GBP5_HUMAN
ID GBP5_HUMAN Reviewed; 586 AA.
AC Q96PP8; B2RCE1; Q86TM5;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Guanylate-binding protein 5;
DE EC=3.6.5.- {ECO:0000269|PubMed:20180847, ECO:0000269|PubMed:22461501};
DE AltName: Full=GBP-TA antigen;
DE AltName: Full=GTP-binding protein 5;
DE Short=GBP-5;
DE AltName: Full=Guanine nucleotide-binding protein 5;
DE Flags: Precursor;
GN Name=GBP5; ORFNames=UNQ2427/PRO4987;
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 1).
RA Avdalovic A., Fu H., Tsurushita N.;
RT "Human GBP-4 and -5: new members of the IFN-gamma-inducible guanylate
RT binding protein family.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Lymphoma;
RX PubMed=15175044; DOI=10.1111/j.0022-202x.2004.22613.x;
RA Fellenberg F., Hartmann T.B., Dummer R., Usener D., Schadendorf D.,
RA Eichmuller S.;
RT "GBP-5 splicing variants: New guanylate-binding proteins with tumor-
RT associated expression and antigenicity.";
RL J. Invest. Dermatol. 122:1510-1517(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP SUBCELLULAR LOCATION, AND INDUCTION BY IFNG.
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DIMERIZATION.
RX PubMed=20180847; DOI=10.1111/j.1742-4658.2010.07586.x;
RA Wehner M., Herrmann C.;
RT "Biochemical properties of the human guanylate binding protein 5 and a
RT tumor-specific truncated splice variant.";
RL FEBS J. 277:1597-1605(2010).
RN [9]
RP SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-583, MUTAGENESIS OF
RP 583-CYS--LEU-586, AND DIMERIZATION.
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).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH NLRP3, OLIGOMERIZATION,
RP MUTAGENESIS OF 51-LYS-SER-52, AND INDUCTION BY IFNG.
RX PubMed=22461501; DOI=10.1126/science.1217141;
RA Shenoy A.R., Wellington D.A., Kumar P., Kassa H., Booth C.J., Cresswell P.,
RA MacMicking J.D.;
RT "GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals.";
RL Science 336:481-485(2012).
CC -!- FUNCTION: As an activator of NLRP3 inflammasome assembly, plays a role
CC in innate immunity and inflammation. Promotes selective NLRP3
CC inflammasome assembly in response to microbial and soluble, but not
CC crystalline, agents (PubMed:22461501). Hydrolyzes GTP, but in contrast
CC to other family members, does not produce GMP (PubMed:20180847).
CC {ECO:0000269|PubMed:20180847, ECO:0000269|PubMed:22461501}.
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:20180847, ECO:0000269|PubMed:22461501};
CC -!- SUBUNIT: Homodimer (PubMed:21151871). Heterodimer with other family
CC members, including GBP1, GBP2, GBP3 and GBP4 (PubMed:21151871).
CC Dimerization is nucleotide-dependent; isoform 1 and isoform 2 form
CC dimers when GTP-bound. GDP-bound isoform 2 is monomeric, while isoform
CC 1 remains dimeric (PubMed:20180847). Dimerization regulates subcellular
CC location. May also form tetramers (dimer of dimers) in the presence of
CC GTP (PubMed:20180847). Interacts with NLRP3, possibly in its tetrameric
CC form, and promotes PYCARD/ASC polymerization (PubMed:22461501).
CC {ECO:0000269|PubMed:20180847, ECO:0000269|PubMed:21151871,
CC ECO:0000269|PubMed:22461501}.
CC -!- INTERACTION:
CC Q96PP8; P32455: GBP1; NbExp=9; IntAct=EBI-749932, EBI-2869161;
CC Q96PP8; P32456: GBP2; NbExp=7; IntAct=EBI-749932, EBI-714388;
CC Q96PP8; Q9H0R5: GBP3; NbExp=2; IntAct=EBI-749932, EBI-2798916;
CC Q96PP8; Q96PP9: GBP4; NbExp=2; IntAct=EBI-749932, EBI-20840650;
CC Q96PP8; Q96PP8: GBP5; NbExp=10; IntAct=EBI-749932, EBI-749932;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17266443,
CC ECO:0000269|PubMed:21151871}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:17266443, ECO:0000269|PubMed:21151871}; Lipid-
CC anchor {ECO:0000269|PubMed:21151871}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q8CFB4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GBP-5a/b;
CC IsoId=Q96PP8-1; Sequence=Displayed;
CC Name=2; Synonyms=GBP-5ta;
CC IsoId=Q96PP8-2; Sequence=VSP_044362, VSP_044363;
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood monocytes (at protein
CC level). {ECO:0000269|PubMed:15175044}.
