ID   HABP2_HUMAN             Reviewed;         560 AA.
AC   Q14520; A8K467; B7Z8U5; F5H5M6; O00663;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   18-JUN-2025, entry version 202.
DE   RecName: Full=Factor VII-activating protease {ECO:0000303|PubMed:10754382};
DE            Short=FSAP {ECO:0000305|PubMed:10754382};
DE            EC=3.4.21.- {ECO:0000269|PubMed:11217080};
DE   AltName: Full=FVII activator {ECO:0000303|PubMed:10754382};
DE   AltName: Full=Hepatocyte growth factor activator-like protein {ECO:0000303|PubMed:10754382};
DE   AltName: Full=Hyaluronan-binding protein 2;
DE   AltName: Full=Plasma hyaluronan-binding protein {ECO:0000303|PubMed:8827452};
DE            Short=PHBP {ECO:0000303|PubMed:8827452};
DE   AltName: Full=Plasma hyaluronan-binding serine protease;
DE            Short=PHBSP;
DE   Contains:
DE     RecName: Full=Factor VII-activating protease 50 kDa N-terminal heavy chain {ECO:0000305|PubMed:11379758};
DE   Contains:
DE     RecName: Full=Factor VII-activating protease 50 kDa N-terminal heavy chain alternate form {ECO:0000305|PubMed:11379758};
DE   Contains:
DE     RecName: Full=Factor VII-activating protease 27 kDa C-terminal light chain {ECO:0000305|PubMed:11379758};
DE   Contains:
DE     RecName: Full=Factor VII-activating protease 27 kDa C-terminal light chain alternate form {ECO:0000305|PubMed:11379758};
DE   Flags: Precursor;
GN   Name=HABP2 {ECO:0000303|PubMed:26222560, ECO:0000312|HGNC:HGNC:4798};
GN   Synonyms=HGFAL;
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), PROTEIN SEQUENCE OF 24-42; 140-169;
RP   174-183; 206-235; 255-260; 314-334; 417-429; 433-459; 500-517 AND 546-551,
RP   PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   SUBUNIT.
RC   TISSUE=Plasma;
RX   PubMed=8827452; DOI=10.1093/oxfordjournals.jbchem.a021362;
RA   Choi-Miura N.-H., Tobe T., Sumiya J., Nakano Y., Sano Y., Mazda T.,
RA   Tomita M.;
RT   "Purification and characterization of a novel hyaluronan-binding protein
RT   (PHBP) from human plasma: it has three EGF, a kringle and a serine protease
RT   domain, similar to hepatocyte growth factor activator.";
RL   J. Biochem. 119:1157-1165(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Kitamura N.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-90 AND GLN-393, AND VARIANT
RP   NMTC5 GLU-534.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Liver, and Trachea;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
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   PARTIAL PROTEIN SEQUENCE, POST-TRANSLATIONAL MODIFICATIONS, AND SUBUNIT.
RX   PubMed=11379758; DOI=10.1248/bpb.24.448;
RA   Choi-Miura N.H., Takahashi K., Yoda M., Saito K., Mazda T., Tomita M.;
RT   "Proteolytic activation and inactivation of the serine protease activity of
RT   plasma hyaluronan binding protein.";
RL   Biol. Pharm. Bull. 24:448-452(2001).
RN   [9]
RP   FUNCTION.
RX   PubMed=10754382; DOI=10.1159/000022515;
RA   Roemisch J., Vermoehlen S., Feussner A., Stoehr H.-A.;
RT   "The FVII activating protease cleaves single-chain plasminogen
RT   activators.";
RL   Haemostasis 29:292-299(1999).
RN   [10]
RP   FUNCTION.
RX   PubMed=11217080; DOI=10.1248/bpb.24.140;
RA   Choi-Miura N.H., Yoda M., Saito K., Takahashi K., Tomita M.;
RT   "Identification of the substrates for plasma hyaluronan binding protein.";
RL   Biol. Pharm. Bull. 24:140-143(2001).
RN   [11]
RP   VARIANT GLN-393, AND VARIANT NMTC5 GLU-534.
RX   PubMed=12578864; DOI=10.1161/01.cir.0000055189.18831.b1;
RA   Willeit J., Kiechl S., Weimer T., Mair A., Santer P., Wiedermann C.J.,
RA   Roemisch J.;
RT   "Marburg I polymorphism of factor VII-activating protease: a prominent risk
RT   predictor of carotid stenosis.";
RL   Circulation 107:667-670(2003).
