PIGQ_HUMAN
ID PIGQ_HUMAN Reviewed; 760 AA.
AC Q9BRB3; A2IDE1; D3DU52; O14927; Q96G00; Q96S22; Q9UJH4;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q {ECO:0000305};
DE AltName: Full=N-acetylglucosamyl transferase component GPI1;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class Q protein;
DE Short=PIG-Q;
GN Name=PIGQ {ECO:0000312|HGNC:HGNC:14135}; Synonyms=GPI1;
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 2).
RX PubMed=9729469; DOI=10.1042/bj3340609;
RA Tiede A., Schubert J., Nischan C., Jensen I., Westfall B., Taron C.H.,
RA Orlean P., Schmidt R.E.;
RT "Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol
RT membrane anchor biosynthesis in yeast mutants.";
RL Biochem. J. 334:609-616(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PIGA; PIGH AND
RP PIGC, COMPONENT OF GPI-GNT COMPLEX, AND FUNCTION.
RX PubMed=9463366; DOI=10.1093/emboj/17.4.877;
RA Watanabe R., Inoue N., Westfall B., Taron C.H., Orlean P., Takeda J.,
RA Kinoshita T.;
RT "The first step of glycosylphosphatidylinositol biosynthesis is mediated by
RT a complex of PIG-A, PIG-H, PIG-C and GPI1.";
RL EMBO J. 17:877-885(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-14.
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ALA-14.
RC TISSUE=Melanoma, and Retinoblastoma;
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 [7]
RP PROTEIN SEQUENCE OF 2-6.
RX PubMed=10944123; DOI=10.1093/emboj/19.16.4402;
RA Watanabe R., Murakami Y., Marmor M.D., Inoue N., Maeda Y., Hino J.,
RA Kangawa K., Julius M., Kinoshita T.;
RT "Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-
RT P and is regulated by DPM2.";
RL EMBO J. 19:4402-4411(2000).
RN [8]
RP COMPONENT OF GPI-GNT COMPLEX, AND FUNCTION.
RX PubMed=16162815; DOI=10.1091/mbc.e05-08-0743;
RA Murakami Y., Siripanyaphinyo U., Hong Y., Tashima Y., Maeda Y.,
RA Kinoshita T.;
RT "The initial enzyme for glycosylphosphatidylinositol biosynthesis requires
RT PIG-Y, a seventh component.";
RL Mol. Biol. Cell 16:5236-5246(2005).
RN [9]
RP INVOLVEMENT IN MCAHS4.
RX PubMed=24463883; DOI=10.1093/hmg/ddu030;
RG WGS500 Consortium;
RA Martin H.C., Kim G.E., Pagnamenta A.T., Murakami Y., Carvill G.L.,
RA Meyer E., Copley R.R., Rimmer A., Barcia G., Fleming M.R., Kronengold J.,
RA Brown M.R., Hudspith K.A., Broxholme J., Kanapin A., Cazier J.B.,
RA Kinoshita T., Nabbout R., Bentley D., McVean G., Heavin S., Zaiwalla Z.,
RA McShane T., Mefford H.C., Shears D., Stewart H., Kurian M.A.,
RA Scheffer I.E., Blair E., Donnelly P., Kaczmarek L.K., Taylor J.C.;
RT "Clinical whole-genome sequencing in severe early-onset epilepsy reveals
RT new genes and improves molecular diagnosis.";
RL Hum. Mol. Genet. 23:3200-3211(2014).
RN [10]
RP INVOLVEMENT IN MCAHS4, AND VARIANT MCAHS4 207-ARG--LEU-760 DEL.
RX PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
RA Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
RA Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
RA Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S.,
RA Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A.,
RA Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W.,
RA Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N.,
RA Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S.,
RA Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F.,
RA Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R.,
RA Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.;
RT "Accelerating novel candidate gene discovery in neurogenetic disorders via
RT whole-exome sequencing of prescreened multiplex consanguineous families.";
RL Cell Rep. 10:148-161(2015).
RN [11]
RP VARIANT MCAHS4 TYR-400 DEL.