CC -!- INDUCTION: By IFNG in endothelial cells and in LPS-primed macrophages.
CC {ECO:0000269|PubMed:17266443, ECO:0000269|PubMed:22461501}.
CC -!- PTM: Isoprenylation is required for proper subcellular location.
CC {ECO:0000269|PubMed:21151871}.
CC -!- MISCELLANEOUS: [Isoform 2]: Antigenic tumor-specific truncated splice
CC form. {ECO:0000305}.
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; AF288815; AAL02055.1; -; mRNA.
DR EMBL; AF328727; AAO40731.1; -; mRNA.
DR EMBL; AF430642; AAN39035.1; -; mRNA.
DR EMBL; AF430643; AAN39036.1; -; mRNA.
DR EMBL; AY358953; AAQ89312.1; -; mRNA.
DR EMBL; AK315064; BAG37538.1; -; mRNA.
DR EMBL; CH471097; EAW73141.1; -; Genomic_DNA.
DR EMBL; BC031639; AAH31639.1; -; mRNA.
DR CCDS; CCDS722.1; -. [Q96PP8-1]
DR RefSeq; NP_001127958.1; NM_001134486.2. [Q96PP8-1]
DR RefSeq; NP_443174.1; NM_052942.3. [Q96PP8-1]
DR PDB; 7CKF; X-ray; 2.28 A; A/B=1-315.
DR PDB; 7E59; X-ray; 3.00 A; A/B/C/G=1-486.
DR PDB; 7E5A; X-ray; 2.50 A; A/B=1-486.
DR PDBsum; 7CKF; -.
DR PDBsum; 7E59; -.
DR PDBsum; 7E5A; -.
DR AlphaFoldDB; Q96PP8; -.
DR SMR; Q96PP8; -.
DR BioGRID; 125431; 14.
DR IntAct; Q96PP8; 16.
DR MINT; Q96PP8; -.
DR STRING; 9606.ENSP00000359488; -.
DR GlyGen; Q96PP8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96PP8; -.
DR PhosphoSitePlus; Q96PP8; -.
DR BioMuta; GBP5; -.
DR DMDM; 37999757; -.
DR EPD; Q96PP8; -.
DR jPOST; Q96PP8; -.
DR MassIVE; Q96PP8; -.
DR MaxQB; Q96PP8; -.
DR PaxDb; Q96PP8; -.
DR PeptideAtlas; Q96PP8; -.
DR PRIDE; Q96PP8; -.
DR ProteomicsDB; 77725; -. [Q96PP8-1]
DR Antibodypedia; 33615; 330 antibodies from 32 providers.
DR DNASU; 115362; -.
DR Ensembl; ENST00000370459.8; ENSP00000359488.3; ENSG00000154451.15. [Q96PP8-1]
DR GeneID; 115362; -.
DR KEGG; hsa:115362; -.
DR MANE-Select; ENST00000370459.8; ENSP00000359488.3; NM_052942.5; NP_443174.1.
DR UCSC; uc057iek.1; human. [Q96PP8-1]
DR CTD; 115362; -.
DR DisGeNET; 115362; -.
DR GeneCards; GBP5; -.
DR HGNC; HGNC:19895; GBP5.
DR HPA; ENSG00000154451; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 611467; gene.
DR neXtProt; NX_Q96PP8; -.
DR OpenTargets; ENSG00000154451; -.
DR PharmGKB; PA134862968; -.
DR VEuPathDB; HostDB:ENSG00000154451; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000162684; -.
DR InParanoid; Q96PP8; -.
DR OMA; CETHHAS; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q96PP8; -.
DR TreeFam; TF331602; -.
DR PathwayCommons; Q96PP8; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q96PP8; -.
