ID PIGS_HUMAN Reviewed; 555 AA. AC Q96S52; Q6UVX6; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 163. DE RecName: Full=GPI transamidase component PIG-S; DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class S protein; GN Name=PIGS; ORFNames=UNQ1873/PRO4316; 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] (ISOFORM 1), PROTEIN SEQUENCE OF 2-21, FUNCTION, RP SUBUNIT, SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY. RX PubMed=11483512; DOI=10.1093/emboj/20.15.4088; RA Ohishi K., Inoue N., Kinoshita T.; RT "PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a RT complex with GAA1 and GPI8."; RL EMBO J. 20:4088-4098(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [4] 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [6] RP INVOLVEMENT IN GPIBD18, VARIANTS GPIBD18 PRO-34; 36-TRP--ASP-555 DEL; RP GLY-308 AND 439-THR--LYS-451 DELINS ARG-LEU-LEU, PATHWAY, AND FUNCTION. RX PubMed=30269814; DOI=10.1016/j.ajhg.2018.08.014; RA Nguyen T.T.M., Murakami Y., Wigby K.M., Baratang N.V., Rousseau J., RA St-Denis A., Rosenfeld J.A., Laniewski S.C., Jones J., Iglesias A.D., RA Jones M.C., Masser-Frye D., Scheuerle A.E., Perry D.L., Taft R.J., RA Le Deist F., Thompson M., Kinoshita T., Campeau P.M.; RT "Mutations in PIGS, encoding a GPI transamidase, cause a neurological RT syndrome ranging from fetal akinesia to epileptic encephalopathy."; RL Am. J. Hum. Genet. 103:602-611(2018). RN [7] RP MUTAGENESIS OF ARG-43; PRO-47; ASN-267; SER-272; TYR-276; PRO-301; PRO-335; RP ASN-370; SER-444; 459-ASP-ASP-460 AND 515-ASP-ASP-516, AND FUNCTION. RX PubMed=34576938; DOI=10.3390/molecules26185462; RA Liu S.S., Jin F., Liu Y.S., Murakami Y., Sugita Y., Kato T., Gao X.D., RA Kinoshita T., Hattori M., Fujita M.; RT "Functional analysis of the GPI transamidase complex by screening for amino RT acid mutations in each subunit."; RL Molecules 26:0-0(2021). RN [8] RP VARIANT [LARGE SCALE ANALYSIS] ILE-159. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Component of the GPI transamidase complex. Essential for CC transfer of GPI to proteins, particularly for formation of carbonyl CC intermediates. {ECO:0000269|PubMed:11483512, CC ECO:0000269|PubMed:30269814, ECO:0000269|PubMed:34576938}. CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor CC biosynthesis. {ECO:0000269|PubMed:30269814}. CC -!- SUBUNIT: Forms a complex with PIGK/GPI8, PIGT, PIGU and GAA1. CC {ECO:0000269|PubMed:11483512}. CC -!- INTERACTION: CC Q96S52; Q6A162: KRT40; NbExp=3; IntAct=EBI-2908273, EBI-10171697; CC Q96S52; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-2908273, EBI-11749135; CC Q96S52; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2908273, EBI-10171774; CC Q96S52; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-2908273, EBI-10172052; CC Q96S52; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-2908273, EBI-12196745; CC Q96S52; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-2908273, EBI-14065470; CC Q96S52; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-2908273, EBI-1044640; CC Q96S52; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-2908273, EBI-945833; CC Q96S52; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2908273, EBI-22310682; CC Q96S52; Q969N2: PIGT; NbExp=11; IntAct=EBI-2908273, EBI-726383; CC Q96S52; Q15654: TRIP6; NbExp=3; IntAct=EBI-2908273, EBI-742327; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:11483512}; Multi-pass membrane protein CC {ECO:0000269|PubMed:11483512}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96S52-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96S52-2; Sequence=VSP_013158; CC -!- DISEASE: Glycosylphosphatidylinositol biosynthesis defect 18 (GPIBD18) CC [MIM:618143]: An autosomal recessive disorder with onset in utero or CC early infancy and characterized by severe global developmental delay, CC seizures, hypotonia, weakness, ataxia, and dysmorphic facial features. CC {ECO:0000269|PubMed:30269814}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the PIGS family. {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; AB057723; BAB60853.1; -; mRNA. DR EMBL; AY359112; AAQ89470.1; -; mRNA. DR EMBL; BC069228; AAH69228.1; -; mRNA. DR CCDS; CCDS11235.1; -. [Q96S52-1] DR RefSeq; NP_149975.1; NM_033198.3. [Q96S52-1] DR PDB; 7W72; EM; 3.10 A; S=7-539. DR PDB; 7WLD; EM; 2.53 A; S=2-555. DR PDB; 8IMX; EM; 2.85 A; S=2-555. DR PDB; 8IMY; EM; 3.22 A; S=2-555. DR PDBsum; 7W72; -. DR PDBsum; 7WLD; -. DR PDBsum; 8IMX; -. DR PDBsum; 8IMY; -. DR AlphaFoldDB; Q96S52; -. DR