ID TMPS4_HUMAN Reviewed; 437 AA.
AC Q9NRS4; A8MU84; B0YJB0; B7Z8C5; E7ERX8; Q5XKQ6; Q6UX37; Q9NZA5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 24-JUL-2024, entry version 204.
DE RecName: Full=Transmembrane protease serine 4 {ECO:0000305};
DE EC=3.4.21.-;
DE AltName: Full=Channel-activating protease 2;
DE Short=CAPH2;
DE AltName: Full=Membrane-type serine protease 2;
DE Short=MT-SP2;
DE Contains:
DE RecName: Full=Transmembrane protease serine 4 catalytic chain;
GN Name=TMPRSS4 {ECO:0000312|HGNC:HGNC:11878};
GN Synonyms=TMPRSS3 {ECO:0000303|PubMed:10825129}; ORFNames=UNQ776/PRO1570;
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] (ISOFORM 1), VARIANT GLY-208, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pancreatic carcinoma;
RX PubMed=10825129;
RA Wallrapp C., Haehnel S., Mueller-Pillasch F., Burghardt B., Iwamura T.,
RA Ruthenbuerger M., Lerch M.M., Adler G., Gress T.M.;
RT "A novel transmembrane serine protease (TMPRSS3) overexpressed in
RT pancreatic cancer.";
RL Cancer Res. 60:2602-2606(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-208.
RA Smeekens S.S., Lorimer D.D., Wang E., Hou J., Linnevers C.;
RT "MT-SP2, a novel type II membrane serine protease expressed in trachea,
RT colon, and small intestine: identification, cloning, and chromosomal
RT localization.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP GLY-208.
RC TISSUE=Colon;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-208.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLY-208.
RC TISSUE=Ovary, and Pancreas;
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 [8]
RP FUNCTION, MUTAGENESIS OF ASP-290 AND SER-387, AND SUBCELLULAR LOCATION.
RX PubMed=24434139; DOI=10.1016/j.bbrc.2014.01.013;
RA Min H.J., Lee M.K., Lee J.W., Kim S.;
RT "TMPRSS4 induces cancer cell invasion through pro-uPA processing.";
RL Biochem. Biophys. Res. Commun. 446:1-7(2014).
RN [9]
RP REVIEW OF FUNCTION.
RX PubMed=25203520; DOI=10.1038/bjc.2014.403;
RA de Aberasturi A.L., Calvo A.;
RT "TMPRSS4: an emerging potential therapeutic target in cancer.";
RL Br. J. Cancer 112:4-8(2015).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RX PubMed=32404436; DOI=10.1126/sciimmunol.abc3582;
RA Zang R., Gomez Castro M.F., McCune B.T., Zeng Q., Rothlauf P.W.,
RA Sonnek N.M., Liu Z., Brulois K.F., Wang X., Greenberg H.B., Diamond M.S.,
RA Ciorba M.A., Whelan S.P.J., Ding S.;
RT "TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal
RT enterocytes.";
RL Sci. Immunol. 5:0-0(2020).
CC -!- FUNCTION: Plasma membrane-anchored serine protease that directly
CC induces processing of pro-uPA/PLAU into the active form through
CC proteolytic activity (PubMed:24434139). Seems to be capable of
CC activating ENaC (By similarity). {ECO:0000250|UniProtKB:Q8VCA5,
CC ECO:0000269|PubMed:24434139}.
CC -!- FUNCTION: (Microbial infection) In gut epithelial cells, facilitates
CC human coronavirus SARS-CoV-2 infection through, at least, the cleavage
CC of coronavirus spike glycoproteins which activates the glycoprotein for
CC host cell entry. {ECO:0000269|PubMed:32404436}.
