GBP2_HUMAN
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 03-AUG-2022, entry version 183.
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). Confers protection to the protozoan pathogen Toxoplasma
CC gondii (By similarity). {ECO:0000250|UniProtKB:P32455,
CC ECO:0000250|UniProtKB:Q9Z0E6, 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}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q9Z0E6}. Note=GBP2-GBP5 dimers localize to the
CC 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 AlphaFoldDB; P32456; -.
DR SMR; P32456; -.
DR BioGRID; 108904; 50.
DR IntAct; P32456; 37.
DR MINT; P32456; -.
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; 388 antibodies from 29 providers.
DR DNASU; 2634; -.
DR Ensembl; ENST00000370466.4; ENSP00000359497.3; ENSG00000162645.13.
DR Ensembl; ENST00000464839.5; ENSP00000434282.1; ENSG00000162645.13.
DR GeneID; 2634; -.
DR KEGG; hsa:2634; -.
DR MANE-Select; ENST00000370466.4; ENSP00000359497.3; NM_004120.5; NP_004111.2.
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 SignaLink; P32456; -.
DR BioGRID-ORCS; 2634; 21 hits in 1081 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 195 other tissues.
DR Genevisible; P32456; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
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; Antimicrobial; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; GTP-binding; Hydrolase; Immunity; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; 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 REGION 1..309
FT /note="GTPase domain (Globular)"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 67..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 97..101
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
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 STRAND 20..23
FT /evidence="ECO:0007829|PDB:7E58"
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 STRAND 187..189
FT /evidence="ECO:0007829|PDB:7E58"
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 TURN 281..283
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 288..303
FT /evidence="ECO:0007829|PDB:6VKJ"
FT HELIX 310..340
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 348..368
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 377..412
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 430..447
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 455..465
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 467..476
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 482..560
FT /evidence="ECO:0007829|PDB:7E58"
FT HELIX 564..581
FT /evidence="ECO:0007829|PDB:7E58"
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
