ID PGAP1_HUMAN Reviewed; 922 AA. AC Q75T13; Q4G0R8; Q4ZG47; Q53SM0; Q6AW92; Q6UWV4; Q9HA24; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=GPI inositol-deacylase; DE EC=3.1.-.-; DE AltName: Full=Post-GPI attachment to proteins factor 1; DE Short=hPGAP1; GN Name=PGAP1; ORFNames=UNQ3024/PRO9822; 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). RX PubMed=14734546; DOI=10.1074/jbc.m313755200; RA Tanaka S., Maeda Y., Tashima Y., Kinoshita T.; RT "Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is RT mediated by mammalian PGAP1 and yeast Bst1p."; RL J. Biol. Chem. 279:14256-14263(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Fetal kidney; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-922 (ISOFORMS 1/2). 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 [7] RP INVOLVEMENT IN NEDDSBA, VARIANT NEDDSBA LEU-197 DEL, AND CHARACTERIZATION RP OF VARIANT NEDDSBA LEU-197 DEL. RX PubMed=24784135; DOI=10.1371/journal.pgen.1004320; RA Murakami Y., Tawamie H., Maeda Y., Buettner C., Buchert R., Radwan F., RA Schaffer S., Sticht H., Aigner M., Reis A., Kinoshita T., Jamra R.A.; RT "Null mutation in PGAP1 impairing Gpi-anchor maturation in patients with RT intellectual disability and encephalopathy."; RL PLoS Genet. 10:E1004320-E1004320(2014). RN [8] RP INVOLVEMENT IN NEDDSBA. RX PubMed=24482476; DOI=10.1126/science.1247363; RA Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L., RA Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A., RA Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M., RA Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G., RA Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S., RA Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M., RA Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J., RA Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A., RA Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T., RA Gleeson J.G.; RT "Exome sequencing links corticospinal motor neuron disease to common RT neurodegenerative disorders."; RL Science 343:506-511(2014). CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins. CC GPI inositol deacylation may important for efficient transport of GPI- CC anchored proteins from the endoplasmic reticulum to the Golgi (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q75T13-1; Sequence=Displayed; CC Name=2; CC IsoId=Q75T13-2; Sequence=VSP_023040; CC Name=3; CC IsoId=Q75T13-3; Sequence=VSP_023042, VSP_023043; CC Name=4; CC IsoId=Q75T13-4; Sequence=VSP_023041, VSP_023044; CC -!- DISEASE: Neurodevelopmental disorder with dysmorphic features, CC spasticity, and brain abnormalities (NEDDSBA) [MIM:615802]: An CC autosomal recessive disorder characterized by severely delayed global CC development, with hypotonia, impaired intellectual development, and CC poor or absent speech. Most patients have spasticity with limb CC hypertonia and brisk tendon reflexes. Additional features include non- CC specific dysmorphic facial features, structural brain abnormalities, CC and cortical visual impairment. {ECO:0000269|PubMed:24482476, CC ECO:0000269|PubMed:24784135}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ88987.