GNAI3_RAT
ID GNAI3_RAT Reviewed; 354 AA.
AC P08753;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-3;
DE AltName: Full=G(i) alpha-3;
GN Name=Gnai3; Synonyms=Gnai-3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2834384; DOI=10.1016/s0021-9258(18)68692-2;
RA Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.;
RT "Presence of three distinct molecular species of Gi protein alpha subunit.
RT Structure of rat cDNAs and human genomic DNAs.";
RL J. Biol. Chem. 263:6656-6664(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2820999; DOI=10.1016/s0021-9258(18)47929-x;
RA Jones D.T., Reed R.R.;
RT "Molecular cloning of five GTP-binding protein cDNA species from rat
RT olfactory neuroepithelium.";
RL J. Biol. Chem. 262:14241-14249(1987).
RN [3]
RP PROTEIN SEQUENCE OF 111-125, FUNCTION, AND SUBUNIT.
RX PubMed=2159473; DOI=10.1016/s0021-9258(19)39064-7;
RA Linder M.E., Ewald D.A., Miller R.J., Gilman A.G.;
RT "Purification and characterization of Go alpha and three types of Gi alpha
RT after expression in Escherichia coli.";
RL J. Biol. Chem. 265:8243-8251(1990).
RN [4]
RP INTERACTION WITH GPSM1.
RX PubMed=11121039; DOI=10.1073/pnas.97.26.14364;
RA de Vries L., Fischer T., Tronchere H., Brothers G.M., Strockbine B.,
RA Siderovski D.P., Farquhar M.G.;
RT "Activator of G protein signaling 3 is a guanine dissociation inhibitor for
RT Galpha i subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14364-14369(2000).
RN [5]
RP INTERACTION WITH RGS12 AND RGS14.
RX PubMed=11387333; DOI=10.1074/jbc.m103208200;
RA Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A.,
RA Gist Farquhar M., Siderovski D.P.;
RT "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
RT guanine nucleotide dissociation inhibitor activity.";
RL J. Biol. Chem. 276:29275-29281(2001).
RN [6]
RP INTERACTION WITH RGS14.
RX PubMed=16870394; DOI=10.1016/j.cellsig.2006.06.002;
RA Shu F.J., Ramineni S., Amyot W., Hepler J.R.;
RT "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR
RT domain of RGS14 influence its dynamic subcellular localization.";
RL Cell. Signal. 19:163-176(2007).
RN [7]
RP INTERACTION WITH CCDC88A, AND MUTAGENESIS OF ARG-208; TRP-211 AND PHE-215.
RX PubMed=19211784; DOI=10.1073/pnas.0900294106;
RA Garcia-Marcos M., Ghosh P., Farquhar M.G.;
RT "GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates
RT Akt signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:3178-3183(2009).
RN [8]
RP IDENTIFICATION IN COMPLEX WITH CCDC88A AND EGFR, AND MUTAGENESIS OF GLY-203
RP AND GLN-204.
RX PubMed=20462955; DOI=10.1091/mbc.e10-01-0028;
RA Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P.,
RA Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.;
RT "A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor
RT and determines whether cells migrate or proliferate.";
RL Mol. Biol. Cell 21:2338-2354(2010).
RN [9]
RP INTERACTION WITH NUCB1 AND NUCB2, AND MUTAGENESIS OF TRP-211; PHE-215;
RP LYS-248 AND TRP-258.
RX PubMed=21653697; DOI=10.1074/jbc.m110.204099;
RA Garcia-Marcos M., Kietrsunthorn P.S., Wang H., Ghosh P., Farquhar M.G.;
RT "G Protein binding sites on Calnuc (nucleobindin 1) and NUCB2 (nucleobindin
RT 2) define a new class of G(alpha)i-regulatory motifs.";
RL J. Biol. Chem. 286:28138-28149(2011).
RN [10]
RP INTERACTION WITH INSR.
RX PubMed=25187647; DOI=10.1091/mbc.e14-05-0978;
RA Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M.,
RA Kufareva I., Abagyan R., Ghosh P.;
RT "Structural basis for activation of trimeric Gi proteins by multiple growth
RT factor receptors via GIV/Girdin.";
RL Mol. Biol. Cell 25:3654-3671(2014).
RN [11] {ECO:0007744|PDB:6MHF}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 26-354 IN COMPLEX WITH HUMAN
RP CCDC88A AND WITH SYNTHETIC G-ALPHA SUBUNIT-BINDING PEPTIDE, AND MUTAGENESIS
RP OF GLN-204; TRP-211 AND PHE-215.