CC -!- INTERACTION:
CC Q9NRS4; O60238: BNIP3L; NbExp=3; IntAct=EBI-10313040, EBI-849893;
CC Q9NRS4; P58418: CLRN1; NbExp=3; IntAct=EBI-10313040, EBI-17274839;
CC Q9NRS4; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-10313040, EBI-9087876;
CC Q9NRS4; P60508: ERVFRD-1; NbExp=3; IntAct=EBI-10313040, EBI-17973325;
CC Q9NRS4; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10313040, EBI-18304435;
CC Q9NRS4; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-10313040, EBI-12142257;
CC Q9NRS4; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10313040, EBI-11721746;
CC Q9NRS4; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10313040, EBI-749265;
CC Q9NRS4; Q8TDF6-2: RASGRP4; NbExp=3; IntAct=EBI-10313040, EBI-12816371;
CC Q9NRS4; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-10313040, EBI-17640454;
CC Q9NRS4; Q96L08: SUSD3; NbExp=3; IntAct=EBI-10313040, EBI-18194029;
CC Q9NRS4; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-10313040, EBI-8649725;
CC Q9NRS4-3; Q9BXN2: CLEC7A; NbExp=3; IntAct=EBI-10312990, EBI-3939278;
CC Q9NRS4-3; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10312990, EBI-749265;
CC Q9NRS4-3; Q8N205: SYNE4; NbExp=3; IntAct=EBI-10312990, EBI-7131783;
CC Q9NRS4-3; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-10312990, EBI-8649725;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24434139};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protease serine 4 catalytic
CC chain]: Secreted {ECO:0000269|PubMed:24434139}. Note=Activated by
CC cleavage and secreted. {ECO:0000269|PubMed:24434139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NRS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRS4-2; Sequence=VSP_013117;
CC Name=3;
CC IsoId=Q9NRS4-3; Sequence=VSP_013116;
CC Name=4;
CC IsoId=Q9NRS4-4; Sequence=VSP_013116, VSP_054229;
CC -!- TISSUE SPECIFICITY: High levels in pancreatic, gastric, colorectal and
CC ampullary cancer. Very weak expression in normal gastrointestinal and
CC urogenital tract (PubMed:10825129). Coexpressed with ACE2 within mature
CC enterocytes (PubMed:32404436). {ECO:0000269|PubMed:10825129,
CC ECO:0000269|PubMed:32404436}.
CC -!- PTM: Proteolytically processed; probably by an autocatalytic mechanism.
CC {ECO:0000305|PubMed:25203520}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31436.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/42594/TMPRSS4";
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DR EMBL; AF179224; AAF74526.1; -; mRNA.
DR EMBL; AF216312; AAF31436.1; ALT_FRAME; mRNA.
DR EMBL; AK172766; BAD18749.1; -; mRNA.
DR EMBL; AK303173; BAH13911.1; -; mRNA.
DR EMBL; AY358530; AAQ88894.1; -; mRNA.
DR EMBL; EF445038; ACA06088.1; -; Genomic_DNA.
DR EMBL; AP000665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004855; AAH04855.1; -; mRNA.
DR EMBL; BC011703; AAH11703.1; -; mRNA.
DR CCDS; CCDS31684.1; -. [Q9NRS4-1]
DR CCDS; CCDS44743.1; -. [Q9NRS4-2]
DR CCDS; CCDS53716.1; -. [Q9NRS4-3]
DR CCDS; CCDS53717.1; -. [Q9NRS4-4]
DR RefSeq; NP_001077416.1; NM_001083947.1. [Q9NRS4-2]
DR RefSeq; NP_001167023.1; NM_001173552.1. [Q9NRS4-4]
DR RefSeq; NP_063947.1; NM_019894.3. [Q9NRS4-1]
DR AlphaFoldDB; Q9NRS4; -.
DR SMR; Q9NRS4; -.
DR BioGRID; 121163; 310.
DR IntAct; Q9NRS4; 14.
DR STRING; 9606.ENSP00000416037; -.
DR BindingDB; Q9NRS4; -.
DR ChEMBL; CHEMBL2331048; -.
DR MEROPS; S01.034; -.
DR GlyCosmos; Q9NRS4; 2 sites, No reported glycans.
DR GlyGen; Q9NRS4; 2 sites.
DR iPTMnet; Q9NRS4; -.
DR PhosphoSitePlus; Q9NRS4; -.
DR BioMuta; TMPRSS4; -.
DR DMDM; 317373304; -.
DR jPOST; Q9NRS4; -.
DR MassIVE; Q9NRS4; -.
DR PaxDb; 9606-ENSP00000477949; -.
DR PeptideAtlas; Q9NRS4; -.
DR ProteomicsDB; 17874; -.
DR ProteomicsDB; 82418; -. [Q9NRS4-1]
DR ProteomicsDB; 82419; -. [Q9NRS4-2]
DR ProteomicsDB; 82420; -. [Q9NRS4-3]
DR ABCD; Q9NRS4; 12 sequenced antibodies.
DR Antibodypedia; 1732; 334 antibodies from 32 providers.
DR DNASU; 56649; -.
DR Ensembl; ENST00000437212.8; ENSP00000416037.3; ENSG00000137648.19. [Q9NRS4-1]
DR Ensembl; ENST00000522824.5; ENSP00000430547.1; ENSG00000137648.19. [Q9NRS4-2]
DR Ensembl; ENST00000523251.5; ENSP00000429209.1; ENSG00000137648.19. [Q9NRS4-4]
DR Ensembl; ENST00000534111.5; ENSP00000435184.1; ENSG00000137648.19. [Q9NRS4-3]
DR GeneID; 56649; -.
DR KEGG; hsa:56649; -.