EMDB; EMD-32336; -. DR EMDB; EMD-32582; -. DR SMR; Q96S52; -. DR BioGRID; 125082; 178. DR ComplexPortal; CPX-6503; GPI-anchor transamidase complex. DR CORUM; Q96S52; -. DR IntAct; Q96S52; 47. DR MINT; Q96S52; -. DR STRING; 9606.ENSP00000309430; -. DR GlyConnect; 1285; 1 N-Linked glycan (1 site). DR GlyCosmos; Q96S52; 3 sites, 2 glycans. DR GlyGen; Q96S52; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; Q96S52; -. DR PhosphoSitePlus; Q96S52; -. DR SwissPalm; Q96S52; -. DR BioMuta; PIGS; -. DR DMDM; 21759353; -. DR EPD; Q96S52; -. DR jPOST; Q96S52; -. DR MassIVE; Q96S52; -. DR MaxQB; Q96S52; -. DR PaxDb; 9606-ENSP00000309430; -. DR PeptideAtlas; Q96S52; -. DR ProteomicsDB; 78065; -. [Q96S52-1] DR ProteomicsDB; 78066; -. [Q96S52-2] DR Pumba; Q96S52; -. DR Antibodypedia; 2984; 124 antibodies from 24 providers. DR DNASU; 94005; -. DR Ensembl; ENST00000308360.8; ENSP00000309430.7; ENSG00000087111.22. [Q96S52-1] DR Ensembl; ENST00000395346.6; ENSP00000378755.2; ENSG00000087111.22. [Q96S52-2] DR GeneID; 94005; -. DR KEGG; hsa:94005; -. DR MANE-Select; ENST00000308360.8; ENSP00000309430.7; NM_033198.4; NP_149975.1. DR UCSC; uc002hbn.3; human. [Q96S52-1] DR AGR; HGNC:14937; -. DR CTD; 94005; -. DR DisGeNET; 94005; -. DR GeneCards; PIGS; -. DR HGNC; HGNC:14937; PIGS. DR HPA; ENSG00000087111; Low tissue specificity. DR MalaCards; PIGS; -. DR MIM; 610271; gene. DR MIM; 618143; phenotype. DR neXtProt; NX_Q96S52; -. DR OpenTargets; ENSG00000087111; -. DR PharmGKB; PA33301; -. DR VEuPathDB; HostDB:ENSG00000087111; -. DR eggNOG; KOG2459; Eukaryota. DR GeneTree; ENSGT00390000017203; -. DR HOGENOM; CLU_010026_3_0_1; -. DR InParanoid; Q96S52; -. DR OMA; AEHKYAV; -. DR OrthoDB; 5476244at2759; -. DR PhylomeDB; Q96S52; -. DR TreeFam; TF105857; -. DR PathwayCommons; Q96S52; -. DR Reactome; R-HSA-162791; Attachment of GPI anchor to uPAR. DR SignaLink; Q96S52; -. DR SIGNOR; Q96S52; -. DR UniPathway; UPA00196; -. DR BioGRID-ORCS; 94005; 95 hits in 1176 CRISPR screens. DR ChiTaRS; PIGS; human. DR GeneWiki; PIGS_(gene); -. DR GenomeRNAi; 94005; -. DR Pharos; Q96S52; Tdark. DR PRO; PR:Q96S52; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96S52; Protein. DR Bgee; ENSG00000087111; Expressed in stromal cell of endometrium and 101 other cell types or tissues. DR ExpressionAtlas; Q96S52; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042765; C:GPI-anchor transamidase complex; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016255; P:attachment of GPI anchor to protein; IBA:GO_Central. DR InterPro; IPR019540; PtdIno-glycan_biosynth_class_S. DR PANTHER; PTHR21072; GPI TRANSAMIDASE COMPONENT PIG-S; 1. DR PANTHER; PTHR21072:SF13; GPI TRANSAMIDASE COMPONENT PIG-S; 1. DR Pfam; PF10510; PIG-S; 1. DR Genevisible; Q96S52; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disease variant; Endoplasmic reticulum; Epilepsy; Glycoprotein; KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11483512" FT CHAIN 2..555 FT /note="GPI transamidase component PIG-S" FT /id="PRO_0000218604" FT TOPO_DOM 2..18 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 19..39 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 40..520 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 521..541 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 542..555 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 267 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 370 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..11 FT /note="MAAAGAAATHL -> MPS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_013158" FT VARIANT 34 FT /note="L -> P (in GPIBD18; partial loss of function; when FT tested in PIGS-knockout cells, mediates partial restoration FT of GPI-anchored protein expression at the cell surface; FT dbSNP:rs1567618413)" FT /evidence="ECO:0000269|PubMed:30269814" FT /id="VAR_081579" FT VARIANT 36..555 FT /note="Missing (in GPIBD18; almost complete loss of FT function; when tested in PIGS-knockout cells, mediates only FT very partial restoration of GPI-anchored protein expression FT at the cell surface; strong decrease in protein level, FT possibly due to nonsense-mediated mRNA decay)" FT /evidence="ECO:0000269|PubMed:30269814" FT /id="VAR_081580" FT VARIANT 159 FT /note="M -> I (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036510" FT VARIANT 253 FT /note="R -> H (in dbSNP:rs34669811)" FT /id="VAR_053582" FT VARIANT 308 FT /note="E -> G (in GPIBD18; dbSNP:rs1426262136)" FT /evidence="ECO:0000269|PubMed:30269814" FT /id="VAR_081581" FT VARIANT 439..451 