RX PubMed=27513193; DOI=10.1038/gim.2016.95;
RA Farwell Hagman K.D., Shinde D.N., Mroske C., Smith E., Radtke K.,
RA Shahmirzadi L., El-Khechen D., Powis Z., Chao E.C., Alcaraz W.A.,
RA Helbig K.L., Sajan S.A., Rossi M., Lu H.M., Huether R., Li S., Wu S.,
RA Nunes M.E., Tang S.;
RT "Candidate-gene criteria for clinical reporting: diagnostic exome
RT sequencing identifies altered candidate genes among 8% of patients with
RT undiagnosed diseases.";
RL Genet. Med. 19:224-235(2017).
RN [12]
RP ERRATUM OF PUBMED:27513193.
RX PubMed=29388939; DOI=10.1038/gim.2017.263;
RA Farwell Hagman K.D., Shinde D.N., Mroske C., Smith E., Radtke K.,
RA Shahmirzadi L., El-Khechen D., Powis Z., Chao E.C., Alcaraz W.A.,
RA Helbig K.L., Sajan S.A., Rossi M., Lu H.M., Huether R., Li S., Wu S.,
RA Nunes M.E., Tang S.;
RL Genet. Med. 20:1099-1102(2018).
RN [13]
RP VARIANT MCAHS4 TYR-400 DEL.
RX PubMed=31148362; DOI=10.1002/ajmg.a.61185;
RA Starr L.J., Spranger J.W., Rao V.K., Lutz R., Yetman A.T.;
RT "PIGQ glycosylphosphatidylinositol-anchored protein deficiency:
RT Characterizing the phenotype.";
RL Am. J. Med. Genet. A 179:1270-1275(2019).
CC -!- FUNCTION: Part of the glycosylphosphatidylinositol-N-
CC acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the
CC transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to
CC phosphatidylinositol and participates in the first step of GPI
CC biosynthesis. {ECO:0000269|PubMed:16162815,
CC ECO:0000269|PubMed:9463366}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000269|PubMed:16162815,
CC ECO:0000269|PubMed:9463366}.
CC -!- SUBUNIT: Component of the glycosylphosphatidylinositol-N-
CC acetylglucosaminyltransferase (GPI-GnT) complex composed at least by
CC PIGA, PIGC, PIGH, PIGP, PIGQ, PIGY and DPM2 (PubMed:16162815,
CC PubMed:9463366). Interacts with PIGA, PIGH and PIGC (PubMed:9463366).
CC {ECO:0000269|PubMed:16162815, ECO:0000269|PubMed:9463366}.
CC -!- INTERACTION:
CC Q9BRB3; O94777: DPM2; NbExp=2; IntAct=EBI-2339260, EBI-9097061;
CC Q9BRB3; P37287: PIGA; NbExp=5; IntAct=EBI-2339260, EBI-26643054;
CC Q9BRB3; Q92535: PIGC; NbExp=4; IntAct=EBI-2339260, EBI-721918;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BRB3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRB3-2; Sequence=VSP_007281, VSP_007282;
CC Name=3;
CC IsoId=Q9BRB3-3; Sequence=VSP_007279, VSP_007280;
CC -!- DISEASE: Multiple congenital anomalies-hypotonia-seizures syndrome 4
CC (MCAHS4) [MIM:618548]: An autosomal recessive syndrome characterized by
CC onset of refractory seizures in the first months of life. Additional
CC clinical features include severe global developmental delay, dysmorphic
CC facial features, and skeletal, renal and ophthalmic anomalies. At the
CC cellular level, the disorder is caused by a defect in the synthesis of
CC glycosylphosphatidylinositol (GPI). {ECO:0000269|PubMed:24463883,
CC ECO:0000269|PubMed:25558065, ECO:0000269|PubMed:27513193,
CC ECO:0000269|PubMed:31148362}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PIGQ family. {ECO:0000305}.
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DR EMBL; AF030177; AAC32661.1; -; mRNA.
DR EMBL; AB003723; BAA24948.1; -; mRNA.
DR EMBL; AE006464; AAK61235.1; -; Genomic_DNA.
DR EMBL; Z98883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85796.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85797.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85799.1; -; Genomic_DNA.
DR EMBL; BC006377; AAH06377.1; -; mRNA.
