RAC3_HUMAN
ID RAC3_HUMAN Reviewed; 192 AA.
AC P60763; O14658; Q5U0M8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Ras-related C3 botulinum toxin substrate 3 {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000269|PubMed:16982419};
DE AltName: Full=p21-Rac3;
DE Flags: Precursor;
GN Name=RAC3 {ECO:0000312|HGNC:HGNC:9803};
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].
RX PubMed=9252344; DOI=10.1074/jbc.272.33.20384;
RA Haataja L., Groffen J., Heisterkamp N.;
RT "Characterization of RAC3, a novel member of the Rho family.";
RL J. Biol. Chem. 272:20384-20388(1997).
RN [2]
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 (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP INTERACTION WITH C1D.
RX PubMed=9852280; DOI=10.3892/ijmm.1.4.665;
RA Haataja L., Groffen J., Heisterkamp N.;
RT "Identification of a novel Rac3-interacting protein C1D.";
RL Int. J. Mol. Med. 1:665-670(1998).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NRBP.
RX PubMed=11956649;
RA De Langhe S., Haataja L., Senadheera D., Groffen J., Heisterkamp N.;
RT "Interaction of the small GTPase Rac3 with NRBP, a protein with a kinase-
RT homology domain.";
RL Int. J. Mol. Med. 9:451-459(2002).
RN [7]
RP FUNCTION, INTERACTION WITH CIB1, AND SUBCELLULAR LOCATION.
RX PubMed=11756406; DOI=10.1074/jbc.m105363200;
RA Haataja L., Kaartinen V., Groffen J., Heisterkamp N.;
RT "The small GTPase Rac3 interacts with the integrin-binding protein CIB and
RT promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading.";
RL J. Biol. Chem. 277:8321-8328(2002).
RN [8]
RP INTERACTION WITH DOCK7, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=16982419; DOI=10.1016/j.neuron.2006.07.020;
RA Watabe-Uchida M., John K.A., Janas J.A., Newey S.E., Van Aelst L.;
RT "The Rac activator DOCK7 regulates neuronal polarity through local
RT phosphorylation of stathmin/Op18.";
RL Neuron 51:727-739(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP GLYCOSYLATION AT TYR-32 (MICROBIAL INFECTION).
RX PubMed=24141704; DOI=10.1038/nsmb.2688;
RA Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
RA Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
RA Aktories K.;
RT "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation
RT of Gq and Gi proteins.";
RL Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN [11]
RP INVOLVEMENT IN NEDBAF, AND VARIANT NEDBAF GLY-59.
RX PubMed=29276006; DOI=10.1016/j.ajhg.2017.10.002;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA White J.J., Mazzeu J.F., Coban-Akdemir Z., Bayram Y., Bahrambeigi V.,
RA Hoischen A., van Bon B.W.M., Gezdirici A., Gulec E.Y., Ramond F.,
RA Touraine R., Thevenon J., Shinawi M., Beaver E., Heeley J., Hoover-Fong J.,
RA Durmaz C.D., Karabulut H.G., Marzioglu-Ozdemir E., Cayir A., Duz M.B.,
RA Seven M., Price S., Ferreira B.M., Vianna-Morgante A.M., Ellard S.,
RA Parrish A., Stals K., Flores-Daboub J., Jhangiani S.N., Gibbs R.A.,
RA Brunner H.G., Sutton V.R., Lupski J.R., Carvalho C.M.B.;
RT "WNT signaling perturbations underlie the genetic heterogeneity of Robinow
RT syndrome.";
RL Am. J. Hum. Genet. 102:27-43(2018).
RN [12]
RP VARIANTS NEDBAF LEU-29; LEU-61 AND LYS-62.
RX PubMed=30293988; DOI=10.1038/s41436-018-0323-y;
RA Costain G., Callewaert B., Gabriel H., Tan T.Y., Walker S.,
RA Christodoulou J., Lazar T., Menten B., Orkin J., Sadedin S., Snell M.,
RA Vanlander A., Vergult S., White S.M., Scherer S.W., Hayeems R.Z.,
RA Blaser S., Wodak S.J., Chitayat D., Marshall C.R., Meyn M.S.;
RT "De novo missense variants in RAC3 cause a novel neurodevelopmental
RT syndrome.";
RL Genet. Med. 21:1021-1026(2019).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC an active GTP-bound and inactive GDP-bound state. In active state binds
CC to a variety of effector proteins to regulate cellular responses, such
CC as cell spreading and the formation of actin-based protusions including
CC lamellipodia and membrane ruffles. Promotes cell adhesion and spreading
CC on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner.
