GNAT1_HUMAN
ID GNAT1_HUMAN Reviewed; 350 AA.
AC P11488; Q4VBN2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-1;
DE AltName: Full=Transducin alpha-1 chain;
GN Name=GNAT1; Synonyms=GNATR;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1614872; DOI=10.1093/nar/20.11.2865;
RA Fong S.-L.;
RT "Characterization of the human rod transducin alpha-subunit gene.";
RL Nucleic Acids Res. 20:2865-2870(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=2534964; DOI=10.1016/0896-6273(89)90261-4;
RA Lerea C.L., Bunt-Milam A.H., Hurley J.B.;
RT "Alpha transducin is present in blue-, green-, and red-sensitive cone
RT photoreceptors in the human retina.";
RL Neuron 3:367-376(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Eye;
RX PubMed=2748346; DOI=10.1093/nar/17.12.4887;
RA van Dop C., Medynski D.C., Apone L.M.;
RT "Nucleotide sequence for a cDNA encoding the alpha subunit of retinal
RT transducin (GNAT1) isolated from the human eye.";
RL Nucleic Acids Res. 17:4887-4887(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PHOSPHORYLATION AT TYR-142.
RX PubMed=11032890; DOI=10.1046/j.1471-4159.2000.0752006.x;
RA Bell M.W., Desai N., Guo X.X., Ghalayini A.J.;
RT "Tyrosine phosphorylation of the alpha subunit of transducin and its
RT association with Src in photoreceptor rod outer segments.";
RL J. Neurochem. 75:2006-2019(2000).
RN [8]
RP INVOLVEMENT IN CSNBAD3, AND VARIANT CSNBAD3 GLU-200.
RX PubMed=17584859; DOI=10.1002/humu.9499;
RA Szabo V., Kreienkamp H.J., Rosenberg T., Gal A.;
RT "p.Gln200Glu, a putative constitutively active mutant of rod alpha-
RT transducin (GNAT1) in autosomal dominant congenital stationary night
RT blindness.";
RL Hum. Mutat. 28:741-742(2007).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INVOLVEMENT IN CSNB1G,
RP AND VARIANT CSNB1G GLY-129.
RX PubMed=22190596; DOI=10.1167/iovs.11-8026;
RA Naeem M.A., Chavali V.R., Ali S., Iqbal M., Riazuddin S., Khan S.N.,
RA Husnain T., Sieving P.A., Ayyagari R., Riazuddin S., Hejtmancik J.F.,
RA Riazuddin S.A.;
RT "GNAT1 associated with autosomal recessive congenital stationary night
RT blindness.";
RL Invest. Ophthalmol. Vis. Sci. 53:1353-1361(2012).
RN [10]
RP VARIANT CSNBAD3 ASP-38.
RX PubMed=8673138; DOI=10.1038/ng0796-358;
RA Dryja T.P., Hahn L.B., Reboul T., Arnaud B.;
RT "Missense mutation in the gene encoding the alpha subunit of rod transducin
RT in the Nougaret form of congenital stationary night blindness.";
RL Nat. Genet. 13:358-360(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-11 IN COMPLEX WITH UNC119,
RP MYRISTOYLATION AT GLY-2, INTERACTION WITH UNC119, AND MUTAGENESIS OF GLY-2.
RX PubMed=21642972; DOI=10.1038/nn.2835;
RA Zhang H., Constantine R., Vorobiev S., Chen Y., Seetharaman J., Huang Y.J.,
RA Xiao R., Montelione G.T., Gerstner C.D., Davis M.W., Inana G., Whitby F.G.,
RA Jorgensen E.M., Hill C.P., Tong L., Baehr W.;
RT "UNC119 is required for G protein trafficking in sensory neurons.";
RL Nat. Neurosci. 14:874-880(2011).
CC -!- FUNCTION: Functions as signal transducer for the rod photoreceptor RHO.
CC Required for normal RHO-mediated light perception by the retina
CC (PubMed:22190596). Guanine nucleotide-binding proteins (G proteins)
CC function as transducers downstream of G protein-coupled receptors
CC (GPCRs), such as the photoreceptor RHO. The alpha chain contains the
CC guanine nucleotide binding site and alternates between an active, GTP-
CC bound state and an inactive, GDP-bound state. Activated RHO promotes
CC GDP release and GTP binding. Signaling is mediated via downstream
CC effector proteins, such as cGMP-phosphodiesterase (By similarity).
