GDN_HUMAN
ID GDN_HUMAN Reviewed; 398 AA.
AC P07093; B2R6A4; B4DIF2; Q53S15; Q5D0C4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Glia-derived nexin;
DE Short=GDN;
DE AltName: Full=Peptidase inhibitor 7;
DE Short=PI-7;
DE AltName: Full=Protease nexin 1;
DE Short=PN-1;
DE AltName: Full=Protease nexin I;
DE AltName: Full=Serpin E2;
DE Flags: Precursor;
GN Name=SERPINE2; Synonyms=PI7, PN1;
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 2).
RX PubMed=3427015; DOI=10.1021/bi00394a016;
RA Sommer J., Gloor S.M., Rovelli G.F., Hofsteenge J., Nick H., Meier R.,
RA Monard D.;
RT "cDNA sequence coding for a rat glia-derived nexin and its homology to
RT members of the serpin superfamily.";
RL Biochemistry 26:6407-6410(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2877744; DOI=10.1016/0092-8674(86)90511-8;
RA Gloor S.M., Odink K., Guenther J., Nick H., Monard D.;
RT "A glia-derived neurite promoting factor with protease inhibitory activity
RT belongs to the protease nexins.";
RL Cell 47:687-693(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA McGrogan M., Kennedy J., Li M.P., Hsu C., Scott R.W., Simonsen C.C.,
RA Baker J.B.;
RT "Molecular cloning and expression of two forms of human protease nexin I.";
RL Biotechnology (N.Y.) 6:172-177(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Hippocampus, and Thalamus;
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=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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skin, and Testis;
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 PROTEIN SEQUENCE OF 20-47, AND CHARACTERIZATION.
RX PubMed=3997857; DOI=10.1016/s0021-9258(18)88883-4;
RA Scott R.W., Bergman B.L., Bajpai A., Hersh R.T., Rodriguez H., Jones B.N.,
RA Barreda C., Watts S., Baker J.B.;
RT "Protease nexin. Properties and a modified purification procedure.";
RL J. Biol. Chem. 260:7029-7034(1985).
RN [9]
RP PROTEIN SEQUENCE OF 20-34.
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 [10]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-204.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Serine protease inhibitor with activity toward thrombin,
CC trypsin, and urokinase. Promotes neurite extension by inhibiting
CC thrombin. Binds heparin.
CC -!- INTERACTION:
CC P07093; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-10195168, EBI-10175124;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P07093-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07093-2; Sequence=VSP_038367;
CC Name=3;
CC IsoId=P07093-3; Sequence=VSP_043668, VSP_038367;
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; M17783; AAA35883.1; -; mRNA.
DR EMBL; AK295564; BAG58464.1; -; mRNA.
DR EMBL; AK312499; BAG35401.1; -; mRNA.
DR EMBL; AC073641; AAY14926.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70821.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70823.1; -; Genomic_DNA.
DR EMBL; BC015663; AAH15663.1; -; mRNA.
DR EMBL; BC042628; AAH42628.1; -; mRNA.
DR CCDS; CCDS2460.1; -. [P07093-1]
DR CCDS; CCDS46525.1; -. [P07093-3]
DR CCDS; CCDS46526.1; -. [P07093-2]
DR PIR; A37274; A37274.
DR RefSeq; NP_001130000.1; NM_001136528.1. [P07093-2]
DR RefSeq; NP_001130002.1; NM_001136530.1. [P07093-3]
DR RefSeq; NP_006207.1; NM_006216.3. [P07093-1]
DR RefSeq; XP_016859818.1; XM_017004329.1.
DR RefSeq; XP_016859819.1; XM_017004330.1. [P07093-1]
DR RefSeq; XP_016859820.1; XM_017004331.1.
DR RefSeq; XP_016859821.1; XM_017004332.1. [P07093-2]
DR PDB; 4DY0; X-ray; 2.35 A; A/B=20-398.
DR PDB; 4DY7; X-ray; 2.80 A; C/F=20-398.
DR PDBsum; 4DY0; -.
DR PDBsum; 4DY7; -.
DR AlphaFoldDB; P07093; -.
DR SMR; P07093; -.
DR BioGRID; 111288; 52.
DR IntAct; P07093; 18.
DR MINT; P07093; -.
DR STRING; 9606.ENSP00000415786; -.
DR MEROPS; I04.021; -.
DR CarbonylDB; P07093; -.
DR GlyGen; P07093; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P07093; -.
DR PhosphoSitePlus; P07093; -.
DR BioMuta; SERPINE2; -.
DR DMDM; 121110; -.
DR EPD; P07093; -.
DR jPOST; P07093; -.
DR MassIVE; P07093; -.
DR MaxQB; P07093; -.
DR PaxDb; P07093; -.
DR PeptideAtlas; P07093; -.
DR PRIDE; P07093; -.
DR ProteomicsDB; 51945; -. [P07093-1]
DR ProteomicsDB; 51946; -. [P07093-2]
DR ProteomicsDB; 51947; -. [P07093-3]
DR ABCD; P07093; 4 sequenced antibodies.
DR Antibodypedia; 34366; 391 antibodies from 31 providers.
DR DNASU; 5270; -.