RN   [12]
RP   FUNCTION, INVOLVEMENT IN NMTC5, VARIANT NMTC5 GLU-534, AND CHARACTERIZATION
RP   OF VARIANT NMTC5 GLU-534.
RX   PubMed=26222560; DOI=10.1056/nejmoa1502449;
RA   Gara S.K., Jia L., Merino M.J., Agarwal S.K., Zhang L., Cam M., Patel D.,
RA   Kebebew E.;
RT   "Germline HABP2 mutation causing familial nonmedullary thyroid cancer.";
RL   N. Engl. J. Med. 373:448-455(2015).
CC   -!- FUNCTION: Cleaves the alpha-chain at multiple sites and the beta-chain
CC       between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and
CC       therefore does not initiate the formation of the fibrin clot and does
CC       not cause the fibrinolysis directly (PubMed:11217080). It does not
CC       cleave (activate) prothrombin and plasminogen but converts the inactive
CC       single chain urinary plasminogen activator (pro-urokinase) to the
CC       active two chain form (PubMed:10754382, PubMed:11217080). Activates
CC       coagulation factor VII (Probable). May function as a tumor suppressor
CC       negatively regulating cell proliferation and cell migration
CC       (PubMed:26222560). {ECO:0000269|PubMed:10754382,
CC       ECO:0000269|PubMed:11217080, ECO:0000269|PubMed:26222560,
CC       ECO:0000305|PubMed:10754382}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. Heterodimer of a 50 kDa heavy
CC       and a 27 kDa light chain linked by a disulfide bond.
CC       {ECO:0000269|PubMed:11379758, ECO:0000269|PubMed:8827452}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8827452}.
CC       Note=Secreted as an inactive single-chain precursor and is then
CC       activated to a heterodimeric form.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14520-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14520-2; Sequence=VSP_044583;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:8827452}.
CC   -!- PTM: Proteolytic cleavage at Gly-23 or Met-27 can give rise to the 50
CC       kDa heavy chain (HC) and cleavage at Arg-313 or Lys-319 can give rise
CC       to the 27 kDa light chain (LC) (PubMed:8827452). The HC can undergo
CC       further proteolytic cleavage giving rise to a 26 kDa fragment
CC       (PubMed:11379758). The LC can undergo further proteolytic cleavage at
CC       Arg-313 leading to a 17-kDa fragment and at Arg-480 leading to a 8-kDa
CC       fragment (PubMed:11379758). {ECO:0000269|PubMed:11379758,
CC       ECO:0000269|PubMed:8827452}.
CC   -!- DISEASE: Thyroid cancer, non-medullary, 5 (NMTC5) [MIM:616535]: A form
CC       of non-medullary thyroid cancer (NMTC), a cancer characterized by
CC       tumors originating from the thyroid follicular cells. NMTCs represent
CC       approximately 95% of all cases of thyroid cancer and are classified
CC       into papillary, follicular, Hurthle cell, and anaplastic neoplasms.
CC       {ECO:0000269|PubMed:12578864, ECO:0000269|PubMed:26222560}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; S83182; AAB46909.1; -; mRNA.
DR   EMBL; D49742; BAA08576.1; -; mRNA.
DR   EMBL; AY534754; AAS16352.1; -; Genomic_DNA.
DR   EMBL; AK290832; BAF83521.1; -; mRNA.
DR   EMBL; AK303948; BAH14081.1; -; mRNA.
DR   EMBL; AL390197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW49505.1; -; Genomic_DNA.
DR   EMBL; BC031412; AAH31412.1; -; mRNA.
DR   CCDS; CCDS53579.1; -. [Q14520-2]
DR   CCDS; CCDS7577.1; -. [Q14520-1]
DR   PIR; JC4795; JC4795.
DR   RefSeq; NP_001171131.1; NM_001177660.3. [Q14520-2]
DR   RefSeq; NP_004123.1; NM_004132.5. [Q14520-1]
DR   AlphaFoldDB; Q14520; -.
DR   SMR; Q14520; -.
DR   BioGRID; 109276; 6.
DR   FunCoup; Q14520; 391.
DR   IntAct; Q14520; 4.
DR   MINT; Q14520; -.
DR   STRING; 9606.ENSP00000277903; -.