DR EMBL; BC010094; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS10411.1; -. [Q9BRB3-1]
DR CCDS; CCDS10412.1; -. [Q9BRB3-2]
DR RefSeq; NP_004195.2; NM_004204.3. [Q9BRB3-2]
DR RefSeq; NP_683721.1; NM_148920.2. [Q9BRB3-1]
DR AlphaFoldDB; Q9BRB3; -.
DR BioGRID; 114545; 34.
DR ComplexPortal; CPX-6502; Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex.
DR CORUM; Q9BRB3; -.
DR IntAct; Q9BRB3; 19.
DR MINT; Q9BRB3; -.
DR STRING; 9606.ENSP00000026218; -.
DR iPTMnet; Q9BRB3; -.
DR PhosphoSitePlus; Q9BRB3; -.
DR BioMuta; PIGQ; -.
DR DMDM; 30173119; -.
DR EPD; Q9BRB3; -.
DR jPOST; Q9BRB3; -.
DR MassIVE; Q9BRB3; -.
DR MaxQB; Q9BRB3; -.
DR PaxDb; Q9BRB3; -.
DR PeptideAtlas; Q9BRB3; -.
DR PRIDE; Q9BRB3; -.
DR ProteomicsDB; 78753; -. [Q9BRB3-1]
DR ProteomicsDB; 78754; -. [Q9BRB3-2]
DR ProteomicsDB; 78755; -. [Q9BRB3-3]
DR Antibodypedia; 22728; 86 antibodies from 22 providers.
DR DNASU; 9091; -.
DR Ensembl; ENST00000026218.9; ENSP00000026218.5; ENSG00000007541.17. [Q9BRB3-1]
DR Ensembl; ENST00000321878.10; ENSP00000326674.6; ENSG00000007541.17. [Q9BRB3-2]
DR Ensembl; ENST00000409527.6; ENSP00000386760.2; ENSG00000007541.17. [Q9BRB3-2]
DR Ensembl; ENST00000470411.2; ENSP00000439650.1; ENSG00000007541.17. [Q9BRB3-3]
DR GeneID; 9091; -.
DR KEGG; hsa:9091; -.
DR MANE-Select; ENST00000321878.10; ENSP00000326674.6; NM_004204.5; NP_004195.2. [Q9BRB3-2]
DR UCSC; uc002chm.4; human. [Q9BRB3-1]
DR CTD; 9091; -.
DR DisGeNET; 9091; -.
DR GeneCards; PIGQ; -.
DR HGNC; HGNC:14135; PIGQ.
DR HPA; ENSG00000007541; Low tissue specificity.
DR MalaCards; PIGQ; -.
DR MIM; 605754; gene.
DR MIM; 618548; phenotype.
DR neXtProt; NX_Q9BRB3; -.
DR OpenTargets; ENSG00000007541; -.
DR Orphanet; 1934; Early infantile epileptic encephalopathy.
DR PharmGKB; PA33299; -.
DR VEuPathDB; HostDB:ENSG00000007541; -.
DR eggNOG; KOG1183; Eukaryota.
DR GeneTree; ENSGT00390000004994; -.
DR HOGENOM; CLU_021157_2_0_1; -.
DR InParanoid; Q9BRB3; -.
DR OMA; GICRSRV; -.
DR OrthoDB; 1247641at2759; -.
DR PhylomeDB; Q9BRB3; -.
DR TreeFam; TF321258; -.
DR BRENDA; 2.4.1.198; 2681.
DR PathwayCommons; Q9BRB3; -.
DR Reactome; R-HSA-162710; Synthesis of glycosylphosphatidylinositol (GPI). [Q9BRB3-2]
DR SignaLink; Q9BRB3; -.
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 9091; 24 hits in 1075 CRISPR screens.
DR ChiTaRS; PIGQ; human.
DR GeneWiki; PIGQ; -.
DR GenomeRNAi; 9091; -.
DR Pharos; Q9BRB3; Tbio.
DR PRO; PR:Q9BRB3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BRB3; protein.
DR Bgee; ENSG00000007541; Expressed in right lobe of thyroid gland and 108 other tissues.
