HABP2_HUMAN
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 03-AUG-2022, entry version 187.
DE RecName: Full=Hyaluronan-binding protein 2;
DE EC=3.4.21.-;
DE AltName: Full=Factor VII-activating protease;
DE AltName: Full=Factor seven-activating protease;
DE Short=FSAP;
DE AltName: Full=Hepatocyte growth factor activator-like protein;
DE AltName: Full=Plasma hyaluronan-binding protein;
DE Contains:
DE RecName: Full=Hyaluronan-binding protein 2 50 kDa heavy chain;
DE Contains:
DE RecName: Full=Hyaluronan-binding protein 2 50 kDa heavy chain alternate form;
DE Contains:
DE RecName: Full=Hyaluronan-binding protein 2 27 kDa light chain;
DE Contains:
DE RecName: Full=Hyaluronan-binding protein 2 27 kDa light chain alternate form;
DE Flags: Precursor;
GN Name=HABP2; Synonyms=HGFAL, PHBP;
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 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 [9]
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 [10]
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 [11]
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. It does not cleave (activate)
CC prothrombin and plasminogen but converts the inactive single chain
CC urinary plasminogen activator (pro-urokinase) to the active two chain
CC form. Activates coagulation factor VII (PubMed:8827452,
CC PubMed:10754382, PubMed:11217080). 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:0000269|PubMed:8827452}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. Heterodimer of a 50 kDa heavy
CC and a 27 kDa light chain linked by a disulfide bond (By similarity).
CC {ECO:0000250}.
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 and cleavage at Arg-313 or Lys-319 can give rise to the
CC 27 kDa light chain. The heavy chain can undergo further proteolytic
CC cleavage at Lys-169 or Arg-170 to give rise to 2 inactive 26 kDa
CC fragments and the light chain can undergo further proteolytic cleavage
CC at Arg-480 to give rise to inactive 17 kDa and 8 kDa fragments (By
CC similarity). {ECO:0000250}.
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}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/habp2/";
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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_001177660.2. [Q14520-2]
DR RefSeq; NP_004123.1; NM_004132.4. [Q14520-1]
DR AlphaFoldDB; Q14520; -.
DR SMR; Q14520; -.
DR BioGRID; 109276; 2.
DR IntAct; Q14520; 4.
DR MINT; Q14520; -.
DR STRING; 9606.ENSP00000277903; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR MEROPS; S01.033; -.
DR GlyGen; Q14520; 6 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q14520; -.
DR PhosphoSitePlus; Q14520; -.
DR BioMuta; HABP2; -.
DR DMDM; 73919921; -.
DR CPTAC; non-CPTAC-2675; -.
DR EPD; Q14520; -.
DR jPOST; Q14520; -.
DR MassIVE; Q14520; -.
DR MaxQB; Q14520; -.
DR PaxDb; Q14520; -.
DR PeptideAtlas; Q14520; -.
DR PRIDE; Q14520; -.
DR ProteomicsDB; 26922; -.
DR ProteomicsDB; 60020; -. [Q14520-1]
DR Antibodypedia; 18461; 298 antibodies from 27 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 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; 1314811at2759; -.
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 1067 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 86 other tissues.
DR Genevisible; Q14520; HS.
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; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 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; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 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; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8827452"
FT CHAIN 24..313
FT /note="Hyaluronan-binding protein 2 50 kDa heavy chain"
FT /id="PRO_0000027899"
FT CHAIN 27..313
FT /note="Hyaluronan-binding protein 2 50 kDa heavy chain
FT alternate form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027900"
FT CHAIN 314..560
FT /note="Hyaluronan-binding protein 2 27 kDa light chain"
FT /id="PRO_0000027901"
FT CHAIN 320..560
FT /note="Hyaluronan-binding protein 2 27 kDa light chain
FT alternate form"
FT /evidence="ECO:0000250"
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"
FT ACT_SITE 411
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 509
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 169..170
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 170..171
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 480..481
FT /note="Cleavage"
FT /evidence="ECO:0000250"
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:0000250"
FT DISULFID 82..97
FT /evidence="ECO:0000250"
FT DISULFID 99..108
FT /evidence="ECO:0000250"
FT DISULFID 115..125
FT /evidence="ECO:0000250"
FT DISULFID 120..136
FT /evidence="ECO:0000250"
FT DISULFID 138..147
FT /evidence="ECO:0000250"
FT DISULFID 154..165
FT /evidence="ECO:0000250"
FT DISULFID 159..176
FT /evidence="ECO:0000250"
FT DISULFID 178..187
FT /evidence="ECO:0000250"
FT DISULFID 194..276
FT /evidence="ECO:0000250"
FT DISULFID 215..257
FT /evidence="ECO:0000250"
FT DISULFID 246..271
FT /evidence="ECO:0000250"
FT DISULFID 301..435
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000255|PROSITE-ProRule:PRU00121, ECO:0000255|PROSITE-
FT ProRule:PRU00274"
FT DISULFID 347..363
FT /evidence="ECO:0000250"
FT DISULFID 447..515
FT /evidence="ECO:0000250"
FT DISULFID 477..493
FT /evidence="ECO:0000250"
FT DISULFID 505..533
FT /evidence="ECO:0000250"
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 pro-
FT urokinase activating potency; increased cell migration and
FT 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
