ID ARF1_YEAST Reviewed; 181 AA. AC P11076; D6VRG1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 226. DE RecName: Full=ADP-ribosylation factor 1; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P84077}; GN Name=ARF1; OrderedLocusNames=YDL192W; ORFNames=D1244; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3133654; DOI=10.1073/pnas.85.13.4620; RA Sewell J., Kahn R.A.; RT "Sequences of the bovine and yeast ADP-ribosylation factor and comparison RT to other GTP-binding proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4620-4624(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8896272; RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1065::aid-yea995%3e3.0.co;2-f; RA Verhasselt P., Voet M., Mathys J., Volckaert G.; RT "The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast RT chromosome IV reveals the location of five known genes and characterizes at RT least six new open reading frames including putative genes for ribosomal RT protein L35 and a sugar transport protein."; RL Yeast 12:1065-1070(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; DOI=10.1038/387s075; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP DISRUPTION PHENOTYPE. RX PubMed=10601336; DOI=10.1083/jcb.147.6.1223; RA Chen C.Y., Ingram M.F., Rosal P.H., Graham T.R.; RT "Role for Drs2p, a P-type ATPase and potential aminophospholipid RT translocase, in yeast late Golgi function."; RL J. Cell Biol. 147:1223-1236(1999). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP INTERACTION WITH RUD3, AND SUBCELLULAR LOCATION. RX PubMed=15504911; DOI=10.1083/jcb.200407088; RA Gillingham A.K., Tong A.H.Y., Boone C., Munro S.; RT "The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to RT recruit the golgin Rud3p to the cis-Golgi."; RL J. Cell Biol. 167:281-292(2004). RN [8] RP FUNCTION IN MRNA TRANSPORT, AND INTERACTION WITH ARF1. RX PubMed=15356266; DOI=10.1091/mbc.e04-05-0411; RA Trautwein M., Dengjel J., Schirle M., Spang A.; RT "Arf1p provides an unexpected link between COPI vesicles and mRNA in RT Saccharomyces cerevisiae."; RL Mol. Biol. Cell 15:5021-5037(2004). RN [9] RP DISRUPTION PHENOTYPE. RX PubMed=16956384; DOI=10.1111/j.1600-0854.2006.00485.x; RA Chen S., Wang J., Muthusamy B.P., Liu K., Zare S., Andersen R.J., RA Graham T.R.; RT "Roles for the Drs2p-Cdc50p complex in protein transport and RT phosphatidylserine asymmetry of the yeast plasma membrane."; RL Traffic 7:1503-1517(2006). RN [10] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-127, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [11] RP FUNCTION, AND INTERACTION WITH VPS13. RX PubMed=34830155; DOI=10.3390/ijms222212274; RA Kolakowski D., Rzepnikowska W., Kaniak-Golik A., Zoladek T., Kaminska J.; RT "The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi RT Apparatus."; RL Int. J. Mol. Sci. 22:12274-12274(2021). RN [12] {ECO:0007744|PDB:2K5U} RP STRUCTURE BY NMR OF 2-181 IN COMPLEX WITH GDP, AND MYRISTOYLATION AT GLY-2. RX PubMed=19141284; DOI=10.1016/j.str.2008.10.020; RA Liu Y., Kahn R.A., Prestegard J.H.; RT "Structure and membrane interaction of myristoylated ARF1."; RL Structure 17:79-87(2009). RN [13] {ECO:0007744|PDB:2KSQ} RP STRUCTURE BY NMR OF 2-181 IN COMPLEX WITH GTP, AND MYRISTOYLATION AT GLY-2. RX PubMed=20601958; DOI=10.1038/nsmb.1853; RA Liu Y., Kahn R.A., Prestegard J.H.; RT "Dynamic structure of membrane-anchored Arf*GTP."; RL Nat. Struct. Mol. Biol. 17:876-881(2010). RN [14] {ECO:0007744|PDB:3TJZ} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 18-181. RX PubMed=22304919; DOI=10.1016/j.cell.2012.01.015; RA Yu X., Breitman M., Goldberg J.; RT "A structure-based mechanism for Arf1-dependent recruitment of coatomer to RT membranes."; RL Cell 148:530-542(2012). CC -!- FUNCTION: GTP-binding protein involved in Golgi vesicle trafficking CC (PubMed:15356266, PubMed:34830155). May modulate vesicle budding and CC uncoating within the Golgi apparatus (PubMed:15356266). May recruit the CC lipid transfer protein VPS13 to Golgi membranes (PubMed:34830155). CC Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this CC is required for correct localization of the asymmetrically distributed CC ASH1 mRNA (PubMed:15356266). {ECO:0000269|PubMed:15356266, CC ECO:0000269|PubMed:34830155}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); 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:0000250|UniProtKB:P84077}; CC -!