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 27-NOV-2024, entry version 199. 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:10754382, CC PubMed:11217080, PubMed:8827452). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 6. DR IntAct; Q14520; 4. DR MINT; Q14520; -. DR STRING; 9606.ENSP00000277903; -. 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; 281 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 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; 4629979at2759; -. 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="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 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 //