DR MANE-Select; ENST00000437212.8; ENSP00000416037.3; NM_019894.4; NP_063947.2.
DR UCSC; uc010rxo.3; human. [Q9NRS4-1]
DR AGR; HGNC:11878; -.
DR CTD; 56649; -.
DR DisGeNET; 56649; -.
DR GeneCards; TMPRSS4; -.
DR HGNC; HGNC:11878; TMPRSS4.
DR HPA; ENSG00000137648; Tissue enhanced (esophagus, intestine, urinary bladder).
DR MalaCards; TMPRSS4; -.
DR MIM; 606565; gene.
DR neXtProt; NX_Q9NRS4; -.
DR OpenTargets; ENSG00000137648; -.
DR Orphanet; 363969; Autosomal recessive cerebral atrophy.
DR PharmGKB; PA36579; -.
DR VEuPathDB; HostDB:ENSG00000137648; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR InParanoid; Q9NRS4; -.
DR OMA; GNWASAC; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; Q9NRS4; -.
DR TreeFam; TF351678; -.
DR PathwayCommons; Q9NRS4; -.
DR SignaLink; Q9NRS4; -.
DR SIGNOR; Q9NRS4; -.
DR BioGRID-ORCS; 56649; 9 hits in 1155 CRISPR screens.
DR ChiTaRS; TMPRSS4; human.
DR GenomeRNAi; 56649; -.
DR Pharos; Q9NRS4; Tbio.
DR PRO; PR:Q9NRS4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NRS4; Protein.
DR Bgee; ENSG00000137648; Expressed in mucosa of transverse colon and 143 other cell types or tissues.
DR ExpressionAtlas; Q9NRS4; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0045967; P:negative regulation of growth rate; IDA:MGI.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001190; SRCR.
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; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50287; SRCR_2; 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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Hydrolase; Membrane; Protease; Reference proteome;
KW Secreted; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..437
FT /note="Transmembrane protease serine 4"
FT /id="PRO_0000088692"
FT CHAIN ?..437
FT /note="Transmembrane protease serine 4 catalytic chain"
FT /id="PRO_0000451627"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 61..93
FT /note="LDL-receptor class A"
FT DOMAIN 94..204
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 205..434
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 387
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 204..205
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..83
FT /evidence="ECO:0000250"
FT DISULFID 77..92
FT /evidence="ECO:0000250"
FT DISULFID 127..183
FT /evidence="ECO:0000250"
FT DISULFID 140..193
FT /evidence="ECO:0000250"
FT DISULFID 196..310
FT /evidence="ECO:0000250"
FT DISULFID 230..246
FT /evidence="ECO:0000250"
FT DISULFID 356..372
FT /evidence="ECO:0000250"
FT DISULFID 383..410
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..3
FT /note="MLQ -> M (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013116"
FT VAR_SEQ 14..53
FT /note="LDVKPLRKPRIPMETFRKVGIPIIIALLSLASIIIVVVLI -> LV (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054229"
FT VAR_SEQ 147..151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013117"
FT VARIANT 177
FT /note="R -> Q (in dbSNP:rs1894176)"
FT /id="VAR_024293"
FT VARIANT 198
FT /note="K -> E (in dbSNP:rs12270001)"
FT /id="VAR_046505"
FT VARIANT 208
FT /note="V -> G (in dbSNP:rs1941635)"
FT /evidence="ECO:0000269|PubMed:10825129,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_046506"
FT MUTAGEN 290
FT /note="D->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:24434139"
FT MUTAGEN 387
FT /note="S->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:24434139"
FT CONFLICT 2
FT /note="L -> V (in Ref. 2; AAF31436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 48246 MW; 3CF55633361A2BE7 CRC64;
MLQDPDSDQP LNSLDVKPLR KPRIPMETFR KVGIPIIIAL LSLASIIIVV VLIKVILDKY
YFLCGQPLHF IPRKQLCDGE LDCPLGEDEE HCVKSFPEGP AVAVRLSKDR STLQVLDSAT
GNWFSACFDN FTEALAETAC RQMGYSSKPT FRAVEIGPDQ DLDVVEITEN SQELRMRNSS
GPCLSGSLVS LHCLACGKSL KTPRVVGVEE ASVDSWPWQV SIQYDKQHVC GGSILDPHWV
LTAAHCFRKH TDVFNWKVRA GSDKLGSFPS LAVAKIIIIE FNPMYPKDND IALMKLQFPL
TFSGTVRPIC LPFFDEELTP ATPLWIIGWG FTKQNGGKMS DILLQASVQV IDSTRCNADD
AYQGEVTEKM MCAGIPEGGV DTCQGDSGGP LMYQSDQWHV VGIVSWGYGC GGPSTPGVYT
KVSAYLNWIY NVWKAEL
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