ID   HGFA_HUMAN              Reviewed;         655 AA.
AC   Q04756; Q14726; Q2M1W7; Q53X47;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   24-JAN-2024, entry version 207.
DE   RecName: Full=Hepatocyte growth factor activator;
DE            Short=HGF activator;
DE            Short=HGFA;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Hepatocyte growth factor activator short chain;
DE   Contains:
DE     RecName: Full=Hepatocyte growth factor activator long chain;
DE   Flags: Precursor;
GN   Name=HGFAC;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver, and Serum;
RX   PubMed=7683665; DOI=10.1016/s0021-9258(18)82167-6;
RA   Miyazawa K., Shimomura T., Kitamura A., Kondo J., Morimoto Y., Kitamura N.;
RT   "Molecular cloning and sequence analysis of the cDNA for a human serine
RT   protease responsible for activation of hepatocyte growth factor. Structural
RT   similarity of the protease precursor to blood coagulation factor XII.";
RL   J. Biol. Chem. 268:10024-10028(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9874200; DOI=10.1046/j.1432-1327.1998.2580355.x;
RA   Miyazawa K., Wang Y., Minoshima S., Shimizu N., Kitamura N.;
RT   "Structural organization and chromosomal localization of the human
RT   hepatocyte growth factor activator gene -- phylogenetic and functional
RT   relationship with blood coagulation factor XII, urokinase, and tissue-type
RT   plasminogen activator.";
RL   Eur. J. Biochem. 258:355-361(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-231.
RC   TISSUE=Liver;
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   [6]
RP   PROTEIN SEQUENCE OF 36-50.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-468.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-468.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 373-655 ALONE AND IN COMPLEX WITH
RP   INHIBITOR HAI1B, ACTIVE SITE, AND DISULFIDE BONDS.
RX   PubMed=15713485; DOI=10.1016/j.jmb.2004.12.048;
RA   Shia S., Stamos J., Kirchhofer D., Fan B., Wu J., Corpuz R.T., Santell L.,
RA   Lazarus R.A., Eigenbrot C.;
RT   "Conformational lability in serine protease active sites: structures of
RT   hepatocyte growth factor activator (HGFA) alone and with the inhibitory
RT   domain from HGFA inhibitor-1B.";
RL   J. Mol. Biol. 346:1335-1349(2005).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 373-655 IN COMPLEX WITH ANTIBODY,
RP   GLYCOSYLATION AT ASN-468, AND DISULFIDE BONDS.
RX   PubMed=18077410; DOI=10.1073/pnas.0708251104;
RA   Wu Y., Eigenbrot C., Liang W.C., Stawicki S., Shia S., Fan B., Ganesan R.,
RA   Lipari M.T., Kirchhofer D.;
RT   "Structural insight into distinct mechanisms of protease inhibition by
RT   antibodies.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19784-19789(2007).
CC   -!- FUNCTION: Activates hepatocyte growth factor (HGF) by converting it
CC       from a single chain to a heterodimeric form.
CC   -!- SUBUNIT: Heterodimer of a short chain and a long chain linked by a
CC       disulfide bond. {ECO:0000269|PubMed:15713485,
CC       ECO:0000269|PubMed:18077410}.
CC   -!- INTERACTION:
CC       Q04756; Q92624: APPBP2; NbExp=3; IntAct=EBI-1041722, EBI-743771;
CC       Q04756; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-1041722, EBI-10175300;
CC       Q04756; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-1041722, EBI-712073;
CC       Q04756; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-1041722, EBI-8644112;
CC       Q04756; Q86XK7: VSIG1; NbExp=3; IntAct=EBI-1041722, EBI-18323486;
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted as an inactive single-
CC       chain precursor and is then activated to a heterodimeric form.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- CAUTION: It is uncertain whether Met-1 is the initiator. {ECO:0000305}.
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DR   EMBL; D14012; BAA03113.1; -; mRNA.
DR   EMBL; BC112190; AAI12191.1; -; mRNA.
DR   EMBL; D50030; BAA74450.1; -; Genomic_DNA.
DR   EMBL; AL590235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471131; EAW82464.1; -; Genomic_DNA.
DR   EMBL; BC112192; AAI12193.1; -; mRNA.
DR   CCDS; CCDS3369.1; -.
DR   PIR; A46688; A46688.
DR   RefSeq; NP_001284368.1; NM_001297439.1.
DR   RefSeq; NP_001519.1; NM_001528.3.
DR   PDB; 1YBW; X-ray; 2.70 A; A/B=373-655.
DR   PDB; 1YC0; X-ray; 2.60 A; A=373-655.
DR   PDB; 2R0K; X-ray; 3.51 A; A=373-655.
DR   PDB; 2R0L; X-ray; 2.20 A; A=408-655, B=373-407.
DR   PDB; 2WUB; X-ray; 2.90 A; A/C=408-655, B/D=373-407.