DR   BindingDB; Q14520; -.
DR   ChEMBL; CHEMBL5465370; -.
DR   DrugBank; DB08818; Hyaluronic acid.
DR   MEROPS; S01.033; -.
DR   GlyCosmos; Q14520; 5 sites, 2 glycans.
DR   GlyGen; Q14520; 8 sites, 3 O-linked glycans (5 sites).
DR   iPTMnet; Q14520; -.
DR   PhosphoSitePlus; Q14520; -.
DR   BioMuta; HABP2; -.
DR   DMDM; 73919921; -.
DR   CPTAC; non-CPTAC-2675; -.
DR   jPOST; Q14520; -.
DR   MassIVE; Q14520; -.
DR   PaxDb; 9606-ENSP00000277903; -.
DR   PeptideAtlas; Q14520; -.
DR   ProteomicsDB; 26922; -.
DR   ProteomicsDB; 60020; -. [Q14520-1]
DR   Antibodypedia; 18461; 284 antibodies from 28 providers.
DR   DNASU; 3026; -.
DR   Ensembl; ENST00000351270.4; ENSP00000277903.4; ENSG00000148702.15. [Q14520-1]
DR   Ensembl; ENST00000542051.5; ENSP00000443283.1; ENSG00000148702.15. [Q14520-2]
DR   GeneID; 3026; -.
DR   KEGG; hsa:3026; -.
DR   MANE-Select; ENST00000351270.4; ENSP00000277903.4; NM_004132.5; NP_004123.1.
DR   UCSC; uc001lai.5; human. [Q14520-1]
DR   AGR; HGNC:4798; -.
DR   CTD; 3026; -.
DR   DisGeNET; 3026; -.
DR   GeneCards; HABP2; -.
DR   HGNC; HGNC:4798; HABP2.
DR   HPA; ENSG00000148702; Tissue enriched (liver).
DR   MalaCards; HABP2; -.
DR   MIM; 603924; gene.
DR   MIM; 616535; phenotype.
DR   neXtProt; NX_Q14520; -.
DR   OpenTargets; ENSG00000148702; -.
DR   Orphanet; 319487; Familial papillary or follicular thyroid carcinoma.
DR   PharmGKB; PA29172; -.
DR   VEuPathDB; HostDB:ENSG00000148702; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000157814; -.
DR   HOGENOM; CLU_006842_18_2_1; -.
DR   InParanoid; Q14520; -.
DR   OMA; GKTACGF; -.
DR   OrthoDB; 9937281at2759; -.
DR   PAN-GO; Q14520; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q14520; -.
DR   TreeFam; TF329901; -.
DR   BRENDA; 3.4.21.B1; 2681.
DR   PathwayCommons; Q14520; -.
DR   SABIO-RK; Q14520; -.
DR   SignaLink; Q14520; -.
DR   BioGRID-ORCS; 3026; 9 hits in 1145 CRISPR screens.
DR   GeneWiki; HABP2; -.
DR   GenomeRNAi; 3026; -.
DR   Pharos; Q14520; Tbio.
DR   PRO; PR:Q14520; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q14520; protein.
DR   Bgee; ENSG00000148702; Expressed in right lobe of liver and 87 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005539; F:glycosaminoglycan binding; TAS:ProtInc.
DR   GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0006508; P:proteolysis; IDA:MGI.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.10.25.10:FF:000571; Hyaluronan-binding protein 2; 1.
DR   FunFam; 2.40.10.10:FF:000069; Hyaluronan-binding protein 2; 1.
DR   FunFam; 2.10.25.10:FF:000463; hyaluronan-binding protein 2; 1.