RX PubMed=31363053; DOI=10.1073/pnas.1906658116;
RA Kalogriopoulos N.A., Rees S.D., Ngo T., Kopcho N.J., Ilatovskiy A.V.,
RA Sun N., Komives E.A., Chang G., Ghosh P., Kufareva I.;
RT "Structural basis for GPCR-independent activation of heterotrimeric Gi
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:16394-16403(2019).
RN [12]
RP ERRATUM OF PUBMED:31363053.
RX PubMed=31570568; DOI=10.1073/pnas.1916094116;
RA Kalogriopoulos N.A., Rees S.D., Ngo T., Kopcho N.J., Ilatovskiy A.V.,
RA Sun N., Komives E.A., Chang G., Ghosh P., Kufareva I.;
RL Proc. Natl. Acad. Sci. U.S.A. 116:20794-20794(2019).
CC -!- FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G
CC proteins) function as transducers downstream of G protein-coupled
CC receptors (GPCRs) in numerous signaling cascades. The alpha chain
CC contains the guanine nucleotide binding site and alternates between an
CC active, GTP-bound state and an inactive, GDP-bound state. Signaling by
CC an activated GPCR promotes GDP release and GTP binding. The alpha
CC subunit has a low GTPase activity that converts bound GTP to GDP,
CC thereby terminating the signal (PubMed:2159473). Both GDP release and
CC GTP hydrolysis are modulated by numerous regulatory proteins. Signaling
CC is mediated via effector proteins, such as adenylate cyclase. Inhibits
CC adenylate cyclase activity, leading to decreased intracellular cAMP
CC levels. Stimulates the activity of receptor-regulated K(+) channels.
CC The active GTP-bound form prevents the association of RGS14 with
CC centrosomes and is required for the translocation of RGS14 from the
CC cytoplasm to the plasma membrane. May play a role in cell division.
CC {ECO:0000250|UniProtKB:P08754, ECO:0000269|PubMed:2159473}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC and gamma. The alpha subunit contains the guanine nucleotide binding
CC site (PubMed:2159473). GTP binding causes dissociation of the
CC heterotrimer, liberating the individual subunits so that they can
CC interact with downstream effector proteins. Forms a complex with
CC CCDC88A/GIV and EGFR which leads to enhanced EGFR signaling and
CC triggering of cell migration; ligand stimulation is required for
CC recruitment of GNAI3 to the complex (PubMed:20462955). Interacts
CC (inactive GDP-bound form) with CCDC88A/GIV (via GBA motif); the
CC interaction leads to activation of GNAI3 (PubMed:19211784). Interacts
CC (inactive GDP-bound form) with CCDC88C/DAPLE (via GBA motif); the
CC interaction leads to activation of GNAI3 (By similarity). Interacts
CC (inactive GDP-bound form) with NUCB1 (via GBA motif) and NUCB2 (via GBA
CC motif); the interaction leads to activation of GNAI3 (PubMed:21653697).
CC Interacts (inactive GDP-bound form) with PLCD4 (via GBA motif); the
CC interaction leads to activation of GNAI3 (By similarity). Interacts
CC with INSR; the interaction is probably mediated by CCDC88A/GIV
CC (PubMed:25187647). Interacts with GPSM1 (PubMed:11121039). Interacts
CC (GDP-bound form) with GPSM2 (via GoLoco domains). Does not interact
CC with RGS2. Interacts with RGS8 and RGS10; this strongly enhances the
CC intrinsic GTPase activity (By similarity). Interacts with RGS12
CC (PubMed:11387333). Interacts with RGS16; this strongly enhances the
CC intrinsic GTPase activity (By similarity). Interacts (via active
CC GTP- or inactive GDP-bound form) with RGS14 (PubMed:11387333,
CC PubMed:16870394). {ECO:0000250|UniProtKB:P08754,
CC ECO:0000250|UniProtKB:Q9DC51, ECO:0000269|PubMed:11121039,
CC ECO:0000269|PubMed:11387333, ECO:0000269|PubMed:16870394,
CC ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:20462955,
CC ECO:0000269|PubMed:2159473, ECO:0000269|PubMed:21653697,
CC ECO:0000269|PubMed:25187647}.
CC -!- INTERACTION:
CC P08753; Q5BJU7: Wasf1; NbExp=2; IntAct=EBI-874897, EBI-7269229;
CC P08753; P49795: RGS19; Xeno; NbExp=4; IntAct=EBI-874897, EBI-874907;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell
CC membrane {ECO:0000250|UniProtKB:P08754}; Lipid-anchor {ECO:0000305}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P08754}. Note=Localizes in the centrosomes of
CC interphase and mitotic cells. Detected at the cleavage furrow and/or
CC the midbody. {ECO:0000250|UniProtKB:P08754}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:2820999}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; J03219; AAA41224.1; -; mRNA.
DR EMBL; M20713; AAA40823.1; -; mRNA.
DR PIR; E27423; RGRTI3.