CC {ECO:0000250|UniProtKB:P04695, ECO:0000269|PubMed:22190596}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 subunits alpha,
CC beta and gamma. The alpha chain contains the guanine nucleotide binding
CC site. Interacts with RHO. Interacts with RGS9 and PDE6G (By
CC similarity). Interacts (when myristoylated) with UNC119; interaction is
CC required for localization in sensory neurons (PubMed:21642972).
CC {ECO:0000250|UniProtKB:P04695, ECO:0000269|PubMed:21642972}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000250|UniProtKB:P04695}. Membrane
CC {ECO:0000250|UniProtKB:P04695}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P04695}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P20612}. Note=Localizes mainly in the outer
CC segment in the dark-adapted state, whereas is translocated to the inner
CC part of the photoreceptors in the light-adapted state. During dark-
CC adapted conditions, in the presence of UNC119 mislocalizes from the
CC outer segment to the inner part of rod photoreceptors which leads to
CC decreased photoreceptor damage caused by light.
CC {ECO:0000250|UniProtKB:P20612}.
CC -!- TISSUE SPECIFICITY: Rod photoreceptor cells (PubMed:1614872).
CC Predominantly expressed in the retina followed by the ciliary body,
CC iris and retinal pigment epithelium (PubMed:22190596).
CC {ECO:0000269|PubMed:1614872, ECO:0000269|PubMed:22190596}.
CC -!- DEVELOPMENTAL STAGE: First detected at low levels at approximately
CC postnatal day 7. Subsequently, expression increases rapidly during the
CC first month after birth. {ECO:0000269|PubMed:22190596}.
CC -!- DISEASE: Night blindness, congenital stationary, autosomal dominant 3
CC (CSNBAD3) [MIM:610444]: A non-progressive retinal disorder
CC characterized by impaired night vision, often associated with nystagmus
CC and myopia. {ECO:0000269|PubMed:17584859, ECO:0000269|PubMed:8673138}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Night blindness, congenital stationary, 1G (CSNB1G)
CC [MIM:616389]: An autosomal recessive form of congenital stationary
CC night blindness, a non-progressive retinal disorder characterized by
CC impaired night vision or in dim light, with good vision only on bright
CC days. {ECO:0000269|PubMed:22190596}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Mutations of the GNAT1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/gntmut.htm";
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DR EMBL; X63749; CAB37839.2; -; Genomic_DNA.
DR EMBL; X15088; CAA33196.1; -; mRNA.
DR EMBL; AF493908; AAM12622.1; -; mRNA.
DR EMBL; AC002077; AAB54048.1; -; Genomic_DNA.
DR EMBL; BC095505; AAH95505.1; -; mRNA.
DR CCDS; CCDS2812.1; -.
DR PIR; S22953; RGHUT1.
DR RefSeq; NP_000163.2; NM_000172.3.
DR RefSeq; NP_653082.1; NM_144499.2.
DR PDB; 3RBQ; X-ray; 2.00 A; G/H/I/J/K/L=2-11.
DR PDBsum; 3RBQ; -.
DR AlphaFoldDB; P11488; -.
DR SMR; P11488; -.
DR BioGRID; 109041; 22.
DR IntAct; P11488; 8.
DR MINT; P11488; -.
DR STRING; 9606.ENSP00000232461; -.
DR DrugBank; DB02994; Cacodylic acid.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB04444; Tetrafluoroaluminate Ion.
DR iPTMnet; P11488; -.
DR PhosphoSitePlus; P11488; -.
DR SwissPalm; P11488; -.
DR BioMuta; GNAT1; -.
DR DMDM; 121032; -.
DR EPD; P11488; -.
DR jPOST; P11488; -.
DR MassIVE; P11488; -.
DR MaxQB; P11488; -.
DR PaxDb; P11488; -.
DR PeptideAtlas; P11488; -.
DR PRIDE; P11488; -.
DR ProteomicsDB; 52784; -.
DR Antibodypedia; 13896; 199 antibodies from 26 providers.
DR DNASU; 2779; -.
DR Ensembl; ENST00000232461.8; ENSP00000232461.3; ENSG00000114349.10.
DR Ensembl; ENST00000433068.5; ENSP00000387555.1; ENSG00000114349.10.
DR GeneID; 2779; -.
DR KEGG; hsa:2779; -.
DR MANE-Select; ENST00000232461.8; ENSP00000232461.3; NM_144499.3; NP_653082.1.
DR UCSC; uc003cyl.3; human.
DR CTD; 2779; -.
DR DisGeNET; 2779; -.