DR   PDB; 2WUC; X-ray; 2.70 A; A=408-654, B=373-407.
DR   PDB; 3K2U; X-ray; 2.35 A; A=408-655, B=373-407.
DR   PDBsum; 1YBW; -.
DR   PDBsum; 1YC0; -.
DR   PDBsum; 2R0K; -.
DR   PDBsum; 2R0L; -.
DR   PDBsum; 2WUB; -.
DR   PDBsum; 2WUC; -.
DR   PDBsum; 3K2U; -.
DR   AlphaFoldDB; Q04756; -.
DR   SMR; Q04756; -.
DR   BioGRID; 109331; 25.
DR   DIP; DIP-6022N; -.
DR   IntAct; Q04756; 13.
DR   STRING; 9606.ENSP00000421801; -.
DR   BindingDB; Q04756; -.
DR   ChEMBL; CHEMBL3351190; -.
DR   DrugCentral; Q04756; -.
DR   MEROPS; S01.228; -.
DR   GlyConnect; 1309; 13 N-Linked glycans (4 sites).
DR   GlyCosmos; Q04756; 10 sites, 17 glycans.
DR   GlyGen; Q04756; 11 sites, 14 N-linked glycans (4 sites), 4 O-linked glycans (6 sites).
DR   iPTMnet; Q04756; -.
DR   PhosphoSitePlus; Q04756; -.
DR   BioMuta; HGFAC; -.
DR   DMDM; 547643; -.
DR   jPOST; Q04756; -.
DR   MassIVE; Q04756; -.
DR   MaxQB; Q04756; -.
DR   PaxDb; 9606-ENSP00000421801; -.
DR   PeptideAtlas; Q04756; -.
DR   ProteomicsDB; 58278; -.
DR   ABCD; Q04756; 3 sequenced antibodies.
DR   Antibodypedia; 3925; 199 antibodies from 23 providers.
DR   DNASU; 3083; -.
DR   Ensembl; ENST00000382774.8; ENSP00000372224.4; ENSG00000109758.9.
DR   GeneID; 3083; -.
DR   KEGG; hsa:3083; -.
DR   MANE-Select; ENST00000382774.8; ENSP00000372224.4; NM_001528.4; NP_001519.1.
DR   UCSC; uc003ghc.4; human.
DR   AGR; HGNC:4894; -.
DR   CTD; 3083; -.
DR   DisGeNET; 3083; -.
DR   GeneCards; HGFAC; -.
DR   HGNC; HGNC:4894; HGFAC.
DR   HPA; ENSG00000109758; Tissue enriched (liver).
DR   MIM; 604552; gene.
DR   neXtProt; NX_Q04756; -.
DR   OpenTargets; ENSG00000109758; -.
DR   PharmGKB; PA29270; -.
DR   VEuPathDB; HostDB:ENSG00000109758; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000159778; -.
DR   InParanoid; Q04756; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; Q04756; -.
DR   TreeFam; TF329901; -.
DR   PathwayCommons; Q04756; -.
DR   Reactome; R-HSA-6806942; MET Receptor Activation.
DR   SignaLink; Q04756; -.
DR   BioGRID-ORCS; 3083; 3 hits in 1145 CRISPR screens.
DR   ChiTaRS; HGFAC; human.
DR   EvolutionaryTrace; Q04756; -.
DR   GeneWiki; HGFAC; -.
DR   GenomeRNAi; 3083; -.
DR   Pharos; Q04756; Tchem.
DR   PRO; PR:Q04756; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q04756; Protein.
DR   Bgee; ENSG00000109758; Expressed in right lobe of liver and 89 other cell types or tissues.
DR   ExpressionAtlas; Q04756; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR   GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR   GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00061; FN1; 1.
DR   CDD; cd00062; FN2; 1.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR014394; Coagulation_fac_XII/HGFA.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000083; Fibronectin_type1.
DR   InterPro; IPR000562; FN_type2_dom.
DR   InterPro; IPR036943; FN_type2_sf.
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   PANTHER; PTHR24264:SF43; HEPATOCYTE GROWTH FACTOR ACTIVATOR; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00040; fn2; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001146; Factor_XII_HGFA; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00013; FNTYPEII.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00058; FN1; 1.
DR   SMART; SM00059; FN2; 1.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57440; Kringle-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01253; FN1_1; 1.
DR   PROSITE; PS51091; FN1_2; 1.
DR   PROSITE; PS00023; FN2_1; 1.
DR   PROSITE; PS51092; FN2_2; 1.
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.