DR BioGRID-ORCS; 115362; 16 hits in 1073 CRISPR screens.
DR GenomeRNAi; 115362; -.
DR Pharos; Q96PP8; Tbio.
DR PRO; PR:Q96PP8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96PP8; protein.
DR Bgee; ENSG00000154451; Expressed in granulocyte and 121 other tissues.
DR ExpressionAtlas; Q96PP8; baseline and differential.
DR Genevisible; Q96PP8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA: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; IEP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:UniProtKB.
DR GO; GO:0032741; P:positive regulation of interleukin-18 production; ISS:UniProtKB.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
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; Alternative splicing; Antimicrobial; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Hydrolase; Immunity;
KW Inflammatory response; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..583
FT /note="Guanylate-binding protein 5"
FT /id="PRO_0000190969"
FT PROPEP 584..586
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370785"
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 REGION 1..306
FT /note="NLRP3-binding"
FT /evidence="ECO:0000269|PubMed:22461501"
FT REGION 529..586
FT /note="Required for tetramerization, but not for
FT dimerization"
FT /evidence="ECO:0000269|PubMed:22461501"
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 583
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 583
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:21151871"
FT VAR_SEQ 489
FT /note="E -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15175044"
FT /id="VSP_044362"
FT VAR_SEQ 490..586
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15175044"
FT /id="VSP_044363"
FT VARIANT 4
FT /note="E -> Q (in dbSNP:rs17130763)"
FT /id="VAR_053104"
FT VARIANT 35
FT /note="T -> M (in dbSNP:rs3806339)"
FT /id="VAR_033956"
FT MUTAGEN 51..52
FT /note="KS->AA: Loss of GTPase activity. No effect on
FT tetramerization."
FT /evidence="ECO:0000269|PubMed:22461501"
FT MUTAGEN 583..586
FT /note="Missing: Loss of isoprenylation and of localization
FT at the Golgi apparatus."
FT /evidence="ECO:0000269|PubMed:21151871"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7E59"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:7E5A"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 36..50
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:7CKF"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:7E5A"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 212..227
FT /evidence="ECO:0007829|PDB:7E5A"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:7CKF"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 258..274
FT /evidence="ECO:0007829|PDB:7CKF"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:7CKF"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:7CKF"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:7E59"
FT HELIX 313..335
FT /evidence="ECO:0007829|PDB:7E5A"
FT HELIX 349..369
FT /evidence="ECO:0007829|PDB:7E5A"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:7E5A"
FT HELIX 377..412
FT /evidence="ECO:0007829|PDB:7E5A"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:7E5A"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:7E5A"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:7E5A"
FT HELIX 455..465
FT /evidence="ECO:0007829|PDB:7E5A"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:7E5A"
FT HELIX 469..482
FT /evidence="ECO:0007829|PDB:7E5A"
SQ SEQUENCE 586 AA; 66617 MW; 95DDC02F0FB705D0 CRC64;
MALEIHMSDP MCLIENFNEQ LKVNQEALEI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG
KNKGFSVAST VQSHTKGIWI WCVPHPNWPN HTLVLLDTEG LGDVEKADNK NDIQIFALAL
LLSSTFVYNT VNKIDQGAID LLHNVTELTD LLKARNSPDL DRVEDPADSA SFFPDLVWTL
RDFCLGLEID GQLVTPDEYL ENSLRPKQGS DQRVQNFNLP RLCIQKFFPK KKCFIFDLPA
HQKKLAQLET LPDDELEPEF VQQVTEFCSY IFSHSMTKTL PGGIMVNGSR LKNLVLTYVN
AISSGDLPCI ENAVLALAQR ENSAAVQKAI AHYDQQMGQK VQLPMETLQE LLDLHRTSER
EAIEVFMKNS FKDVDQSFQK ELETLLDAKQ NDICKRNLEA SSDYCSALLK DIFGPLEEAV
KQGIYSKPGG HNLFIQKTEE LKAKYYREPR KGIQAEEVLQ KYLKSKESVS HAILQTDQAL
TETEKKKKEA QVKAEAEKAE AQRLAAIQRQ NEQMMQERER LHQEQVRQME IAKQNWLAEQ
QKMQEQQMQE QAAQLSTTFQ AQNRSLLSEL QHAQRTVNND DPCVLL
