ID SEC14_YEAST Reviewed; 304 AA. AC P24280; D6VZQ3; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 198. DE RecName: Full=SEC14 cytosolic factor; DE AltName: Full=Phosphatidylinositol/phosphatidylcholine transfer protein; DE Short=PI/PC TP; GN Name=SEC14; Synonyms=PIT1; OrderedLocusNames=YMR079W; GN ORFNames=YM9582.04; 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], FUNCTION, AND SUBCELLULAR LOCATION. RC STRAIN=CTY1-1A; RX PubMed=2466847; DOI=10.1083/jcb.108.4.1271; RA Bankaitis V.A., Malehorn D.E., Emr S.D., Greene R.; RT "The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is RT required for transport of secretory proteins from the yeast Golgi RT complex."; RL J. Cell Biol. 108:1271-1281(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [3] 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 [4] RP PROTEIN SEQUENCE OF 2-31. RX PubMed=2407740; DOI=10.1016/s0021-9258(19)39620-6; RA Aitken J.F., van Heusden G.P.H., Temkin M., Dowhan W.; RT "The gene encoding the phosphatidylinositol transfer protein is essential RT for cell growth."; RL J. Biol. Chem. 265:4711-4717(1990). RN [5] RP FUNCTION. RX PubMed=2215682; DOI=10.1038/347561a0; RA Bankaitis V.A., Aitken J.R., Cleves A.E., Dowhan W.; RT "An essential role for a phospholipid transfer protein in yeast Golgi RT function."; RL Nature 347:561-562(1990). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=1997207; DOI=10.1016/0092-8674(91)90508-v; RA Cleves A.E., McGee T.P., Whitters E.A., Champion K.M., Aitken J.R., RA Dowhan W., Goebl M., Bankaitis V.A.; RT "Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass RT the requirement for an essential phospholipid transfer protein."; RL Cell 64:789-800(1991). RN [7] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=7816798; DOI=10.1073/pnas.92.1.112; RA Skinner H.B., McGee T.P., McMaster C.R., Fry M.R., Bell R.M., RA Bankaitis V.A.; RT "The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects RT a ligand-dependent inhibition of choline-phosphate cytidylyltransferase RT activity."; RL Proc. Natl. Acad. Sci. U.S.A. 92:112-116(1995). RN [8] RP FUNCTION, AND MUTAGENESIS OF LYS-66 AND LYS-239. RX PubMed=10488334; DOI=10.1016/s1097-2765(00)80366-4; RA Phillips S.E., Sha B., Topalof L., Xie Z., Alb J.G., Klenchin V.A., RA Swigart P., Cockcroft S., Martin T.F., Luo M., Bankaitis V.A.; RT "Yeast Sec14p deficient in phosphatidylinositol transfer activity is RT functional in vivo."; RL Mol. Cell 4:187-197(1999). RN [9] RP CATALYTIC ACTIVITY. RX PubMed=10848624; DOI=10.1091/mbc.11.6.1989; RA Li X., Routt S.M., Xie Z., Cui X., Fang M., Kearns M.A., Bard M., RA Kirsch D.R., Bankaitis V.A.; RT "Identification of a novel family of nonclassic yeast phosphatidylinositol RT transfer proteins whose function modulates phospholipase D activity and RT Sec14p-independent cell growth."; RL Mol. Biol. Cell 11:1989-2005(2000). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=12869188; DOI=10.1046/j.1432-1033.2003.03688.x; RA Schnabl M., Oskolkova O.V., Holic R., Brezna B., Pichler H., Zagorsek M., RA Kohlwein S.D., Paltauf F., Daum G., Griac P.; RT "Subcellular localization of yeast Sec14 homologues and their involvement RT in regulation of phospholipid turnover."; RL Eur. J. Biochem. 