GPAT1_HUMAN
ID GPAT1_HUMAN Reviewed; 828 AA.
AC Q9HCL2; Q5VW51; Q86TA3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 1, mitochondrial {ECO:0000305};
DE Short=GPAT-1;
DE EC=2.3.1.15 {ECO:0000269|PubMed:18238778};
DE Flags: Precursor;
GN Name=GPAM {ECO:0000312|HGNC:HGNC:24865}; Synonyms=GPAT1, KIAA1560;
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 [LARGE SCALE MRNA].
RC TISSUE=Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-828.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18238778; DOI=10.1074/jbc.m708151200;
RA Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E.,
RA Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E.,
RA Konrad R.J., Beigneux A.P., Young S.G., Cao G.;
RT "AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase.";
RL J. Biol. Chem. 283:10048-10057(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19075029; DOI=10.1194/jlr.m800567-jlr200;
RA Zhao Y., Chen Y.-Q., Li S., Konrad R.J., Cao G.;
RT "The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin
RT acyltransferase is an acyltransferase of multiple anionic
RT lysophospholipids.";
RL J. Lipid Res. 50:945-956(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of
CC glycerol-3-phosphate, an essential step in glycerolipids biosynthesis
CC such as triglycerides, phosphatidic acids and lysophosphatidic acids.
CC {ECO:0000269|PubMed:18238778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000269|PubMed:18238778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000305|PubMed:18238778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-
CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:74547;
CC Evidence={ECO:0000269|PubMed:18238778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC Evidence={ECO:0000305|PubMed:18238778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74544; Evidence={ECO:0000269|PubMed:18238778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000305|PubMed:18238778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37195,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74565; Evidence={ECO:0000269|PubMed:18238778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196;
CC Evidence={ECO:0000305|PubMed:18238778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:18238778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000305|PubMed:18238778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-
CC glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682;
CC Evidence={ECO:0000269|PubMed:18238778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC Evidence={ECO:0000305|PubMed:18238778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA =
CC 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA;
CC Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:64840;
CC Evidence={ECO:0000269|PubMed:19075029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC Evidence={ECO:0000269|PubMed:19075029};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000269|PubMed:18238778}.
CC -!- INTERACTION:
CC Q9HCL2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-7600236, EBI-7062247;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P97564}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97564}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; AL833093; CAD89932.1; -; mRNA.
DR EMBL; AL391986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB046780; BAB13386.1; -; mRNA.
DR CCDS; CCDS7570.1; -.
DR RefSeq; NP_001231878.1; NM_001244949.1.
DR RefSeq; NP_065969.3; NM_020918.5.
DR RefSeq; XP_005270055.1; XM_005269998.1.
DR AlphaFoldDB; Q9HCL2; -.
DR BioGRID; 121707; 34.
DR IntAct; Q9HCL2; 12.
DR MINT; Q9HCL2; -.
DR STRING; 9606.ENSP00000265276; -.
DR BindingDB; Q9HCL2; -.
DR ChEMBL; CHEMBL3734642; -.
DR SwissLipids; SLP:000000094; -.
DR iPTMnet; Q9HCL2; -.
DR PhosphoSitePlus; Q9HCL2; -.
DR BioMuta; GPAM; -.
DR DMDM; 59803040; -.
DR EPD; Q9HCL2; -.
DR jPOST; Q9HCL2; -.
DR MassIVE; Q9HCL2; -.
DR MaxQB; Q9HCL2; -.
DR PaxDb; Q9HCL2; -.
DR PeptideAtlas; Q9HCL2; -.
DR PRIDE; Q9HCL2; -.
DR ProteomicsDB; 81752; -.
DR Antibodypedia; 31772; 253 antibodies from 30 providers.
DR DNASU; 57678; -.
DR Ensembl; ENST00000348367.9; ENSP00000265276.4; ENSG00000119927.14.
DR GeneID; 57678; -.
DR KEGG; hsa:57678; -.