CC {ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11956649}.
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; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:16982419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. Regulated by the GEF protein DOCK7.
CC {ECO:0000269|PubMed:16982419}.
CC -!- SUBUNIT: Interacts with the GEF protein DOCK7, which promotes the
CC exchange between GDP and GTP, and therefore activates it
CC (PubMed:16982419). Interacts with C1D (PubMed:9852280). Interacts (via
CC C-terminal region) with CIB1; the interaction induces their association
CC with the cytoskeleton upon alpha-IIb/beta3 integrin-mediated adhesion
CC (PubMed:11756406). Interacts with NRBP (PubMed:11956649).
CC {ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11956649,
CC ECO:0000269|PubMed:16982419, ECO:0000269|PubMed:9852280}.
CC -!- INTERACTION:
CC P60763; P53365: ARFIP2; NbExp=3; IntAct=EBI-767084, EBI-638194;
CC P60763; P03372: ESR1; NbExp=5; IntAct=EBI-767084, EBI-78473;
CC P60763; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-767084, EBI-12094670;
CC P60763; Q9UHY1: NRBP1; NbExp=3; IntAct=EBI-767084, EBI-749731;
CC P60763; Q9BYG5: PARD6B; NbExp=3; IntAct=EBI-767084, EBI-295391;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endomembrane system. Cell projection,
CC lamellipodium. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm,
CC cytoskeleton. Note=Membrane-associated when activated. Colocalizes with
CC NRBP to endomembranes and at the cell periphery in lamellipodia.
CC Colocalized with CIB1 in the perinuclear area and at the cell
CC periphery.
CC -!- TISSUE SPECIFICITY: Highest levels in brain, also detected in heart,
CC placenta and pancreas.
CC -!- INDUCTION: Expression down-regulated in quiescent fibroblasts and
CC clearly induced by serum stimulation.
CC -!- PTM: (Microbial infection) Glycosylated at Tyr-32 by Photorhabdus
CC asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits
CC downstream signaling by an impaired interaction with diverse regulator
CC and effector proteins of Rac and leads to actin disassembly.
CC {ECO:0000269|PubMed:24141704}.
CC -!- DISEASE: Neurodevelopmental disorder with structural brain anomalies
CC and dysmorphic facies (NEDBAF) [MIM:618577]: An autosomal dominant
CC neurodevelopmental disorder characterized by global developmental
CC delay, severe intellectual disability, poor language, seizures,
CC dysmorphic features, and thin corpus callosum.
CC {ECO:0000269|PubMed:29276006, ECO:0000269|PubMed:30293988}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RAC3ID42022ch17q25.html";
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DR EMBL; AF008591; AAC51667.1; -; mRNA.
DR EMBL; AF498966; AAM21113.1; -; mRNA.
DR EMBL; BT019443; AAV38250.1; -; mRNA.
DR EMBL; BC009605; AAH09605.1; -; mRNA.
DR EMBL; BC015197; AAH15197.1; -; mRNA.
DR CCDS; CCDS11798.1; -.
DR RefSeq; NP_005043.1; NM_005052.2.
DR PDB; 2C2H; X-ray; 1.85 A; A/B=1-192.
DR PDB; 2G0N; X-ray; 1.90 A; A/B=1-177.
DR PDB; 2IC5; X-ray; 1.90 A; A/B=1-178.
DR PDB; 2OV2; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-177.
DR PDB; 2QME; X-ray; 1.75 A; A=1-177.
DR PDB; 6TM1; X-ray; 3.71 A; A=1-192.
DR PDBsum; 2C2H; -.
DR PDBsum; 2G0N; -.
DR PDBsum; 2IC5; -.
DR PDBsum; 2OV2; -.
DR PDBsum; 2QME; -.
DR PDBsum; 6TM1; -.
DR AlphaFoldDB; P60763; -.
DR SMR; P60763; -.
DR BioGRID; 111819; 607.
DR ComplexPortal; CPX-6135; Phagocyte NADPH oxidase complex, RAC3 variant.
DR DIP; DIP-33881N; -.
DR IntAct; P60763; 31.
DR MINT; P60763; -.
DR STRING; 9606.ENSP00000304283; -.
DR ChEMBL; CHEMBL6087; -.