270:3133-3145(2003). RN [11] 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 [12] RP FUNCTION. RX PubMed=16997918; DOI=10.1074/jbc.m603054200; RA Smirnova T.I., Chadwick T.G., MacArthur R., Poluektov O., Song L., RA Ryan M.M., Schaaf G., Bankaitis V.A.; RT "The chemistry of phospholipid binding by the Saccharomyces cerevisiae RT phosphatidylinositol transfer protein Sec14p as determined by EPR RT spectroscopy."; RL J. Biol. Chem. 281:34897-34908(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [14] RP FUNCTION. RX PubMed=19129178; DOI=10.1074/jbc.m808732200; RA Curwin A.J., Fairn G.D., McMaster C.R.; RT "Phospholipid transfer protein Sec14 is required for trafficking from RT endosomes and regulates distinct trans-Golgi export pathways."; RL J. Biol. Chem. 284:7364-7375(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [16] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-42 AND LYS-84, AND RP IDENTIFICATION BY 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 [17] RP FUNCTION, AND MUTAGENESIS OF GLY-266. RX PubMed=23383173; DOI=10.1371/journal.pone.0055388; RA Curwin A.J., Leblanc M.A., Fairn G.D., McMaster C.R.; RT "Localization of lipid raft proteins to the plasma membrane is a major RT function of the phospholipid transfer protein Sec14."; RL PLoS ONE 8:e55388-e55388(2013). RN [18] RP FUNCTION. RX PubMed=32828847; DOI=10.1016/j.bbamem.2020.183450; RA Sugiura T., Nakao H., Ikeda K., Khan D., Nile A.H., Bankaitis V.A., RA Nakano M.; RT "Biophysical parameters of the Sec14 phospholipid exchange cycle - Effect RT of lipid packing in membranes."; RL Biochim. Biophys. Acta 1863:183450-183450(2021). RN [19] {ECO:0007744|PDB:1AUA} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-299. RX PubMed=9461221; DOI=10.1038/35179; RA Sha B., Phillips S.E., Bankaitis V.A., Luo M.; RT "Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol- RT transfer protein."; RL Nature 391:506-510(1998). RN [20] {ECO:0007744|PDB:6F0E} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS). RX PubMed=29307839; DOI=10.1016/j.chembiol.2017.12.007; RA Pries V., Nocker C., Khan D., Johnen P., Hong Z., Tripathi A., Keller A.L., RA Fitz M., Perruccio F., Filipuzzi I., Thavam S., Aust T., Riedl R., RA Ziegler S., Bono F., Schaaf G., Bankaitis V.A., Waldmann H., Hoepfner D.; RT "Target identification and mechanism of action of picolinamide and RT benzamide chemotypes with antifungal properties."; RL Cell Chem. Biol. 25:279-290.e7(2018). CC -!- FUNCTION: Required for transport of secretory proteins from the Golgi CC complex. Catalyzes the transfer of phosphatidylinositol (PI) and CC phosphatidylcholine (PC) between membranes in vitro. Essential for CC viability and secretion (PubMed:2466847, PubMed:2215682). Exchanges its CC bound phospholipid with phospholipid monomers that reside in membrane CC bilayers (PubMed:16997918). Regulates specific trans-Golgi export CC pathways, like transport from endosomes to the trans-Golgi or transport CC from the plasma membrane to the vacuole at the level of the endosome CC (PubMed:19129178). Increased membrane curvature and lipid unsaturation CC levels at the trans-Golgi membrane promotes membrane binding and CC phospholipid transfer of SEC14. Thus, SEC14 may act at the trans-Golgi CC membrane to exchange lipids and promote vesicle formation CC (PubMed:32828847). The phosphatidylcholine-bound form of SEC14 CC represses the CDP-choline pathway activity by inhibiting CCTase, the CC rate-determining enzyme of the CDP-choline pathway (PubMed:7816798). PI CC binding/transfer is dispensable for function in vivo (PubMed:10488334). CC Required for trafficking and localization of lipid raft proteins to the CC plasma membrane (PubMed:23383173). {ECO:0000269|PubMed:10488334, CC ECO:0000269|PubMed:16997918, ECO:0000269|PubMed:19129178, CC ECO:0000269|PubMed:2215682, ECO:0000269|PubMed:23383173, CC ECO:0000269|PubMed:2466847, ECO:0000269|PubMed:32828847, CC ECO:0000269|PubMed:7816798}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out); CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880; CC Evidence={ECO:0000269|PubMed:10848624}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692; CC Evidence={ECO:0000269|PubMed:10848624}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl- CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:10848624}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; CC Evidence={ECO:0000269|PubMed:10848624}; CC -!