IIGP1_MOUSE
ID IIGP1_MOUSE Reviewed; 413 AA.
AC Q9QZ85; Q9Z1M3;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Interferon-inducible GTPase 1;
DE EC=3.6.5.- {ECO:0000269|PubMed:12732635};
GN Name=Iigp1; Synonyms=Irga6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=Embryonic fibroblast, and Macrophage;
RX PubMed=9862701;
RA Boehm U., Guethlein L., Klamp T., Ozbek K., Schaub A., Fuetterer A.,
RA Pfeffer K., Howard J.C.;
RT "Two families of GTPases dominate the complex cellular response to IFN-
RT gamma.";
RL J. Immunol. 161:6715-6723(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Splenocyte;
RX PubMed=11907101; DOI=10.4049/jimmunol.168.7.3428;
RA Zerrahn J., Schaible U.E., Brinkmann V., Guhlich U., Kaufmann S.H.E.;
RT "The IFN-inducible Golgi- and endoplasmic reticulum- associated 47-kDa
RT GTPase IIGP is transiently expressed during listeriosis.";
RL J. Immunol. 168:3428-3436(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP INTERACTION WITH HOOK3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-83.
RX PubMed=15075236; DOI=10.1242/jcs.01039;
RA Kaiser F., Kaufmann S.H.E., Zerrahn J.;
RT "IIGP, a member of the IFN inducible and microbial defense mediating 47 kDa
RT GTPase family, interacts with the microtubule binding protein hook3.";
RL J. Cell Sci. 117:1747-1756(2004).
RN [7]
RP SUBCELLULAR LOCATION, PROBABLE MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF
RP GLY-2.
RC STRAIN=C57BL/6J;
RX PubMed=15294976; DOI=10.4049/jimmunol.173.4.2594;
RA Martens S., Sabel K., Lange R., Uthaiah R., Wolf E., Howard J.C.;
RT "Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-
RT 47 and IIGP1 on cellular membranes: retargeting to plasma membrane induced
RT by phagocytosis.";
RL J. Immunol. 173:2594-2606(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-82.
RC STRAIN=C57BL/6J;
RX PubMed=16304607; DOI=10.1371/journal.ppat.0010024;
RA Martens S., Parvanova I., Zerrahn J., Griffiths G., Schell G.,
RA Reichmann G., Howard J.C.;
RT "Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-
RT resistance GTPases.";
RL PLoS Pathog. 1:E24-E24(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-82 AND SER-83.
RC STRAIN=C57BL/6J;
RX PubMed=18772884; DOI=10.1038/emboj.2008.176;
RA Hunn J.P., Koenen-Waisman S., Papic N., Schroeder N., Pawlowski N.,
RA Lange R., Kaiser F., Zerrahn J., Martens S., Howard J.C.;
RT "Regulatory interactions between IRG resistance GTPases in the cellular
RT response to Toxoplasma gondii.";
RL EMBO J. 27:2495-2509(2008).
RN [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18784077; DOI=10.1074/jbc.m804846200;
RA Papic N., Hunn J.P., Pawlowski N., Zerrahn J., Howard J.C.;
RT "Inactive and active states of the interferon-inducible resistance GTPase,
RT Irga6, in vivo.";
RL J. Biol. Chem. 283:32143-32151(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19242543; DOI=10.1371/journal.pone.0004588;
RA Al-Zeer M.A., Al-Younes H.M., Braun P.R., Zerrahn J., Meyer T.F.;
RT "IFN-gamma-inducible Irga6 mediates host resistance against Chlamydia
RT trachomatis via autophagy.";
RL PLoS ONE 4:E4588-E4588(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-411 IN COMPLEX WITH GTP,
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=12732635; DOI=10.1074/jbc.m211973200;
RA Uthaiah R.C., Praefcke G.J.K., Howard J.C., Herrmann C.;
RT "IIGP1, an interferon-gamma-inducible 47-kDa GTPase of the mouse, showing
RT cooperative enzymatic activity and GTP-dependent multimerization.";
RL J. Biol. Chem. 278:29336-29343(2003).
CC -!- FUNCTION: GTPase with low activity. Has higher affinity for GDP than
CC for GTP. Plays a role in resistance to intracellular pathogens.
CC Required for disruption of the parasitophorous vacuole formed following
CC T.gondii infection and subsequent killing of the parasite. Mediates
CC resistance to C.trachomatis infection by targeting bacterial inclusions
CC to autophagosomes for subsequent lysosomal destruction.