DR GlyGen; P60763; 1 site.
DR iPTMnet; P60763; -.
DR PhosphoSitePlus; P60763; -.
DR SwissPalm; P60763; -.
DR BioMuta; RAC3; -.
DR DMDM; 46397673; -.
DR EPD; P60763; -.
DR jPOST; P60763; -.
DR MassIVE; P60763; -.
DR MaxQB; P60763; -.
DR PaxDb; P60763; -.
DR PeptideAtlas; P60763; -.
DR PRIDE; P60763; -.
DR ProteomicsDB; 57225; -.
DR TopDownProteomics; P60763; -.
DR Antibodypedia; 32958; 94 antibodies from 24 providers.
DR DNASU; 5881; -.
DR Ensembl; ENST00000306897.9; ENSP00000304283.4; ENSG00000169750.9.
DR GeneID; 5881; -.
DR KEGG; hsa:5881; -.
DR MANE-Select; ENST00000306897.9; ENSP00000304283.4; NM_005052.3; NP_005043.1.
DR UCSC; uc002kdf.4; human.
DR CTD; 5881; -.
DR DisGeNET; 5881; -.
DR GeneCards; RAC3; -.
DR HGNC; HGNC:9803; RAC3.
DR HPA; ENSG00000169750; Low tissue specificity.
DR MalaCards; RAC3; -.
DR MIM; 602050; gene.
DR MIM; 618577; phenotype.
DR neXtProt; NX_P60763; -.
DR OpenTargets; ENSG00000169750; -.
DR PharmGKB; PA34164; -.
DR VEuPathDB; HostDB:ENSG00000169750; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153500; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P60763; -.
DR OMA; DRRMQPI; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P60763; -.
DR TreeFam; TF101109; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P60763; -.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; P60763; -.
DR SIGNOR; P60763; -.
DR BioGRID-ORCS; 5881; 129 hits in 1081 CRISPR screens.
DR EvolutionaryTrace; P60763; -.
DR GeneWiki; RAC3; -.
DR GenomeRNAi; 5881; -.
DR Pharos; P60763; Tbio.
DR PRO; PR:P60763; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P60763; protein.
DR Bgee; ENSG00000169750; Expressed in cortical plate and 100 other tissues.
DR ExpressionAtlas; P60763; baseline and differential.
DR Genevisible; P60763; HS.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IDA:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0043020; C:NADPH oxidase complex; IC:ComplexPortal.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IDA:UniProtKB.
DR GO; GO:0021894; P:cerebral cortex GABAergic interneuron development; IEA:Ensembl.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:UniProtKB.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0014041; P:regulation of neuron maturation; IEA:Ensembl.
DR GO; GO:0045730; P:respiratory burst; IC:ComplexPortal.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Disease variant; Glycoprotein; GTP-binding; Hydrolase;
KW Intellectual disability; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..189
FT /note="Ras-related C3 botulinum toxin substrate 3"
FT /id="PRO_0000198889"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281240"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="O-linked (GlcNAc) tyrosine; by Photorhabdus
FT PAU_02230"
FT /evidence="ECO:0000269|PubMed:24141704"
FT VARIANT 29
FT /note="P -> L (in NEDBAF; dbSNP:rs1568018697)"
FT /evidence="ECO:0000269|PubMed:30293988"
FT /id="VAR_083040"
FT VARIANT 59
FT /note="A -> G (in NEDBAF; dbSNP:rs1379395211)"
FT /evidence="ECO:0000269|PubMed:29276006"
FT /id="VAR_083245"
FT VARIANT 61
FT /note="Q -> L (in NEDBAF; dbSNP:rs1568018920)"
FT /evidence="ECO:0000269|PubMed:30293988"
FT /id="VAR_083041"
FT VARIANT 62
FT /note="E -> K (in NEDBAF; dbSNP:rs1064797229)"
FT /evidence="ECO:0000269|PubMed:30293988"
FT /id="VAR_083042"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:2QME"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:2QME"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2QME"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2QME"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:2QME"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:2C2H"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:2QME"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:2QME"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2QME"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2QME"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:2QME"
SQ SEQUENCE 192 AA; 21379 MW; 560BBC26BB7CDF4A CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPHTPI LLVGTKLDLR
DDKDTIERLR DKKLAPITYP QGLAMAREIG SVKYLECSAL TQRGLKTVFD EAIRAVLCPP
PVKKPGKKCT VF