FT /note="TTTLTSLAQLLGK -> RLL (in GPIBD18; uncertain FT significance)" FT /evidence="ECO:0000269|PubMed:30269814" FT /id="VAR_081582" FT MUTAGEN 43 FT /note="R->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 47 FT /note="P->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 267 FT /note="N->Q: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 272 FT /note="S->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 276 FT /note="Y->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 301 FT /note="P->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 335 FT /note="P->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 370 FT /note="N->Q: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 444 FT /note="S->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 459..460 FT /note="DD->AA: No effect on function in GPI-anchor FT attachment to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 515..516 FT /note="DD->AA: No effect on function in GPI-anchor FT attachment to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT HELIX 4..38 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 48..54 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 58..69 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 71..73 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 78..81 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 85..92 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:8IMX" FT STRAND 99..107 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 113..120 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 124..131 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:8IMX" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 164..166 FT /evidence="ECO:0007829|PDB:8IMY" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 180..192 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 197..200 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:7W72" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 225..236 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 238..240 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 241..244 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 247..253 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 255..262 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 267..277 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 288..291 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 297..299 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 305..307 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 308..311 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 317..319 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 321..327 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 335..339 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 350..353 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 354..356 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 357..361 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 367..370 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 372..379 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 382..396 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 408..410 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 415..417 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 420..451 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 459..481 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 484..502 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 505..507 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 509..511 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 515..517 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 518..522 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 523..525 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 527..530 FT /evidence="ECO:0007829|PDB:7WLD" SQ SEQUENCE 555 AA; 61656 MW; A20B323C5475EF4F CRC64; MAAAGAAATH LEVARGKRAA LFFAAVAIVL GLPLWWKTTE TYRASLPYSQ ISGLNALQLR LMVPVTVVFT RESVPLDDQE KLPFTVVHER EIPLKYKMKI KCRFQKAYRR ALDHEEEALS SGSVQEAEAM LDEPQEQAEG SLTVYVISEH SSLLPQDMMS YIGPKRTAVV RGIMHREAFN IIGRRIVQVA QAMSLTEDVL AAALADHLPE DKWSAEKRRP LKSSLGYEIT FSLLNPDPKS HDVYWDIEGA VRRYVQPFLN ALGAAGNFSV DSQILYYAML GVNPRFDSAS SSYYLDMHSL PHVINPVESR LGSSAASLYP VLNFLLYVPE LAHSPLYIQD KDGAPVATNA FHSPRWGGIM VYNVDSKTYN ASVLPVRVEV DMVRVMEVFL AQLRLLFGIA QPQLPPKCLL SGPTSEGLMT WELDRLLWAR SVENLATATT TLTSLAQLLG KISNIVIKDD VASEVYKAVA AVQKSAEELA SGHLASAFVA SQEAVTSSEL AFFDPSLLHL LYFPDDQKFA IYIPLFLPMA VPILLSLVKI FLETRKSWRK PEKTD //