DR   FunFam; 2.40.20.10:FF:000001; Urokinase-type plasminogen activator; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR050127; Serine_Proteases_S1.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264:SF40; HYALURONAN-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_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; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Kringle; Protease; Proteomics identification;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:8827452"
FT   CHAIN           24..313
FT                   /note="Factor VII-activating protease 50 kDa N-terminal
FT                   heavy chain"
FT                   /evidence="ECO:0000269|PubMed:8827452"
FT                   /id="PRO_0000027899"
FT   CHAIN           28..313
FT                   /note="Factor VII-activating protease 50 kDa N-terminal
FT                   heavy chain alternate form"
FT                   /evidence="ECO:0000269|PubMed:8827452"
FT                   /id="PRO_0000027900"
FT   CHAIN           314..560
FT                   /note="Factor VII-activating protease 27 kDa C-terminal
FT                   light chain"
FT                   /evidence="ECO:0000269|PubMed:11379758,
FT                   ECO:0000269|PubMed:8827452"
FT                   /id="PRO_0000027901"
FT   CHAIN           320..560
FT                   /note="Factor VII-activating protease 27 kDa C-terminal
FT                   light chain alternate form"
FT                   /evidence="ECO:0000269|PubMed:8827452"
FT                   /id="PRO_0000027902"
FT   DOMAIN          73..109
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          111..148
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          150..188
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          193..276
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          314..555
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        362
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q04756,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        411
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q04756,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        509
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q04756,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   SITE            480..481
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000269|PubMed:11379758"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        82..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        99..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        115..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        120..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        138..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        154..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        159..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        178..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        194..276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        215..257
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        246..271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        301..435
FT                   /evidence="ECO:0000250|UniProtKB:Q04756"
FT   DISULFID        301
FT                   /note="Interchain (with C-521)"
FT                   /evidence="ECO:0000250|UniProtKB:Q04756"
FT   DISULFID        347..363
FT                   /evidence="ECO:0000250|UniProtKB:Q04756,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        355..424
FT                   /evidence="ECO:0000250|UniProtKB:Q04756"
FT   DISULFID        435
FT                   /note="Interchain (with C-394)"
FT                   /evidence="ECO:0000250|UniProtKB:Q04756"
FT   DISULFID        447..515
FT                   /evidence="ECO:0000250|UniProtKB:Q04756,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        477..493
FT                   /evidence="ECO:0000250|UniProtKB:Q04756,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        505..533
FT                   /evidence="ECO:0000250|UniProtKB:Q04756,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274"
FT   VAR_SEQ         1..26
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044583"
FT   VARIANT         90
FT                   /note="V -> I (in dbSNP:rs11575750)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_023399"
FT   VARIANT         393
FT                   /note="E -> Q (variant Marburg II; dbSNP:rs11575688)"
FT                   /evidence="ECO:0000269|PubMed:12578864, ECO:0000269|Ref.3"
FT                   /id="VAR_023400"
FT   VARIANT         534
FT                   /note="G -> E (in NMTC5; associated with disease
FT                   susceptibility; variant Marburg I; could be a prominent
FT                   risk predictor of carotid stenosis; impairs the
FT                   pro-urokinase activating potency; increased cell migration
FT                   and increased cell proliferation; dominant negative effect;
FT                   dbSNP:rs7080536)"
FT                   /evidence="ECO:0000269|PubMed:12578864,
FT                   ECO:0000269|PubMed:26222560, ECO:0000269|Ref.3"
FT                   /id="VAR_023401"
FT   CONFLICT        157
FT                   /note="N -> S (in Ref. 4; BAH14081)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   560 AA;  62672 MW;  5C1907230784ACD4 CRC64;
     MFARMSDLHV LLLMALVGKT ACGFSLMSLL ESLDPDWTPD QYDYSYEDYN QEENTSSTLT
     HAENPDWYYT EDQADPCQPN PCEHGGDCLV HGSTFTCSCL APFSGNKCQK VQNTCKDNPC
     GRGQCLITQS PPYYRCVCKH PYTGPSCSQV VPVCRPNPCQ NGATCSRHKR RSKFTCACPD
     QFKGKFCEIG SDDCYVGDGY SYRGKMNRTV NQHACLYWNS HLLLQENYNM FMEDAETHGI
     GEHNFCRNPD ADEKPWCFIK VTNDKVKWEY CDVSACSAQD VAYPEESPTE PSTKLPGFDS
     CGKTEIAERK IKRIYGGFKS TAGKHPWQAS LQSSLPLTIS MPQGHFCGGA LIHPCWVLTA
     AHCTDIKTRH LKVVLGDQDL KKEEFHEQSF RVEKIFKYSH YNERDEIPHN DIALLKLKPV
     DGHCALESKY VKTVCLPDGS FPSGSECHIS GWGVTETGKG SRQLLDAKVK LIANTLCNSR
     QLYDHMIDDS MICAGNLQKP GQDTCQGDSG GPLTCEKDGT YYVYGIVSWG LECGKRPGVY
     TQVTKFLNWI KATIKSESGF
//