CC {ECO:0000269|PubMed:11907101, ECO:0000269|PubMed:12732635,
CC ECO:0000269|PubMed:16304607, ECO:0000269|PubMed:19242543}.
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:12732635};
CC -!- SUBUNIT: Monomer, as apoenzyme and in the GDP-bound form. Homooligomer,
CC upon GTP binding. Interacts with HOOK3. {ECO:0000269|PubMed:12732635,
CC ECO:0000269|PubMed:15075236, ECO:0000269|PubMed:18784077}.
CC -!- INTERACTION:
CC Q9QZ85; Q9QZ85: Iigp1; NbExp=2; IntAct=EBI-6910173, EBI-6910173;
CC Q9QZ85; A1E140: ROP18; Xeno; NbExp=3; IntAct=EBI-6910173, EBI-15902261;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus membrane; Peripheral membrane
CC protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
CC Golgi apparatus, Golgi stack membrane; Peripheral membrane protein.
CC Parasitophorous vacuole membrane. Note=Localizes to the bacterial
CC inclusions formed following C.trachomatis infection. Accumulates in a
CC GTP-bound form on the parasitophorous vacuole membranes formed
CC following T.gondii infection but exists in a GDP-bound form in
CC uninfected cells.
CC -!- INDUCTION: Up-regulated by IFNG, IFNA1 and lipopolysaccharide (LPS)
CC within 20 hours. Transiently up-regulated during the early stages of
CC infection by Listeria monocytogenes. After 6 days expression is back to
CC basal levels. {ECO:0000269|PubMed:11907101,
CC ECO:0000269|PubMed:9862701}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. IRG family. {ECO:0000255|PROSITE-ProRule:PRU01053,
CC ECO:0000305}.
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DR EMBL; AJ007971; CAA07798.1; -; mRNA.
DR EMBL; AF194871; AAF07195.1; -; mRNA.
DR EMBL; AK153060; BAE31686.1; -; mRNA.
DR EMBL; CT010300; CAJ18508.1; -; mRNA.
DR EMBL; BC004649; AAH04649.1; -; mRNA.
DR CCDS; CCDS29270.1; -.
DR RefSeq; NP_001139747.1; NM_001146275.1.
DR RefSeq; NP_068564.4; NM_021792.4.
DR RefSeq; XP_011245279.1; XM_011246977.2.
DR RefSeq; XP_011245280.1; XM_011246978.2.
DR RefSeq; XP_011245281.1; XM_011246979.2.
DR RefSeq; XP_011245282.1; XM_011246980.1.
DR PDB; 1TPZ; X-ray; 2.00 A; A/B=1-411.
DR PDB; 1TQ2; X-ray; 2.70 A; A/B=1-411.
DR PDB; 1TQ4; X-ray; 1.95 A; A=1-413.
DR PDB; 1TQ6; X-ray; 2.70 A; A=1-413.
DR PDB; 1TQD; X-ray; 2.30 A; A/B=1-413.
DR PDB; 4LV5; X-ray; 1.70 A; B=1-413.
DR PDB; 4LV8; X-ray; 1.72 A; B=1-413.
DR PDB; 5FPH; X-ray; 3.20 A; A/B/C/D/E/F/G=1-413.
DR PDBsum; 1TPZ; -.
DR PDBsum; 1TQ2; -.
DR PDBsum; 1TQ4; -.
DR PDBsum; 1TQ6; -.
DR PDBsum; 1TQD; -.
DR PDBsum; 4LV5; -.
DR PDBsum; 4LV8; -.
DR PDBsum; 5FPH; -.
DR AlphaFoldDB; Q9QZ85; -.
DR SMR; Q9QZ85; -.
DR BioGRID; 208563; 4.
DR CORUM; Q9QZ85; -.
DR DIP; DIP-58958N; -.
DR IntAct; Q9QZ85; 2.
DR STRING; 10090.ENSMUSP00000032473; -.
DR iPTMnet; Q9QZ85; -.
DR MetOSite; Q9QZ85; -.
DR PhosphoSitePlus; Q9QZ85; -.
DR SwissPalm; Q9QZ85; -.
DR EPD; Q9QZ85; -.
DR jPOST; Q9QZ85; -.
DR PaxDb; Q9QZ85; -.
DR PRIDE; Q9QZ85; -.
DR ProteomicsDB; 267305; -.
