ID   GBP2_HUMAN              Reviewed;         591 AA.
AC   P32456; Q6GPH0; Q6IAU2; Q86TB0;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 3.
DT   29-SEP-2021, entry version 180.
DE   RecName: Full=Guanylate-binding protein 2;
DE            EC=3.6.5.- {ECO:0000269|PubMed:8706832};
DE   AltName: Full=GTP-binding protein 2;
DE            Short=GBP-2;
DE            Short=HuGBP-2;
DE   AltName: Full=Guanine nucleotide-binding protein 2;
DE   AltName: Full=Interferon-induced guanylate-binding protein 2;
DE   Flags: Precursor;
GN   Name=GBP2;
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 VARIANT ALA-285.
RC   TISSUE=Keratinocyte;
RX   PubMed=1715024; DOI=10.1128/mcb.11.9.4717-4725.1991;
RA   Cheng Y.-S.E., Patterson C.E., Staeheli P.;
RT   "Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus
RT   motif and bind GMP in addition to GDP and GTP.";
RL   Mol. Cell. Biol. 11:4717-4725(1991).
RN   [2]
RP   SEQUENCE REVISION.
RC   TISSUE=Foreskin;
RA   Schwemmle M.;
RL   Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-285 AND GLY-303.
RC   TISSUE=Spinal cord;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-285 AND GLY-303.
RC   TISSUE=Thymus;
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 MRNA], AND VARIANTS ALA-285 AND GLY-303.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-285 AND
RP   GLY-303.
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8706832; DOI=10.1016/0014-5793(96)00628-x;
RA   Neun R., Richter M.F., Staeheli P., Schwemmle M.;
RT   "GTPase properties of the interferon-induced human guanylate-binding
RT   protein 2.";
RL   FEBS Lett. 390:69-72(1996).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=17266443; DOI=10.1089/jir.2007.0086;
RA   Tripal P., Bauer M., Naschberger E., Mortinger T., Hohenadl C., Cornali E.,
RA   Thurau M., Sturzl M.;
RT   "Unique features of different members of the human guanylate-binding
RT   protein family.";
RL   J. Interferon Cytokine Res. 27:44-52(2007).
RN   [11]
RP   SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-588, DIMERIZATION, AND
RP   MUTAGENESIS OF 588-CYS--LEU-591.
RX   PubMed=21151871; DOI=10.1371/journal.pone.0014246;
RA   Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A.,
RA   Reipschlager S., Naschberger E., Herrmann C., Sturzl M.;
RT   "Intracellular trafficking of guanylate-binding proteins is regulated by
RT   heterodimerization in a hierarchical manner.";
RL   PLoS ONE 5:E14246-E14246(2010).
CC   -!- FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions,
CC       but the major reaction product is GDP (PubMed:8706832). Exhibits
CC       antiviral activity against influenza virus. Promotes oxidative killing
CC       and delivers antimicrobial peptides to autophagolysosomes, providing
CC       broad host protection against different pathogen classes (By
CC       similarity). {ECO:0000250|UniProtKB:P32455,
CC       ECO:0000269|PubMed:8706832}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:8706832};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=313 uM for GTP {ECO:0000269|PubMed:8706832};
CC   -!- SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is
CC       required for the association with membranous structures. Heterodimer
CC       with other family members, including GBP1, GBP3, GBP4 and GBP5.
CC       {ECO:0000269|PubMed:21151871}.
CC   -!- INTERACTION:
CC       P32456; P32455: GBP1; NbExp=9; IntAct=EBI-714388, EBI-2869161;
CC       P32456; P32456: GBP2; NbExp=5; IntAct=EBI-714388, EBI-714388;
CC       P32456; Q9H0R5: GBP3; NbExp=3; IntAct=EBI-714388, EBI-2798916;
CC       P32456; Q96PP9: GBP4; NbExp=2; IntAct=EBI-714388, EBI-20840650;
CC       P32456; Q96PP8: GBP5; NbExp=7; IntAct=EBI-714388, EBI-749932;
CC       P32456; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-714388, EBI-6863741;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21151871}.