DR MANE-Select; ENST00000348367.9; ENSP00000265276.4; NM_001244949.2; NP_001231878.1.
DR UCSC; uc001kzp.4; human.
DR CTD; 57678; -.
DR DisGeNET; 57678; -.
DR GeneCards; GPAM; -.
DR HGNC; HGNC:24865; GPAM.
DR HPA; ENSG00000119927; Tissue enhanced (adipose tissue, liver).
DR MIM; 602395; gene.
DR neXtProt; NX_Q9HCL2; -.
DR OpenTargets; ENSG00000119927; -.
DR PharmGKB; PA134983031; -.
DR VEuPathDB; HostDB:ENSG00000119927; -.
DR eggNOG; KOG3729; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR InParanoid; Q9HCL2; -.
DR OMA; QSWEKFF; -.
DR OrthoDB; 198209at2759; -.
DR PhylomeDB; Q9HCL2; -.
DR TreeFam; TF313360; -.
DR BioCyc; MetaCyc:57678-MON; -.
DR BRENDA; 2.3.1.15; 2681.
DR PathwayCommons; Q9HCL2; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR Reactome; R-HSA-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; Q9HCL2; -.
DR UniPathway; UPA00557; UER00612.
DR BioGRID-ORCS; 57678; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; GPAM; human.
DR GeneWiki; GPAM; -.
DR GenomeRNAi; 57678; -.
DR Pharos; Q9HCL2; Tbio.
DR PRO; PR:Q9HCL2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9HCL2; protein.
DR Bgee; ENSG00000119927; Expressed in pericardium and 179 other tissues.
DR ExpressionAtlas; Q9HCL2; baseline and differential.
DR Genevisible; Q9HCL2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IMP:UniProtKB.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IEA:Ensembl.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..828
FT /note="Glycerol-3-phosphate acyltransferase 1,
FT mitochondrial"
FT /id="PRO_0000024690"
FT TOPO_DOM ?..471
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..828
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 435..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 230..235
FT /note="HXXXXD motif"
FT COMPBIAS 439..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97564"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT MOD_RES 784
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61586"
FT VARIANT 4
FT /note="S -> Y (in dbSNP:rs11549703)"
FT /id="VAR_050585"
FT VARIANT 43
FT /note="I -> V (in dbSNP:rs2792751)"
FT /id="VAR_050586"
FT VARIANT 131
FT /note="E -> G (in dbSNP:rs10787428)"
FT /id="VAR_050587"
FT VARIANT 386
FT /note="I -> T (in dbSNP:rs35019520)"
FT /id="VAR_050588"
FT CONFLICT 204
FT /note="I -> F (in Ref. 1; CAD89932)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="Q -> R (in Ref. 1; CAD89932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 828 AA; 93795 MW; 7AADD21BC8684693 CRC64;
MDESALTLGT IDVSYLPHSS EYSVGRCKHT SEEWGECGFR PTIFRSATLK WKESLMSRKR
PFVGRCCYSC TPQSWDKFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YVLFIQERDV
HKGMFATNVT ENVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAVNKVKKKA KRILQEMVAT
VSPAMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT
FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDV LYRALLHGHI
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS TNVIPDILII PVGISYDRII
EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGCVRVDF AQPFSLKEYL ESQSQKPVSA
LLSLEQALLP AILPSRPSDA ADEGRDTSIN ESRNATDESL RRRLIANLAE HILFTASKSC
AIMSTHIVAC LLLYRHRQGI DLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL
GNCVTITHTS RNDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSL YAVLNKRGLG
GPTSTPPNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF IQYGILTVAE
HDDQEDISPS LAEQQWDKKL PEPLSWRSDE EDEDSDFGEE QRDCYLKVSQ SKEHQQFITF
LQRLLGPLLE AYSSAAIFVH NFSGPVPEPE YLQKLHKYLI TRTERNVAVY AESATYCLVK
NAVKMFKDIG VFKETKQKRV SVLELSSTFL PQCNRQKLLE YILSFVVL
