GenomeNet

Database: UniProt
Entry: Q14520
LinkDB: Q14520
Original site: Q14520 
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   13-FEB-2019, entry version 169.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-42;
RP   140-169; 174-183; 206-235; 255-260; 314-334; 417-429; 433-459; 500-517
RP   AND 546-551, 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
RT   protein (PHBP) from human plasma: it has three EGF, a kringle and a
RT   serine protease domain, similar to hepatocyte growth factor
RT   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
RP   VARIANT 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=10754382;
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
RT   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
RT   risk predictor of carotid stenosis.";
RL   Circulation 107:667-670(2003).
RN   [11]
RP   FUNCTION, INVOLVEMENT IN NMTC5, VARIANT NMTC5 GLU-534, AND
RP   CHARACTERIZATION 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.,
RA   Patel D., Kebebew E.;
RT   "Germline HABP2 mutation causing familial nonmedullary thyroid
RT   cancer.";
RL   N. Engl. J. Med. 373:448-455(2015).
CC   -!- FUNCTION: Cleaves the alpha-chain at multiple sites and the beta-
CC       chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of
CC       fibrinogen and therefore does not initiate the formation of the
CC       fibrin clot and does not cause the fibrinolysis directly. It does
CC       not cleave (activate) prothrombin and plasminogen but converts the
CC       inactive single chain urinary plasminogen activator (pro-
CC       urokinase) to the active two chain form. Activates coagulation
CC       factor VII (PubMed:8827452, PubMed:10754382, PubMed:11217080). May
CC       function as a tumor suppressor negatively regulating cell
CC       proliferation and cell migration (PubMed:26222560).
CC       {ECO:0000269|PubMed:10754382, ECO:0000269|PubMed:11217080,
CC       ECO:0000269|PubMed:26222560, ECO:0000269|PubMed:8827452}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. Heterodimer of a 50 kDa
CC       heavy and a 27 kDa light chain linked by a disulfide bond (By
CC       similarity). {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         Note=No experimental confirmation available.;
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
CC       50 kDa heavy chain and cleavage at Arg-313 or Lys-319 can give
CC       rise to the 27 kDa light chain. The heavy chain can undergo
CC       further proteolytic cleavage at Lys-169 or Arg-170 to give rise to
CC       2 inactive 26 kDa fragments and the light chain can undergo
CC       further proteolytic cleavage at Arg-480 to give rise to inactive
CC       17 kDa and 8 kDa fragments (By similarity). {ECO:0000250}.
CC   -!- DISEASE: Thyroid cancer, non-medullary, 5 (NMTC5) [MIM:616535]: A
CC       form of non-medullary thyroid cancer (NMTC), a cancer
CC       characterized by tumors originating from the thyroid follicular
CC       cells. NMTCs represent approximately 95% of all cases of thyroid
CC       cancer and are classified into papillary, follicular, Hurthle
CC       cell, and anaplastic neoplasms. {ECO:0000269|PubMed:12578864,
CC       ECO:0000269|PubMed:26222560}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/habp2/";
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   UniGene; Hs.422542; -.
DR   ProteinModelPortal; Q14520; -.
DR   SMR; Q14520; -.
DR   IntAct; Q14520; 3.
DR   MINT; Q14520; -.
DR   STRING; 9606.ENSP00000277903; -.
DR   DrugBank; DB08818; Hyaluronic acid.
DR   MEROPS; S01.033; -.
DR   iPTMnet; Q14520; -.
DR   PhosphoSitePlus; Q14520; -.
DR   BioMuta; HABP2; -.
DR   DMDM; 73919921; -.
DR   EPD; Q14520; -.
DR   jPOST; Q14520; -.
DR   MaxQB; Q14520; -.
DR   PaxDb; Q14520; -.
DR   PeptideAtlas; Q14520; -.
DR   PRIDE; Q14520; -.
DR   ProteomicsDB; 60020; -.
DR   DNASU; 3026; -.
DR   Ensembl; ENST00000351270; ENSP00000277903; ENSG00000148702. [Q14520-1]
DR   Ensembl; ENST00000542051; ENSP00000443283; ENSG00000148702. [Q14520-2]
DR   GeneID; 3026; -.
DR   KEGG; hsa:3026; -.
DR   UCSC; uc001lai.5; human. [Q14520-1]
DR   CTD; 3026; -.