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BC040517; Type=Frameshift; Evidence={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; AB128038; BAD13427.1; -; mRNA. DR EMBL; AK022439; BAB14035.1; -; mRNA. DR EMBL; BX648642; CAH10543.1; -; mRNA. DR EMBL; AC017035; AAY15059.1; -; Genomic_DNA. DR EMBL; AC012486; AAX88854.1; -; Genomic_DNA. DR EMBL; BC040517; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AY358624; AAQ88987.1; ALT_INIT; mRNA. DR CCDS; CCDS2318.1; -. [Q75T13-1] DR RefSeq; NP_001308028.1; NM_001321099.1. [Q75T13-2] DR RefSeq; NP_001308029.1; NM_001321100.1. DR RefSeq; NP_079265.2; NM_024989.3. [Q75T13-1] DR RefSeq; XP_016860481.1; XM_017004992.1. [Q75T13-2] DR RefSeq; XP_016860482.1; XM_017004993.1. [Q75T13-2] DR AlphaFoldDB; Q75T13; -. DR BioGRID; 123093; 33. DR IntAct; Q75T13; 10. DR MINT; Q75T13; -. DR STRING; 9606.ENSP00000346809; -. DR ESTHER; human-PGAP1; PGAP1. DR GlyConnect; 2044; 1 N-Linked glycan (1 site). DR GlyCosmos; Q75T13; 2 sites, 2 glycans. DR GlyGen; Q75T13; 4 sites, 2 N-linked glycans (1 site). DR iPTMnet; Q75T13; -. DR PhosphoSitePlus; Q75T13; -. DR BioMuta; PGAP1; -. DR DMDM; 74758940; -. DR EPD; Q75T13; -. DR jPOST; Q75T13; -. DR MassIVE; Q75T13; -. DR MaxQB; Q75T13; -. DR PaxDb; 9606-ENSP00000346809; -. DR PeptideAtlas; Q75T13; -. DR ProteomicsDB; 68649; -. [Q75T13-1] DR ProteomicsDB; 68650; -. [Q75T13-2] DR ProteomicsDB; 68651; -. [Q75T13-3] DR ProteomicsDB; 68652; -. [Q75T13-4] DR Pumba; Q75T13; -. DR Antibodypedia; 34062; 37 antibodies from 15 providers. DR DNASU; 80055; -. DR Ensembl; ENST00000354764.9; ENSP00000346809.3; ENSG00000197121.15. [Q75T13-1] DR Ensembl; ENST00000409475.5; ENSP00000387028.1; ENSG00000197121.15. [Q75T13-3] DR GeneID; 80055; -. DR KEGG; hsa:80055; -. DR MANE-Select; ENST00000354764.9; ENSP00000346809.3; NM_024989.4; NP_079265.2. DR UCSC; uc002utw.4; human. [Q75T13-1] DR AGR; HGNC:25712; -. DR CTD; 80055; -. DR DisGeNET; 80055; -. DR GeneCards; PGAP1; -. DR HGNC; HGNC:25712; PGAP1. DR HPA; ENSG00000197121; Low tissue specificity. DR MalaCards; PGAP1; -. DR MIM; 611655; gene. DR MIM; 615802; phenotype. DR neXtProt; NX_Q75T13; -. DR OpenTargets; ENSG00000197121; -. DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability. DR Orphanet; 401820; Autosomal recessive spastic paraplegia type 67. DR PharmGKB; PA162399235; -. DR VEuPathDB; HostDB:ENSG00000197121; -. DR eggNOG; KOG3724; Eukaryota. DR GeneTree; ENSGT00390000016484; -. DR HOGENOM; CLU_013735_1_0_1; -. DR InParanoid; Q75T13; -. DR OMA; YGLYYYY; -. DR OrthoDB; 5477082at2759; -. DR PhylomeDB; Q75T13; -. DR TreeFam; TF314565; -. DR PathwayCommons; Q75T13; -. DR Reactome; R-HSA-162791; Attachment of GPI anchor to uPAR. DR SignaLink; Q75T13; -. DR BioGRID-ORCS; 80055; 10 hits in 1147 CRISPR screens. DR ChiTaRS; PGAP1; human. DR GenomeRNAi; 80055; -. DR Pharos; Q75T13; Tbio. DR PRO; PR:Q75T13; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q75T13; Protein. DR Bgee; ENSG00000197121; Expressed in endothelial cell and 188 other cell types or tissues. DR ExpressionAtlas; Q75T13; baseline and differential. DR Genevisible; Q75T13; HS. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; TAS:Reactome. DR GO; GO:0050185; F:phosphatidylinositol deacylase activity; ISS:UniProtKB. DR GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl. DR GO; GO:0016255; P:attachment of GPI anchor to protein; TAS:Reactome. DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central. DR GO; GO:0021871; P:forebrain regionalization; IEA:Ensembl. DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central. DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; ISS:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR012908; PGAP1-like. DR InterPro; IPR039529; PGAP1/BST1. DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1. DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1. DR Pfam; PF07819; PGAP1; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00120; LIPASE_SER; 1. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein; KW Hydrolase; Intellectual disability; Membrane; Protein transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..922 FT /note="GPI inositol-deacylase" FT /id="PRO_0000277623" FT TOPO_DOM 1..11 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 33..641 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 642..662 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 663..668 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 669..689 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 690..733 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 734..754 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 755..817 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 818..838 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 839..853 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 854..874 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 875..893 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 894..914 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 915..922 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 775..799 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 781..799 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 174 FT /evidence="ECO:0000250" FT CARBOHYD 402 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 558 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..174 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_023040" FT VAR_SEQ 50..269 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023041" FT VAR_SEQ 592 FT /note="R -> A (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023042" FT VAR_SEQ 593..922 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023043" FT VAR_SEQ 652..922 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023044" FT VARIANT 197 FT /note="Missing (in NEDDSBA; results in loss of PI-specific FT phospholipase C sensitivity which could be rescued by FT expression of the wild-type protein; dbSNP:rs587777378)" FT /evidence="ECO:0000269|PubMed:24784135" FT /id="VAR_071772" FT CONFLICT 304 FT /note="D -> G (in Ref. 2; BAB14035)" FT /evidence="ECO:0000305" FT CONFLICT 389 FT /note="T -> A (in Ref. 3; CAH10543)" FT /evidence="ECO:0000305" FT CONFLICT 701 FT /note="S -> P (in Ref. 3; CAH10543)" FT /evidence="ECO:0000305" FT CONFLICT 809 FT /note="A -> T (in Ref. 3; CAH10543)" FT /evidence="ECO:0000305" SQ SEQUENCE 922 AA; 105383 MW; 0305D18F5BF292D6 CRC64; MFLHSVNLWN LAFYVFMVFL ATLGLWDVFF GFEENKCSMS YMFEYPEYQK IELPKKLAKR YPAYELYLYG EGSYAEEHKI LPLTGIPVLF LPGNAGSYKQ VRSIGSIALR KAEDIDFKYH FDFFSVNFNE ELVALYGGSL QKQTKFVHEC IKTILKLYKG QEFAPKSVAI IGHSMGGLVA RALLTLKNFK HDLINLLITQ ATPHVAPVMP LDRFITDFYT TVNNYWILNA RHINLTTLSV AGGFRDYQVR SGLTFLPKLS HHTSALSVVS SAVPKTWVST DHLSIVWCKQ LQLTTVRAFF DLIDADTKQI TQNSKKKLSV LYHHFIRHPS KHFEENPAII SDLTGTSMWV LVKVSKWTYV AYNESEKIYF TFPLENHRKI YTHVYCQSTM LDTNSWIFAC INSTSMCLQG VDLSWKAELL PTIKYLTLRL QDYPSLSHLV VYVPSVRGSK FVVDCEFFKK EKRYIQLPVT HLFSFGLSSR KVVLNTNGLY YNLELLNFGQ IYQAFKINVV SKCSAVKEEI TSIYRLHIPW SYEDSLTIAQ APSSTEISLK LHIAQPENNT HVALFKMYTS SDCRYEVTVK TSFSQILGQV VRFHGGALPA YVVSNILLAY RGQLYSLFST GCCLEYATML DKEAKPYKVD PFVIIIKFLL GYKWFKELWD VLLLPELDAV ILTCQSMCFP LISLILFLFG TCTAYWSGLL SSASVRLLSS LWLALKRPSE LPKDIKMISP DLPFLTIVLI IVSWTTCGAL AILLSYLYYV FKVVHLQASL TTFKNSQPVN PKHSRRSEKK SNHHKDSSIH HLRLSANDAE DSLRMHSTVI NLLTWIVLLS MPSLIYWLKN LRYYFKLNPD PCKPLAFILI PTMAILGNTY TVSIKSSKLL KTTSQFPLPL AVGVIAFGSA HLYRLPCFVF IPLLLHALCN FM //