DR ExpressionAtlas; Q9BRB3; baseline and differential.
DR Genevisible; Q9BRB3; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR007720; PigQ/GPI1.
DR PANTHER; PTHR21329; PTHR21329; 1.
DR Pfam; PF05024; Gpi1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disease variant; Epilepsy;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10944123"
FT CHAIN 2..760
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit Q"
FT /id="PRO_0000215664"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 696..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 275..299
FT /note="KANTVASVLLDVALGLMLLSWLHGR -> CGPALVSAGLGACPLAPSPSPSA
FT PR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007279"
FT VAR_SEQ 300..760
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007280"
FT VAR_SEQ 511..581
FT /note="DKPTALQPRGAHLPPPQLWLPPQALLGRPVPQAVPWGAHLPLEAERGQAGLR
FT ELLARLAPPHGHSQPSALP -> AGVKFRVLRHEAGRPLRLLMQINPLPYSRVVHTYRL
FT PSCGCHPKHSWGALCRKLFLGELIYPWRQRGDKQD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9463366,
FT ECO:0000303|PubMed:9729469"
FT /id="VSP_007281"
FT VAR_SEQ 582..760
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9463366,
FT ECO:0000303|PubMed:9729469"
FT /id="VSP_007282"
FT VARIANT 14
FT /note="T -> A (in dbSNP:rs2071979)"
FT /evidence="ECO:0000269|PubMed:11157797,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_015596"
FT VARIANT 207..760
FT /note="Missing (in MCAHS4)"
FT /evidence="ECO:0000269|PubMed:25558065"
FT /id="VAR_083110"
FT VARIANT 400
FT /note="Missing (in MCAHS4)"
FT /evidence="ECO:0000269|PubMed:27513193,
FT ECO:0000269|PubMed:31148362"
FT /id="VAR_083111"
FT VARIANT 592
FT /note="C -> R (in dbSNP:rs1045277)"
FT /id="VAR_053579"
FT VARIANT 668
FT /note="C -> R (in dbSNP:rs710924)"
FT /id="VAR_053580"
FT VARIANT 668
FT /note="C -> Y (in dbSNP:rs710925)"
FT /id="VAR_053581"
SQ SEQUENCE 760 AA; 84082 MW; DBF900ADCE08DA98 CRC64;
MVLKAFFPTC CVSTDSGLLV GRWVPEQSSA VVLAVLHFPF IPIQVKQLLA QVRQASQVGV
AVLGTWCHCR QEPEESLGRF LESLGAVFPH EPWLRLCRER GGTFWSCEAT HRQAPTAPGA
PGEDQVMLIF YDQRQVLLSQ LHLPTVLPDR QAGATTASTG GLAAVFDTVA RSEVLFRSDR
FDEGPVRLSH WQSEGVEASI LAELARRASG PICLLLASLL SLVSAVSACR VFKLWPLSFL
GSKLSTCEQL RHRLEHLTLI FSTRKAENPA QLMRKANTVA SVLLDVALGL MLLSWLHGRS
RIGHLADALV PVADHVAEEL QHLLQWLMGA PAGLKMNRAL DQVLGRFFLY HIHLWISYIH
LMSPFVEHIL WHVGLSACLG LTVALSLLSD IIALLTFHIY CFYVYGARLY CLKIHGLSSL
WRLFRGKKWN VLRQRVDSCS YDLDQLFIGT LLFTILLFLL PTTALYYLVF TLLRLLVVAV
QGLIHLLVDL INSLPLYSLG LRLCRPYRLA DKPTALQPRG AHLPPPQLWL PPQALLGRPV
PQAVPWGAHL PLEAERGQAG LRELLARLAP PHGHSQPSAL PGWHQLSWRM SCALWTLLCA
PEHGRPCYHT LGLEVIGSEQ MWGWPARLAA LHHWHCLPWD PLPTCCGHHG GEHSNPRCPE
HCPMPTLCTQ VQRVRPPQQP QVEGWSPWGL PSGSALAVGV EGPCQDEPPS PRHPLAPSAE
QHPASGGLKQ SLTPVPSGPG PSLPEPHGVY LRMFPGEVAL