DR   DisGeNET; 3026; -.
DR   EuPathDB; HostDB:ENSG00000148702.14; -.
DR   GeneCards; HABP2; -.
DR   HGNC; HGNC:4798; HABP2.
DR   HPA; HPA019518; -.
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   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000157814; -.
DR   HOGENOM; HOG000237314; -.
DR   HOVERGEN; HBG106385; -.
DR   InParanoid; Q14520; -.
DR   KO; K08648; -.
DR   OMA; ITQSPPY; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q14520; -.
DR   TreeFam; TF329901; -.
DR   BRENDA; 3.4.21.B1; 2681.
DR   SABIO-RK; Q14520; -.
DR   ChiTaRS; HABP2; human.
DR   GeneWiki; HABP2; -.
DR   GenomeRNAi; 3026; -.
DR   PRO; PR:Q14520; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000148702; Expressed in 73 organ(s), highest expression level in right lobe of liver.
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:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.20.10; -; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; 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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Kringle; Polymorphism;
KW   Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW   Signal.
FT   SIGNAL        1     23       {ECO:0000269|PubMed:8827452}.
FT   CHAIN        24    313       Hyaluronan-binding protein 2 50 kDa heavy
FT                                chain.
FT                                /FTId=PRO_0000027899.
FT   CHAIN        27    313       Hyaluronan-binding protein 2 50 kDa heavy
FT                                chain alternate form. {ECO:0000250}.
FT                                /FTId=PRO_0000027900.
FT   CHAIN       314    560       Hyaluronan-binding protein 2 27 kDa light
FT                                chain.
FT                                /FTId=PRO_0000027901.
FT   CHAIN       320    560       Hyaluronan-binding protein 2 27 kDa light
FT                                chain alternate form. {ECO:0000250}.
FT                                /FTId=PRO_0000027902.
FT   DOMAIN       73    109       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      111    148       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      150    188       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      193    276       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      314    555       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    362    362       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    411    411       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    509    509       Charge relay system. {ECO:0000250}.
FT   SITE        169    170       Cleavage. {ECO:0000250}.
FT   SITE        170    171       Cleavage. {ECO:0000250}.
FT   SITE        480    481       Cleavage. {ECO:0000250}.
FT   CARBOHYD     54     54       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    207    207       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     77     88       {ECO:0000250}.
FT   DISULFID     82     97       {ECO:0000250}.
FT   DISULFID     99    108       {ECO:0000250}.
FT   DISULFID    115    125       {ECO:0000250}.
FT   DISULFID    120    136       {ECO:0000250}.
FT   DISULFID    138    147       {ECO:0000250}.
FT   DISULFID    154    165       {ECO:0000250}.
FT   DISULFID    159    176       {ECO:0000250}.
FT   DISULFID    178    187       {ECO:0000250}.
FT   DISULFID    194    276       {ECO:0000250}.
FT   DISULFID    215    257       {ECO:0000250}.
FT   DISULFID    246    271       {ECO:0000250}.
FT   DISULFID    301    435       Interchain (between heavy and light
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00121, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DISULFID    347    363       {ECO:0000250}.
FT   DISULFID    447    515       {ECO:0000250}.
FT   DISULFID    477    493       {ECO:0000250}.
FT   DISULFID    505    533       {ECO:0000250}.
FT   VAR_SEQ       1     26       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_044583.
FT   VARIANT      90     90       V -> I (in dbSNP:rs11575750).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_023399.
FT   VARIANT     393    393       E -> Q (polymorphism; Marburg II;
FT                                dbSNP:rs11575688).
FT                                {ECO:0000269|PubMed:12578864,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_023400.
FT   VARIANT     534    534       G -> E (in NMTC5; associated with disease
FT                                susceptibility; Marburg I polymorphism;
FT                                could be a prominent risk predictor of
FT                                carotid stenosis; impairs the pro-
FT                                urokinase activating potency; increased
FT                                cell migration and increased cell
FT                                proliferation; dominant negative effect;
FT                                dbSNP:rs7080536).
FT                                {ECO:0000269|PubMed:12578864,
FT                                ECO:0000269|PubMed:26222560,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_023401.
FT   CONFLICT    157    157       N -> S (in Ref. 4; BAH14081).
FT                                {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
//
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