PGAP1_HUMAN
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 03-AUG-2022, entry version 148.
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};
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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; 30.
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 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; Q75T13; -.
DR PeptideAtlas; Q75T13; -.
DR PRIDE; Q75T13; -.
DR ProteomicsDB; 68649; -. [Q75T13-1]
DR ProteomicsDB; 68650; -. [Q75T13-2]
DR ProteomicsDB; 68651; -. [Q75T13-3]
DR ProteomicsDB; 68652; -. [Q75T13-4]
DR Antibodypedia; 34062; 36 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 CTD; 80055; -.
DR DisGeNET; 80055; -.
DR GeneCards; PGAP1; -.
DR HGNC; HGNC:25712; PGAP1.
DR HPA; ENSG00000197121; Tissue enriched (brain).
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; 438490at2759; -.
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 1065 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 186 other 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495; PTHR15495; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; SSF53474; 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