DR Ensembl; ENST00000258405.9; ENSP00000258405.4; ENSG00000135919.14. [P07093-1]
DR Ensembl; ENST00000409304.6; ENSP00000386412.1; ENSG00000135919.14. [P07093-2]
DR Ensembl; ENST00000409840.7; ENSP00000386969.3; ENSG00000135919.14. [P07093-2]
DR Ensembl; ENST00000447280.6; ENSP00000415786.2; ENSG00000135919.14. [P07093-3]
DR GeneID; 5270; -.
DR KEGG; hsa:5270; -.
DR MANE-Select; ENST00000409304.6; ENSP00000386412.1; NM_001136528.2; NP_001130000.1. [P07093-2]
DR UCSC; uc002vnu.3; human. [P07093-1]
DR CTD; 5270; -.
DR DisGeNET; 5270; -.
DR GeneCards; SERPINE2; -.
DR HGNC; HGNC:8951; SERPINE2.
DR HPA; ENSG00000135919; Tissue enriched (placenta).
DR MIM; 177010; gene.
DR neXtProt; NX_P07093; -.
DR OpenTargets; ENSG00000135919; -.
DR PharmGKB; PA269; -.
DR VEuPathDB; HostDB:ENSG00000135919; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158424; -.
DR HOGENOM; CLU_023330_0_4_1; -.
DR InParanoid; P07093; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P07093; -.
DR TreeFam; TF352620; -.
DR PathwayCommons; P07093; -.
DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
DR SignaLink; P07093; -.
DR BioGRID-ORCS; 5270; 7 hits in 1078 CRISPR screens.
DR ChiTaRS; SERPINE2; human.
DR GeneWiki; SERPINE2; -.
DR GenomeRNAi; 5270; -.
DR Pharos; P07093; Tbio.
DR PRO; PR:P07093; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P07093; protein.
DR Bgee; ENSG00000135919; Expressed in decidua and 203 other tissues.
DR ExpressionAtlas; P07093; baseline and differential.
DR Genevisible; P07093; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0031594; C:neuromuscular junction; ISS:BHF-UCL.
DR GO; GO:0031091; C:platelet alpha granule; IDA:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0021683; P:cerebellar granular layer morphogenesis; IEA:Ensembl.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IEA:Ensembl.
DR GO; GO:0060384; P:innervation; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0042628; P:mating plug formation; IEA:Ensembl.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IDA:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IMP:BHF-UCL.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:BHF-UCL.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0010955; P:negative regulation of protein processing; IC:BHF-UCL.
DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0010766; P:negative regulation of sodium ion transport; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; IEA:Ensembl.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; IDA:BHF-UCL.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; NAS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0048505; P:regulation of timing of cell differentiation; IEA:Ensembl.
DR GO; GO:0032940; P:secretion by cell; IEA:Ensembl.
DR GO; GO:0033363; P:secretory granule organization; IEA:Ensembl.
DR GO; GO:0061108; P:seminal vesicle epithelium development; IEA:Ensembl.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW Direct protein sequencing; Glycoprotein; Heparin-binding; Neurogenesis;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:3997857"
FT CHAIN 20..398
FT /note="Glia-derived nexin"
FT /id="PRO_0000032504"
FT SITE 365..366
FT /note="Reactive bond"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MSDCRSSLVEGTM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043668"
FT VAR_SEQ 329..330
FT /note="TG -> R (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:3427015"
FT /id="VSP_038367"
FT VARIANT 51
FT /note="I -> M (in dbSNP:rs3795875)"
FT /id="VAR_051955"
FT VARIANT 204
FT /note="K -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036027"
FT CONFLICT 159
FT /note="N -> D (in Ref. 4; BAG35401)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="S -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 24..45
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:4DY0"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:4DY0"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4DY0"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4DY7"
FT STRAND 214..232
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 249..260
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4DY7"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:4DY0"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:4DY0"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:4DY0"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:4DY7"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:4DY7"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:4DY7"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:4DY0"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:4DY0"
FT STRAND 388..396
FT /evidence="ECO:0007829|PDB:4DY0"
SQ SEQUENCE 398 AA; 44002 MW; 2A165604E2CBE6B8 CRC64;
MNWHLPLFLL ASVTLPSICS HFNPLSLEEL GSNTGIQVFN QIVKSRPHDN IVISPHGIAS
VLGMLQLGAD GRTKKQLAMV MRYGVNGVGK ILKKINKAIV SKKNKDIVTV ANAVFVKNAS
EIEVPFVTRN KDVFQCEVRN VNFEDPASAC DSINAWVKNE TRDMIDNLLS PDLIDGVLTR
LVLVNAVYFK GLWKSRFQPE NTKKRTFVAA DGKSYQVPML AQLSVFRCGS TSAPNDLWYN
FIELPYHGES ISMLIALPTE SSTPLSAIIP HISTKTIDSW MSIMVPKRVQ VILPKFTAVA
QTDLKEPLKV LGITDMFDSS KANFAKITTG SENLHVSHIL QKAKIEVSED GTKASAATTA
ILIARSSPPW FIVDRPFLFF IRHNPTGAVL FMGQINKP