DR   Genevisible; Q04756; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Kringle; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   PROPEP          36..372
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000027911"
FT   CHAIN           373..407
FT                   /note="Hepatocyte growth factor activator short chain"
FT                   /id="PRO_0000027912"
FT   CHAIN           408..655
FT                   /note="Hepatocyte growth factor activator long chain"
FT                   /id="PRO_0000027913"
FT   DOMAIN          103..150
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT                   ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          160..198
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          200..240
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          241..279
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          286..367
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          408..646
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          64..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        447
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:15713485"
FT   ACT_SITE        497
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:15713485"
FT   ACT_SITE        598
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:15713485"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        468
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:18077410, ECO:0000269|PubMed:19159218"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..148
FT                   /evidence="ECO:0000250"
FT   DISULFID        164..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        169..186
FT                   /evidence="ECO:0000250"
FT   DISULFID        188..197
FT                   /evidence="ECO:0000250"
FT   DISULFID        202..230
FT                   /evidence="ECO:0000250"
FT   DISULFID        228..237
FT                   /evidence="ECO:0000250"
FT   DISULFID        245..256
FT                   /evidence="ECO:0000250"
FT   DISULFID        250..267
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..278
FT                   /evidence="ECO:0000250"
FT   DISULFID        286..367
FT                   /evidence="ECO:0000250"
FT   DISULFID        307..349
FT                   /evidence="ECO:0000250"
FT   DISULFID        338..362
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..521
FT                   /note="Interchain (between short and long chains)"
FT   DISULFID        432..448
FT   DISULFID        440..510
FT   DISULFID        535..604
FT   DISULFID        567..583
FT   DISULFID        594..622
FT   VARIANT         218
FT                   /note="A -> S (in dbSNP:rs3748034)"
FT                   /id="VAR_051851"
FT   VARIANT         225
FT                   /note="V -> M (in dbSNP:rs16844370)"
FT                   /id="VAR_033651"
FT   VARIANT         231
FT                   /note="F -> L (in dbSNP:rs1987546)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033652"
FT   VARIANT         509
FT                   /note="R -> H (in dbSNP:rs16844401)"
FT                   /id="VAR_024294"
FT   VARIANT         644
FT                   /note="R -> Q (in dbSNP:rs2498323)"
FT                   /id="VAR_024295"
FT   STRAND          422..427
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          430..438
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          441..444
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   HELIX           446..449
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   HELIX           455..457
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          458..463
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          479..484
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          490..492
FT                   /evidence="ECO:0007829|PDB:3K2U"
FT   TURN            493..496
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          499..503
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          506..508
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          509..511
FT                   /evidence="ECO:0007829|PDB:1YC0"
FT   STRAND          514..516
FT                   /evidence="ECO:0007829|PDB:1YBW"
FT   STRAND          534..540
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          543..546
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          555..561
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   HELIX           564..567
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   TURN            570..573
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   HELIX           574..576
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          581..585
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          587..589
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   TURN            595..599
FT                   /evidence="ECO:0007829|PDB:1YBW"
FT   STRAND          601..606
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          609..618
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   TURN            621..623
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   STRAND          625..627
FT                   /evidence="ECO:0007829|PDB:1YBW"
FT   STRAND          629..633
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   HELIX           634..637
FT                   /evidence="ECO:0007829|PDB:2R0L"
FT   HELIX           638..645
FT                   /evidence="ECO:0007829|PDB:2R0L"
SQ   SEQUENCE   655 AA;  70682 MW;  2CF72F1E1B862ED7 CRC64;
     MGRWAWVPSP WPPPGLGPFL LLLLLLLLLP RGFQPQPGGN RTESPEPNAT ATPAIPTILV
     TSVTSETPAT SAPEAEGPQS GGLPPPPRAV PSSSSPQAQA LTEDGRPCRF PFRYGGRMLH
     ACTSEGSAHR KWCATTHNYD RDRAWGYCVE ATPPPGGPAA LDPCASGPCL NGGSCSNTQD
     PQSYHCSCPR AFTGKDCGTE KCFDETRYEY LEGGDRWARV RQGHVEQCEC FGGRTWCEGT
     RHTACLSSPC LNGGTCHLIV ATGTTVCACP PGFAGRLCNI EPDERCFLGN GTGYRGVAST
     SASGLSCLAW NSDLLYQELH VDSVGAAALL GLGPHAYCRN PDNDERPWCY VVKDSALSWE
     YCRLEACESL TRVQLSPDLL ATLPEPASPG RQACGRRHKK RTFLRPRIIG GSSSLPGSHP
     WLAAIYIGDS FCAGSLVHTC WVVSAAHCFS HSPPRDSVSV VLGQHFFNRT TDVTQTFGIE
     KYIPYTLYSV FNPSDHDLVL IRLKKKGDRC ATRSQFVQPI CLPEPGSTFP AGHKCQIAGW
     GHLDENVSGY SSSLREALVP LVADHKCSSP EVYGADISPN MLCAGYFDCK SDACQGDSGG
     PLACEKNGVA YLYGIISWGD GCGRLHKPGV YTRVANYVDW INDRIRPPRR LVAPS
//