- ACTIVITY REGULATION: The inhibitor activity of SEC14 is controlled by CC whether PI or PC is bound to SEC14. The pPC-bound form of SEC14 is an CC inhibitor, while the PI-bound form is not. The phospholipid CC binding/exchange activity of SEC14 represents a mechanism by which the CC regulatory activity of SEC14 is itself controlled. CC {ECO:0000269|PubMed:7816798}. CC -!- INTERACTION: CC P24280; P38797: PTC7; NbExp=4; IntAct=EBI-16535, EBI-24588; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:1997207}; Peripheral membrane protein. Cytoplasm CC {ECO:0000269|PubMed:12869188, ECO:0000269|PubMed:1997207, CC ECO:0000269|PubMed:2466847}. CC -!- MISCELLANEOUS: Present with 84300 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. 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; X15483; CAA33511.1; -; Genomic_DNA. DR EMBL; Z49259; CAA89225.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09977.1; -; Genomic_DNA. DR PIR; A30106; A30106. DR RefSeq; NP_013796.1; NM_001182578.1. DR PDB; 1AUA; X-ray; 2.50 A; A=4-299. DR PDB; 6F0E; X-ray; 2.60 A; A=1-304. DR PDB; 7ZG9; X-ray; 1.76 A; A/B=3-301. DR PDB; 7ZGA; X-ray; 2.30 A; A=3-298. DR PDB; 7ZGB; X-ray; 2.70 A; A=4-299. DR PDB; 7ZGC; X-ray; 2.24 A; A=1-304. DR PDB; 7ZGD; X-ray; 2.08 A; A=1-304. DR PDBsum; 1AUA; -. DR PDBsum; 6F0E; -. DR PDBsum; 7ZG9; -. DR PDBsum; 7ZGA; -. DR PDBsum; 7ZGB; -. DR PDBsum; 7ZGC; -. DR PDBsum; 7ZGD; -. DR AlphaFoldDB; P24280; -. DR SMR; P24280; -. DR BioGRID; 35255; 273. DR DIP; DIP-1610N; -. DR IntAct; P24280; 8. DR MINT; P24280; -. DR STRING; 4932.YMR079W; -. DR SwissLipids; SLP:000000359; -. DR iPTMnet; P24280; -. DR MaxQB; P24280; -. DR PaxDb; 4932-YMR079W; -. DR PeptideAtlas; P24280; -. DR EnsemblFungi; YMR079W_mRNA; YMR079W; YMR079W. DR GeneID; 855103; -. DR KEGG; sce:YMR079W; -. DR AGR; SGD:S000004684; -. DR SGD; S000004684; SEC14. DR VEuPathDB; FungiDB:YMR079W; -. DR eggNOG; KOG1471; Eukaryota. DR GeneTree; ENSGT00530000066638; -. DR HOGENOM; CLU_014001_0_1_1; -. DR InParanoid; P24280; -. DR OMA; WAFSTVW; -. DR OrthoDB; 6048at2759; -. DR BioCyc; YEAST:G3O-32781-MONOMER; -. DR BioGRID-ORCS; 855103; 1 hit in 10 CRISPR screens. DR EvolutionaryTrace; P24280; -. DR PRO; PR:P24280; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P24280; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD. DR GO; GO:0000139; C:Golgi membrane; IDA:SGD. DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IDA:SGD. DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:SGD. DR GO; GO:0030437; P:ascospore formation; IMP:SGD. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:SGD. DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD. DR GO; GO:0048194; P:Golgi vesicle budding; IDA:SGD. DR GO; GO:2001246; P:negative regulation of phosphatidylcholine biosynthetic process; IDA:SGD. DR GO; GO:1901352; P:negative regulation of phosphatidylglycerol biosynthetic process; IMP:SGD. