HGFA_HUMAN
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 03-AUG-2022, entry version 199.
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}.
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; 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 GlyGen; Q04756; 10 sites, 14 N-linked glycans (4 sites), 3 O-linked glycans (5 sites).
DR iPTMnet; Q04756; -.
DR PhosphoSitePlus; Q04756; -.
DR BioMuta; HGFAC; -.
DR DMDM; 547643; -.
DR jPOST; Q04756; -.
DR MassIVE; Q04756; -.
DR MaxQB; Q04756; -.
DR PaxDb; Q04756; -.
DR PeptideAtlas; Q04756; -.
DR PRIDE; Q04756; -.
DR ProteomicsDB; 58278; -.
DR ABCD; Q04756; 3 sequenced antibodies.
DR Antibodypedia; 3925; 158 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 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; 1314811at2759; -.
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 1067 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 87 other tissues.
DR ExpressionAtlas; Q04756; baseline and differential.
DR Genevisible; Q04756; HS.
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; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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; -; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 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 Pfam; PF00008; EGF; 1.
DR Pfam; PF00039; fn1; 1.
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 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 2.
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.
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
