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 27-MAR-2024, entry version 218. 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}. 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; 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; 54. DR IntAct; P07093; 20. DR MINT; P07093; -. DR STRING; 9606.ENSP00000415786; -. DR MEROPS; I04.021; -. DR CarbonylDB; P07093; -. DR GlyCosmos; P07093; 3 sites, 1 glycan. DR GlyGen; P07093; 5 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P07093; -. DR PhosphoSitePlus; P07093; -. DR SwissPalm; P07093; -. DR BioMuta; SERPINE2; -. DR DMDM; 121110; -. DR EPD; P07093; -. DR jPOST; P07093; -. DR MassIVE; P07093; -. DR MaxQB; P07093; -. DR PaxDb; 9606-ENSP00000415786; -. DR PeptideAtlas; P07093; -. DR ProteomicsDB; 51945; -. [P07093-1] DR ProteomicsDB; 51946; -. [P07093-2] DR ProteomicsDB; 51947; -. [P07093-3] DR Pumba; P07093; -. DR ABCD; P07093; 4 sequenced antibodies. DR Antibodypedia; 34366; 455 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 AGR; HGNC:8951; -. DR CTD; 5270; -. DR DisGeNET; 5270; -. DR GeneCards; SERPINE2; -. DR HGNC; HGNC:8951; SERPINE2. DR HPA; ENSG00000135919; Group enriched (ovary, 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; 3218836at2759; -. 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; 8 hits in 1159 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 205 other cell types or tissues. DR ExpressionAtlas; P07093; baseline and differential. 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:MGI. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. 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:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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 CDD; cd19573; serpinE2_GDN; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1. DR Gene3D; 2.10.310.10; Serpins superfamily; 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:SF48; GLIA-DERIVED NEXIN; 1. DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00284; SERPIN; 1. DR Genevisible; P07093; HS. 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 //