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:SGD. DR GO; GO:0015914; P:phospholipid transport; IDA:SGD. DR CDD; cd00170; SEC14; 1. DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1. DR Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1. DR InterPro; IPR001251; CRAL-TRIO_dom. DR InterPro; IPR036865; CRAL-TRIO_dom_sf. DR InterPro; IPR011074; CRAL/TRIO_N_dom. DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf. DR PANTHER; PTHR45657; CRAL-TRIO DOMAIN-CONTAINING PROTEIN YKL091C-RELATED; 1. DR PANTHER; PTHR45657:SF1; CRAL-TRIO DOMAIN-CONTAINING PROTEIN YKL091C-RELATED; 1. DR Pfam; PF00650; CRAL_TRIO; 1. DR Pfam; PF03765; CRAL_TRIO_N; 1. DR PRINTS; PR00180; CRETINALDHBP. DR SMART; SM01100; CRAL_TRIO_N; 1. DR SMART; SM00516; SEC14; 1. DR SUPFAM; SSF52087; CRAL/TRIO domain; 1. DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1. DR PROSITE; PS50191; CRAL_TRIO; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Golgi apparatus; KW Isopeptide bond; Membrane; Phosphoprotein; Protein transport; KW Reference proteome; Transport; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2407740" FT CHAIN 2..304 FT /note="SEC14 cytosolic factor" FT /id="PRO_0000210744" FT DOMAIN 99..272 FT /note="CRAL-TRIO" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056" FT MOD_RES 302 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT CROSSLNK 42 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 84 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 66 FT /note="K->A: Inactivates phosphatidylinositol, but not FT phosphatidylcholine, transfer activity, but rescues the FT lethality and Golgi secretory defects associated with sec14 FT null mutations; when associated with A-239." FT /evidence="ECO:0000269|PubMed:10488334" FT MUTAGEN 239 FT /note="K->A: Inactivates phosphatidylinositol, but not FT phosphatidylcholine, transfer activity, but rescues the FT lethality and Golgi secretory defects associated with sec14 FT null mutations; when associated with A-66." FT /evidence="ECO:0000269|PubMed:10488334" FT MUTAGEN 266 FT /note="G->D: In SEC14(ts); temperature-sesnitive allele FT that is targeted to the proteasome at the restrictive FT temperature." FT /evidence="ECO:0000269|PubMed:23383173" FT HELIX 4..10 FT /evidence="ECO:0007829|PDB:7ZG9" FT TURN 26..28 FT /evidence="ECO:0007829|PDB:1AUA" FT HELIX 31..46 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 55..64 FT /evidence="ECO:0007829|PDB:7ZG9" FT TURN 65..67 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 69..86 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 91..94 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 100..103 FT /evidence="ECO:0007829|PDB:7ZG9" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:7ZG9" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:7ZG9" FT STRAND 120..125 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:7ZGD" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:7ZG9" FT TURN 135..137 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 140..156 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 158..166 FT /evidence="ECO:0007829|PDB:7ZG9" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 184..189 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 191..204 FT /evidence="ECO:0007829|PDB:7ZG9" FT STRAND 209..216 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 219..228 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 234..237 FT /evidence="ECO:0007829|PDB:7ZG9" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 248..254 FT /evidence="ECO:0007829|PDB:7ZG9" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:7ZGD" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:7ZG9" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:7ZG9" FT TURN 288..290 FT /evidence="ECO:0007829|PDB:7ZG9" SQ SEQUENCE 304 AA; 34901 MW; CCB69404A8A0963B CRC64; MVTQQEKEFL ESYPQNCPPD ALPGTPGNLD SAQEKALAEL RKLLEDAGFI ERLDDSTLLR FLRARKFDVQ LAKEMFENCE KWRKDYGTDT ILQDFHYDEK PLIAKFYPQY YHKTDKDGRP VYFEELGAVN LHEMNKVTSE ERMLKNLVWE YESVVQYRLP ACSRAAGHLV ETSCTIMDLK GISISSAYSV MSYVREASYI SQNYYPERMG KFYIINAPFG FSTAFRLFKP FLDPVTVSKI FILGSSYQKE LLKQIPAENL PVKFGGKSEV DESKGGLYLS DIGPWRDPKY IGPEGEAPEA FSMK //