CC       Cytoplasm, perinuclear region {ECO:0000269|PubMed:21151871}. Golgi
CC       apparatus membrane {ECO:0000269|PubMed:21151871}. Membrane; Lipid-
CC       anchor {ECO:0000269|PubMed:21151871}. Note=GBP2-GBP5 dimers localize to
CC       the Golgi apparatus. {ECO:0000269|PubMed:21151871}.
CC   -!- INDUCTION: By IFNG/IFN-gamma during macrophage activation, and by TNF
CC       and IL1B. {ECO:0000269|PubMed:17266443}.
CC   -!- PTM: Isoprenylation is required for proper subcellular location.
CC       {ECO:0000269|PubMed:21151871}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR   EMBL; M55543; AAA67323.1; -; mRNA.
DR   EMBL; AL832451; CAD89925.1; -; mRNA.
DR   EMBL; AK314325; BAG36973.1; -; mRNA.
DR   EMBL; CR457062; CAG33343.1; -; mRNA.
DR   EMBL; AC104459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471097; EAW73146.1; -; Genomic_DNA.
DR   EMBL; BC073163; AAH73163.1; -; mRNA.
DR   CCDS; CCDS719.1; -.
DR   PIR; S70524; S70524.
DR   RefSeq; NP_004111.2; NM_004120.4.
DR   PDB; 6VKJ; X-ray; 2.10 A; A=5-309.
DR   PDB; 7E58; X-ray; 2.60 A; A/B=1-591.
DR   PDBsum; 6VKJ; -.
DR   PDBsum; 7E58; -.
DR   SMR; P32456; -.
DR   BioGRID; 108904; 46.
DR   IntAct; P32456; 37.
DR   STRING; 9606.ENSP00000359497; -.
DR   iPTMnet; P32456; -.
DR   PhosphoSitePlus; P32456; -.
DR   BioMuta; GBP2; -.
DR   DMDM; 226694187; -.
DR   EPD; P32456; -.
DR   jPOST; P32456; -.
DR   MassIVE; P32456; -.
DR   MaxQB; P32456; -.
DR   PaxDb; P32456; -.
DR   PeptideAtlas; P32456; -.
DR   PRIDE; P32456; -.
DR   ProteomicsDB; 54878; -.
DR   Antibodypedia; 33611; 362 antibodies.
DR   DNASU; 2634; -.
DR   Ensembl; ENST00000370466; ENSP00000359497; ENSG00000162645.
DR   Ensembl; ENST00000464839; ENSP00000434282; ENSG00000162645.
DR   GeneID; 2634; -.
DR   KEGG; hsa:2634; -.
DR   UCSC; uc001dmz.3; human.
DR   CTD; 2634; -.
DR   DisGeNET; 2634; -.
DR   GeneCards; GBP2; -.
DR   HGNC; HGNC:4183; GBP2.
DR   HPA; ENSG00000162645; Low tissue specificity.
DR   MIM; 600412; gene.
DR   neXtProt; NX_P32456; -.
DR   OpenTargets; ENSG00000162645; -.
DR   PharmGKB; PA28597; -.
DR   VEuPathDB; HostDB:ENSG00000162645; -.
DR   eggNOG; KOG2037; Eukaryota.
DR   GeneTree; ENSGT00940000162297; -.
DR   HOGENOM; CLU_018608_2_2_1; -.
DR   InParanoid; P32456; -.
DR   OMA; TFVWTLR; -.
DR   OrthoDB; 1027269at2759; -.
DR   PhylomeDB; P32456; -.
DR   TreeFam; TF331602; -.
DR   PathwayCommons; P32456; -.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR   BioGRID-ORCS; 2634; 13 hits in 1015 CRISPR screens.
DR   ChiTaRS; GBP2; human.
DR   GeneWiki; GBP2; -.
DR   GenomeRNAi; 2634; -.
DR   Pharos; P32456; Tbio.
DR   PRO; PR:P32456; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P32456; protein.
DR   Bgee; ENSG00000162645; Expressed in tendon of biceps brachii and 234 other tissues.