DR GeneCards; GNAT1; -.
DR HGNC; HGNC:4393; GNAT1.
DR HPA; ENSG00000114349; Tissue enriched (retina).
DR MalaCards; GNAT1; -.
DR MIM; 139330; gene.
DR MIM; 610444; phenotype.
DR MIM; 616389; phenotype.
DR neXtProt; NX_P11488; -.
DR OpenTargets; ENSG00000114349; -.
DR Orphanet; 215; Congenital stationary night blindness.
DR PharmGKB; PA28773; -.
DR VEuPathDB; HostDB:ENSG00000114349; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000160395; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P11488; -.
DR OMA; EFIVIIY; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P11488; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; P11488; -.
DR Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P11488; -.
DR SIGNOR; P11488; -.
DR BioGRID-ORCS; 2779; 34 hits in 1066 CRISPR screens.
DR GeneWiki; GNAT1; -.
DR GenomeRNAi; 2779; -.
DR Pharos; P11488; Tbio.
DR PRO; PR:P11488; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P11488; protein.
DR Bgee; ENSG00000114349; Expressed in neuron projection bundle connecting eye with brain and 91 other tissues.
DR ExpressionAtlas; P11488; baseline and differential.
DR Genevisible; P11488; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0000035; F:acyl binding; ISS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IEA:Ensembl.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
DR GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB.
DR GO; GO:0007603; P:phototransduction, visible light; IMP:UniProtKB.
DR GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0009642; P:response to light intensity; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; ISS:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0050917; P:sensory perception of umami taste; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:UniProtKB.
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; ADP-ribosylation; Cell projection;
KW Congenital stationary night blindness; Disease variant; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sensory transduction; Transducer; Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..350
FT /note="Guanine nucleotide-binding protein G(t) subunit
FT alpha-1"
FT /id="PRO_0000203737"
FT DOMAIN 28..350
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..44
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 169..177
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 192..201
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 261..268
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 320..325
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 340..350
FT /note="Interaction with RHO"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 171..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 265..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT BINDING 322
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04695"
FT MOD_RES 142
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:11032890"
FT MOD_RES 174
FT /note="ADP-ribosylarginine; by cholera toxin"
FT /evidence="ECO:0000250"
FT MOD_RES 347
FT /note="ADP-ribosylcysteine; by pertussis toxin"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:21642972"
FT VARIANT 38
FT /note="G -> D (in CSNBAD3; dbSNP:rs104893740)"
FT /evidence="ECO:0000269|PubMed:8673138"
FT /id="VAR_009279"
FT VARIANT 129
FT /note="D -> G (in CSNB1G; dbSNP:rs786205854)"
FT /evidence="ECO:0000269|PubMed:22190596"
FT /id="VAR_073798"
FT VARIANT 200
FT /note="Q -> E (in CSNBAD3; dbSNP:rs786205853)"
FT /evidence="ECO:0000269|PubMed:17584859"
FT /id="VAR_073799"
FT MUTAGEN 2
FT /note="G->A: Abolishes myristoylation, interaction with
FT UNC119 and localization."
FT /evidence="ECO:0000269|PubMed:21642972"
FT CONFLICT 204
FT /note="R -> P (in Ref. 3; CAA33196)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="S -> T (in Ref. 3; CAA33196)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="I -> V (in Ref. 3; CAA33196)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="V -> C (in Ref. 3; CAA33196)"
FT /evidence="ECO:0000305"
FT TURN 3..7
FT /evidence="ECO:0007829|PDB:3RBQ"
SQ SEQUENCE 350 AA; 40041 MW; D901013CFF5B0C7F CRC64;
MGAGASAEEK HSRELEKKLK EDAEKDARTV KLLLLGAGES GKSTIVKQMK IIHQDGYSLE
ECLEFIAIIY GNTLQSILAI VRAMTTLNIQ YGDSARQDDA RKLMHMADTI EEGTMPKEMS
DIIQRLWKDS GIQACFERAS EYQLNDSAGY YLSDLERLVT PGYVPTEQDV LRSRVKTTGI
IETQFSFKDL NFRMFDVGGQ RSERKKWIHC FEGVTCIIFI AALSAYDMVL VEDDEVNRMH
ESLHLFNSIC NHRYFATTSI VLFLNKKDVF FEKIKKAHLS ICFPDYDGPN TYEDAGNYIK
VQFLELNMRR DVKEIYSHMT CATDTQNVKF VFDAVTDIII KENLKDCGLF