DR RefSeq; NP_037238.1; NM_013106.1.
DR PDB; 6MHE; X-ray; 2.20 A; A=26-354.
DR PDB; 6MHF; X-ray; 2.00 A; A=26-354.
DR PDBsum; 6MHE; -.
DR PDBsum; 6MHF; -.
DR AlphaFoldDB; P08753; -.
DR BMRB; P08753; -.
DR SMR; P08753; -.
DR BioGRID; 247672; 2.
DR CORUM; P08753; -.
DR DIP; DIP-608N; -.
DR IntAct; P08753; 3.
DR MINT; P08753; -.
DR STRING; 10116.ENSRNOP00000026710; -.
DR iPTMnet; P08753; -.
DR PhosphoSitePlus; P08753; -.
DR SwissPalm; P08753; -.
DR jPOST; P08753; -.
DR PaxDb; P08753; -.
DR PRIDE; P08753; -.
DR GeneID; 25643; -.
DR KEGG; rno:25643; -.
DR UCSC; RGD:2714; rat.
DR CTD; 2773; -.
DR RGD; 2714; Gnai3.
DR VEuPathDB; HostDB:ENSRNOG00000019465; -.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P08753; -.
DR OMA; MRIIHDV; -.
DR OrthoDB; 754573at2759; -.
DR TreeFam; TF300673; -.
DR Reactome; R-RNO-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR SABIO-RK; P08753; -.
DR PRO; PR:P08753; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019465; Expressed in duodenum and 19 other tissues.
DR Genevisible; P08753; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; TAS:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042588; C:zymogen granule; IDA:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IPI:RGD.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:RGD.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:RGD.
DR GO; GO:0051048; P:negative regulation of secretion; TAS:UniProtKB.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IMP:RGD.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0006906; P:vesicle fusion; IDA:RGD.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; GTP-binding; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(i) subunit
FT alpha-3"
FT /id="PRO_0000203694"
FT DOMAIN 32..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 173..181
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 196..205
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 265..272
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 324..329
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 43..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 150..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 175..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 200..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 269..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT BINDING 326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P08754"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 203
FT /note="G->A: Reduces cell migration by 50% and increases
FT mitosis six-fold."
FT /evidence="ECO:0000269|PubMed:20462955"
FT MUTAGEN 204
FT /note="Q->L: No effect on promotion of cell migration or
FT GTP-binding activity. Increases sensitivity to activation
FT by CCDC88A."
FT /evidence="ECO:0000269|PubMed:20462955,
FT ECO:0000269|PubMed:31363053"
FT MUTAGEN 208
FT /note="R->A: Dramatically decreases binding to CCDC88A."
FT /evidence="ECO:0000269|PubMed:19211784"
FT MUTAGEN 211
FT /note="W->A: Abolishes binding to NUCB1. Dramatically
FT decreases binding to CCDC88A. Does not affect GTP-binding
FT activity but increases the basal exchange rate."
FT /evidence="ECO:0000269|PubMed:19211784,
FT ECO:0000269|PubMed:21653697, ECO:0000269|PubMed:31363053"
FT MUTAGEN 215
FT /note="F->A: Abolishes binding to NUCB1. Dramatically
FT decreases binding to CCDC88A. Does not affect GTP-binding
FT activity but increases the basal exchange rate."
FT /evidence="ECO:0000269|PubMed:19211784,
FT ECO:0000269|PubMed:21653697, ECO:0000269|PubMed:31363053"
FT MUTAGEN 248
FT /note="K->E: Abolishes binding to NUCB1."
FT /evidence="ECO:0000269|PubMed:21653697"
FT MUTAGEN 248
FT /note="K->M: Dramatically decreases interaction with
FT NUCB1."
FT /evidence="ECO:0000269|PubMed:21653697"
FT MUTAGEN 258
FT /note="W->F: No effect on interaction with NUCB1."
FT /evidence="ECO:0000269|PubMed:21653697"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 70..91
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:6MHF"
FT TURN 111..116
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:6MHF"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:6MHF"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:6MHF"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:6MHF"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:6MHF"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:6MHF"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:6MHF"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6MHE"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6MHF"
FT HELIX 329..345
FT /evidence="ECO:0007829|PDB:6MHF"
SQ SEQUENCE 354 AA; 40522 MW; A65D63CE5A32C777 CRC64;
MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV KQMKIIHEDG
YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEAAR ADDARQLFVL AGSAEEGVMT
SELAGVIKRL WRDGGVQACF SRSREYQLND SASYYLNDLD RISQTNYIPT QQDVLRTRVK
TTGIVETHFT FKELYFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA
AYIQCQFEDL NRRKDTKEVY THFTCATDTK NVQFVFDAVT DVIIKNNLKE CGLY