DR   Genevisible; P32456; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0042832; P:defense response to protozoan; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
DR   CDD; cd16269; GBP_C; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030386; G_GB1_RHD3_dom.
DR   InterPro; IPR037684; GBP_C.
DR   InterPro; IPR003191; Guanylate-bd/ATL_C.
DR   InterPro; IPR036543; Guanylate-bd_C_sf.
DR   InterPro; IPR015894; Guanylate-bd_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02263; GBP; 1.
DR   Pfam; PF02841; GBP_C; 1.
DR   SUPFAM; SSF48340; SSF48340; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51715; G_GB1_RHD3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Golgi apparatus; GTP-binding; Hydrolase;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Reference proteome.
FT   CHAIN           1..588
FT                   /note="Guanylate-binding protein 2"
FT                   /id="PRO_0000190964"
FT   PROPEP          589..591
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000370782"
FT   DOMAIN          35..276
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   NP_BIND         45..52
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         67..69
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         97..101
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   REGION          1..309
FT                   /note="GTPase domain (Globular)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         588
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           588
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:21151871"
FT   VARIANT         281
FT                   /note="S -> P (in dbSNP:rs2230336)"
FT                   /id="VAR_054815"
FT   VARIANT         285
FT                   /note="P -> A (in dbSNP:rs1803632)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:1715024, ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|Ref.5, ECO:0000269|Ref.7"
FT                   /id="VAR_054816"
FT   VARIANT         303
FT                   /note="S -> G (in dbSNP:rs2230338)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:17974005, ECO:0000269|Ref.5,
FT                   ECO:0000269|Ref.7"
FT                   /id="VAR_054817"
FT   MUTAGEN         588..591
FT                   /note="Missing: No effect on subcellular location by
FT                   confocal microscopy, but loss of membrane-association by
FT                   subcellular fractionation."
FT                   /evidence="ECO:0000269|PubMed:21151871"
FT   CONFLICT        310
FT                   /note="M -> R (in Ref. 8; AAH73163)"
FT                   /evidence="ECO:0000305"
FT   STRAND          11..15
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           25..32
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   STRAND          36..44
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           51..59
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   STRAND          77..84
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   STRAND          124..133
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           136..154
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   TURN            157..161
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           167..172
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   STRAND          175..182
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           196..204
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   TURN            215..217
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           218..227
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   STRAND          230..235
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           242..250
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           258..274
FT                   /evidence="ECO:0007829|PDB:6VKJ"
FT   HELIX           288..303
FT                   /evidence="ECO:0007829|PDB:6VKJ"
SQ   SEQUENCE   591 AA;  67209 MW;  B09B3C2F3C3E1EA2 CRC64;
     MAPEINLPGP MSLIDNTKGQ LVVNPEALKI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG
     KKNGFSLGST VKSHTKGIWM WCVPHPKKPE HTLVLLDTEG LGDIEKGDNE NDSWIFALAI
     LLSSTFVYNS MGTINQQAMD QLHYVTELTD RIKANSSPGN NSVDDSADFV SFFPAFVWTL
     RDFTLELEVD GEPITADDYL ELSLKLRKGT DKKSKSFNDP RLCIRKFFPK RKCFVFDWPA
     PKKYLAHLEQ LKEEELNPDF IEQVAEFCSY ILSHSNVKTL SGGIPVNGPR LESLVLTYVN
     AISSGDLPCM ENAVLALAQI ENSAAVEKAI AHYEQQMGQK VQLPTETLQE LLDLHRDSER
     EAIEVFMKNS FKDVDQMFQR KLGAQLEARR DDFCKQNSKA SSDCCMALLQ DIFGPLEEDV
     KQGTFSKPGG YRLFTQKLQE LKNKYYQVPR KGIQAKEVLK KYLESKEDVA DALLQTDQSL
     SEKEKAIEVE RIKAESAEAA KKMLEEIQKK NEEMMEQKEK SYQEHVKQLT EKMERDRAQL
     MAEQEKTLAL KLQEQERLLK EGFENESKRL QKDIWDIQMR SKSLEPICNI L
//