DR DNASU; 60440; -.
DR Ensembl; ENSMUST00000032473; ENSMUSP00000032473; ENSMUSG00000054072.
DR Ensembl; ENSMUST00000066912; ENSMUSP00000063390; ENSMUSG00000054072.
DR Ensembl; ENSMUST00000237185; ENSMUSP00000157568; ENSMUSG00000054072.
DR GeneID; 60440; -.
DR KEGG; mmu:60440; -.
DR UCSC; uc008fac.2; mouse.
DR CTD; 60440; -.
DR MGI; MGI:1926259; Iigp1.
DR VEuPathDB; HostDB:ENSMUSG00000054072; -.
DR eggNOG; ENOG502QS9R; Eukaryota.
DR GeneTree; ENSGT00950000183007; -.
DR HOGENOM; CLU_015342_2_0_1; -.
DR InParanoid; Q9QZ85; -.
DR OMA; NDMKLAK; -.
DR OrthoDB; 688334at2759; -.
DR PhylomeDB; Q9QZ85; -.
DR TreeFam; TF331897; -.
DR BioGRID-ORCS; 60440; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Iigp1; mouse.
DR EvolutionaryTrace; Q9QZ85; -.
DR PRO; PR:Q9QZ85; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9QZ85; protein.
DR Bgee; ENSMUSG00000054072; Expressed in heart right ventricle and 194 other tissues.
DR ExpressionAtlas; Q9QZ85; baseline and differential.
DR Genevisible; Q9QZ85; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0042832; P:defense response to protozoan; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030385; G_IRG_dom.
DR InterPro; IPR007743; Immunity-related_GTPase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF05049; IIGP; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51716; G_IRG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW GTP-binding; Hydrolase; Immunity; Innate immunity; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..413
FT /note="Interferon-inducible GTPase 1"
FT /id="PRO_0000223527"
FT DOMAIN 68..250
FT /note="IRG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01053"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12732635"
FT BINDING 102..106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12732635"
FT BINDING 184..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12732635"
FT BINDING 231..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12732635"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305"
FT MUTAGEN 2
FT /note="G->A: Protein is detected exclusively in the aqueous
FT phase."
FT /evidence="ECO:0000269|PubMed:15294976"
FT MUTAGEN 82
FT /note="K->A: Constitutively active. Binds GTP but fails to
FT hydrolyze it. Does not localize to the parasitophorous
FT vacuole membrane following T.gondii infection."
FT /evidence="ECO:0000269|PubMed:16304607,
FT ECO:0000269|PubMed:18772884"
FT MUTAGEN 83
FT /note="S->N: Abrogates interaction with HOOK3. Greatly
FT reduces binding affinity for GDP and GTP. Abolishes GTP-
FT dependent oligomer formation."
FT /evidence="ECO:0000269|PubMed:15075236,
FT ECO:0000269|PubMed:18772884"
FT CONFLICT 138
FT /note="N -> D (in Ref. 2; AAF07195)"
FT /evidence="ECO:0000305"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1TQ4"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1TPZ"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:4LV5"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 202..219
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5FPH"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4LV5"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:1TQD"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1TQ2"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 268..288
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 303..319
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:1TQ2"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:4LV5"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4LV5"
FT HELIX 386..409
FT /evidence="ECO:0007829|PDB:4LV5"
SQ SEQUENCE 413 AA; 47572 MW; 44B5A95FCA58A37A CRC64;
MGQLFSSPKS DENNDLPSSF TGYFKKFNTG RKIISQEILN LIELRMRKGN IQLTNSAISD
ALKEIDSSVL NVAVTGETGS GKSSFINTLR GIGNEEEGAA KTGVVEVTME RHPYKHPNIP
NVVFWDLPGI GSTNFPPNTY LEKMKFYEYD FFIIISATRF KKNDIDIAKA ISMMKKEFYF
VRTKVDSDIT NEADGKPQTF DKEKVLQDIR LNCVNTFREN GIAEPPIFLL SNKNVCHYDF
PVLMDKLISD LPIYKRHNFM VSLPNITDSV IEKKRQFLKQ RIWLEGFAAD LVNIIPSLTF
LLDSDLETLK KSMKFYRTVF GVDETSLQRL ARDWEIEVDQ VEAMIKSPAV FKPTDEETIQ
ERLSRYIQEF CLANGYLLPK NSFLKEIFYL KYYFLDMVTE DAKTLLKEIC LRN
