT ECO:0007744|PDB:1P57, ECO:0007744|PDB:1Z8G"
FT DISULFID 119..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:12962630, ECO:0000269|PubMed:15839837,
FT ECO:0007744|PDB:1O5E, ECO:0007744|PDB:1O5F,
FT ECO:0007744|PDB:1P57, ECO:0007744|PDB:1Z8G"
FT DISULFID 153..277
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:12962630, ECO:0000269|PubMed:15839837,
FT ECO:0007744|PDB:1O5E, ECO:0007744|PDB:1O5F,
FT ECO:0007744|PDB:1P57, ECO:0007744|PDB:1Z8G"
FT DISULFID 188..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:12962630, ECO:0000269|PubMed:15839837,
FT ECO:0007744|PDB:1O5E, ECO:0007744|PDB:1O5F,
FT ECO:0007744|PDB:1P57, ECO:0007744|PDB:1Z8G"
FT DISULFID 291..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:12962630, ECO:0000269|PubMed:15839837,
FT ECO:0007744|PDB:1O5E, ECO:0007744|PDB:1O5F,
FT ECO:0007744|PDB:1P57, ECO:0007744|PDB:1Z8G"
FT DISULFID 322..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:12962630, ECO:0000269|PubMed:15839837,
FT ECO:0007744|PDB:1O5E, ECO:0007744|PDB:1O5F,
FT ECO:0007744|PDB:1P57, ECO:0007744|PDB:1Z8G"
FT DISULFID 349..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:12962630, ECO:0000269|PubMed:15839837,
FT ECO:0007744|PDB:1O5E, ECO:0007744|PDB:1O5F,
FT ECO:0007744|PDB:1P57, ECO:0007744|PDB:1Z8G"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1Z8G"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1Z8G"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1Z8G"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 185..200
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 290..300
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:1Z8G"
FT TURN 325..330
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1O5E"
FT TURN 350..354
FT /evidence="ECO:0007829|PDB:5CE1"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 368..382
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:1Z8G"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:1Z8G"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:1Z8G"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:1Z8G"
SQ SEQUENCE 417 AA; 45011 MW; B2086FF661E551D7 CRC64;
MAQKEGGRTV PCCSRPKVAA LTAGTLLLLT AIGAASWAIV AVLLRSDQEP LYPVQVSSAD
ARLMVFDKTE GTWRLLCSSR SNARVAGLSC EEMGFLRALT HSELDVRTAG ANGTSGFFCV
DEGRLPHTQR LLEVISVCDC PRGRFLAAIC QDCGRRKLPV DRIVGGRDTS LGRWPWQVSL
RYDGAHLCGG SLLSGDWVLT AAHCFPERNR VLSRWRVFAG AVAQASPHGL QLGVQAVVYH
GGYLPFRDPN SEENSNDIAL VHLSSPLPLT EYIQPVCLPA AGQALVDGKI CTVTGWGNTQ
YYGQQAGVLQ EARVPIISND VCNGADFYGN QIKPKMFCAG YPEGGIDACQ GDSGGPFVCE
DSISRTPRWR LCGIVSWGTG CALAQKPGVY TKVSDFREWI FQAIKTHSEA SGMVTQL