- SUBUNIT: Interacts with RUD3 (PubMed:15356266, PubMed:15504911, CC PubMed:19141284, PubMed:20601958). Interacts with VPS13 (via C-terminal CC part); the interaction is direct (PubMed:34830155). CC {ECO:0000269|PubMed:15356266, ECO:0000269|PubMed:15504911, CC ECO:0000269|PubMed:19141284, ECO:0000269|PubMed:20601958, CC ECO:0000269|PubMed:34830155}. CC -!- INTERACTION: CC P11076; P19146: ARF2; NbExp=5; IntAct=EBI-2816, EBI-2820; CC P11076; Q05029: BCH1; NbExp=3; IntAct=EBI-2816, EBI-27508; CC P11076; P36122: BCH2; NbExp=2; IntAct=EBI-2816, EBI-26374; CC P11076; Q08754: BUD7; NbExp=2; IntAct=EBI-2816, EBI-32770; CC P11076; Q12114: CHS5; NbExp=5; IntAct=EBI-2816, EBI-4640; CC P11076; P40955: CHS6; NbExp=3; IntAct=EBI-2816, EBI-4649; CC P11076; P41909: PXA1; NbExp=2; IntAct=EBI-2816, EBI-14344; CC P11076; P34230: PXA2; NbExp=2; IntAct=EBI-2816, EBI-2464632; CC P11076; Q12234: RUD3; NbExp=5; IntAct=EBI-2816, EBI-31697; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15504911}. CC -!- DISRUPTION PHENOTYPE: Increases phosphatidylserine levels in the outer CC leaflet of the cell membrane (PubMed:16956384). Simultaneous knockout CC of DRS2 results in inviability (PubMed:10601336). CC {ECO:0000269|PubMed:10601336, ECO:0000269|PubMed:16956384}. CC -!- MISCELLANEOUS: Present with 19300 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J03276; AAA34431.1; -; Genomic_DNA. DR EMBL; X83276; CAA58255.1; -; Genomic_DNA. DR EMBL; Z74240; CAA98769.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11671.1; -; Genomic_DNA. DR PIR; B36167; B36167. DR RefSeq; NP_010089.1; NM_001180252.1. DR PDB; 2K5U; NMR; -; A=2-181. DR PDB; 2KSQ; NMR; -; A=2-181. DR PDB; 3TJZ; X-ray; 2.90 A; A/D=18-181. DR PDB; 4Q66; X-ray; 3.35 A; C/F/I/L=18-181. DR PDB; 5A1U; EM; 13.00 A; A/B=1-181. DR PDB; 5A1V; EM; 21.00 A; A/B/I/J/R/S=1-181. DR PDB; 5A1W; EM; 18.00 A; A/B=1-181. DR PDB; 5A1X; EM; 23.00 A; A/B/I/J=1-181. DR PDB; 5A1Y; EM; 21.00 A; A/B/I/J/R=1-181. DR PDB; 5NZR; EM; 9.20 A; F/M/R=1-181. DR PDB; 5NZS; EM; 10.10 A; F/M/R=1-181. DR PDB; 5NZT; EM; 17.00 A; F/J/M/R=1-181. DR PDB; 5NZU; EM; 15.00 A; F/M/R=1-181. DR PDB; 5NZV; EM; 17.30 A; F/M/P/R/T=1-181. DR PDB; 7URO; EM; 4.20 A; B/D=1-181. DR PDB; 8S5C; EM; 3.10 A; A=1-181. DR PDB; 8S5D; EM; 3.79 A; A=1-181. DR PDB; 8S5E; EM; 3.10 A; A/B/C/D/E/F/G=1-181. DR AlphaFoldDB; P11076; -. DR BMRB; P11076; -. DR EMDB; EMD-19731; -. DR EMDB; EMD-19732; -. DR EMDB; EMD-19733; -. DR EMDB; EMD-2985; -. DR EMDB; EMD-2986; -. DR EMDB; EMD-2987; -. DR EMDB; EMD-2988; -. DR EMDB; EMD-2989; -. DR EMDB; EMD-3720; -. DR EMDB; EMD-3721; -. DR EMDB; EMD-3722; -. DR EMDB; EMD-3723; -. DR EMDB; EMD-3724; -. DR SMR; P11076; -. DR BioGRID; 31853; 414. DR DIP; DIP-2213N; -. DR FunCoup; P11076; 1277. DR IntAct; P11076; 85. DR MINT; P11076; -. DR STRING; 4932.YDL192W; -. DR iPTMnet; P11076; -. DR PaxDb; 4932-YDL192W; -. DR PeptideAtlas; P11076; -. DR TopDownProteomics; P11076; -. DR EnsemblFungi; YDL192W_mRNA; YDL192W; YDL192W. DR GeneID; 851335; -. DR KEGG; sce:YDL192W; -. DR AGR; SGD:S000002351; -. DR SGD; S000002351; ARF1. DR VEuPathDB; FungiDB:YDL192W; -. DR eggNOG; KOG0070; Eukaryota. DR HOGENOM; CLU_040729_9_3_1; -. DR InParanoid; P11076; -. DR OMA; IRQRHWF; -. DR OrthoDB; 2011769at2759; -. DR BioCyc; YEAST:G3O-29577-MONOMER; -. DR Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane. DR Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane. DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding. DR Reactome; R-SCE-5620916; VxPx cargo-targeting to cilium. DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport. DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-SCE-6811438; Intra-Golgi traffic. DR BioGRID-ORCS; 851335; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P11076; -. DR PRO; PR:P11076; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P11076; protein. DR GO; GO:0005829; C:cytosol; HDA:SGD. DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD. DR GO; GO:0044232; C:organelle membrane contact site; IDA:SGD. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. 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:SGD. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:SGD. DR GO; GO:0006893; P:Golgi to plasma membrane transport; IGI:SGD. DR GO; GO:0048193; P:Golgi vesicle transport; IMP:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0016236; P:macroautophagy; IMP:SGD. DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IGI:SGD. DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IGI:SGD. DR GO; GO:1903292; P:protein localization to Golgi membrane; IDA:SGD. DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IGI:SGD. DR GO; GO:1903358; P:regulation of Golgi organization; IDA:SGD. DR CDD; cd04150; Arf1_5_like; 1. DR FunFam; 3.40.50.300:FF:000024; ADP-ribosylation factor 1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR045872; Arf1-5-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR024156; Small_GTPase_ARF. DR InterPro; IPR006689; Small_GTPase_ARF/SAR. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00178; SAR; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51417; ARF; 1. DR PDBsum; 2K5U; -. DR PDBsum; 2KSQ; -. DR PDBsum; 3TJZ; -. DR PDBsum; 4Q66; -. DR PDBsum; 5A1U; -. DR PDBsum; 5A1V; -. DR PDBsum; 5A1W; -. DR PDBsum; 5A1X; -. DR PDBsum; 5A1Y; -. DR PDBsum; 5NZR; -. DR PDBsum; 5NZS; -. DR PDBsum; 5NZT; -. DR PDBsum; 5NZU; -. DR PDBsum; 5NZV; -. DR PDBsum; 7URO; -. DR PDBsum; 8S5C; -. DR PDBsum; 8S5D; -. DR PDBsum; 8S5E; -. PE 1: Evidence at protein level; KW 3D-structure; ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; KW Isopeptide bond; Lipoprotein; Myristate; Nucleotide-binding; KW Protein transport; Reference proteome; Transport; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..181 FT /note="ADP-ribosylation factor 1" FT /id="PRO_0000207418" FT BINDING 25..32 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20601958" FT BINDING 48 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20601958" FT BINDING 70 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20601958" FT BINDING 126..129 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20601958" FT BINDING 160..161 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20601958" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:19141284, FT ECO:0000269|PubMed:20601958" FT CROSSLNK 127 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT STRAND 4..8 FT /evidence="ECO:0007829|PDB:2K5U" FT HELIX 11..13 FT /evidence="ECO:0007829|PDB:2KSQ" FT TURN 14..16 FT /evidence="ECO:0007829|PDB:2KSQ" FT STRAND 19..23 FT /evidence="ECO:0007829|PDB:3TJZ" FT TURN 26..28 FT /evidence="ECO:0007829|PDB:2KSQ" FT HELIX 30..39 FT /evidence="ECO:0007829|PDB:3TJZ" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:2K5U" FT STRAND 49..58 FT /evidence="ECO:0007829|PDB:3TJZ" FT STRAND 61..68 FT /evidence="ECO:0007829|PDB:3TJZ" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:3TJZ" FT TURN 76..78 FT /evidence="ECO:0007829|PDB:3TJZ" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:3TJZ" FT STRAND 86..93 FT /evidence="ECO:0007829|PDB:3TJZ" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:3TJZ" FT HELIX 100..110 FT /evidence="ECO:0007829|PDB:3TJZ" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:3TJZ" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:3TJZ" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:3TJZ" FT HELIX 136..143 FT /evidence="ECO:0007829|PDB:3TJZ" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:3TJZ" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:3TJZ" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:3TJZ" FT HELIX 166..174 FT /evidence="ECO:0007829|PDB:3TJZ" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:2KSQ" SQ SEQUENCE 181 AA; 20529 MW; 796859026AC63CC0 CRC64; MGLFASKLFS NLFGNKEMRI LMVGLDGAGK TTVLYKLKLG EVITTIPTIG FNVETVQYKN ISFTVWDVGG QDRIRSLWRH YYRNTEGVIF VVDSNDRSRI GEAREVMQRM LNEDELRNAA WLVFANKQDL PEAMSAAEIT EKLGLHSIRN RPWFIQATCA TSGEGLYEGL EWLSNSLKNS T //