PAFA2_HUMAN
ID PAFA2_HUMAN Reviewed; 392 AA.
AC Q99487; D3DPK1; O15458; Q5SY02;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Platelet-activating factor acetylhydrolase 2, cytoplasmic {ECO:0000303|PubMed:8955149};
DE EC=3.1.1.47 {ECO:0000269|PubMed:9494101};
DE AltName: Full=PAF:lysophospholipid transacetylase {ECO:0000250|UniProtKB:P83006};
DE AltName: Full=PAF:sphingosine transacetylase {ECO:0000250|UniProtKB:P83006};
DE AltName: Full=Platelet-activating factor acetyltransferase PAFAH2 {ECO:0000250|UniProtKB:P83006};
DE EC=2.3.1.149 {ECO:0000250|UniProtKB:P83006};
DE AltName: Full=Serine-dependent phospholipase A2 {ECO:0000303|PubMed:9494101};
DE Short=SD-PLA2 {ECO:0000305};
DE Short=hSD-PLA2 {ECO:0000303|PubMed:9494101};
GN Name=PAFAH2 {ECO:0000312|HGNC:HGNC:8579};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8955149; DOI=10.1074/jbc.271.51.33032;
RA Hattori K., Adachi H., Matsuzawa A., Yamamoto K., Tsujimoto M., Aoki J.,
RA Hattori M., Arai H., Inoue K.;
RT "cDNA cloning and expression of intracellular platelet-activating factor
RT (PAF) acetylhydrolase II. Its homology with plasma PAF acetylhydrolase.";
RL J. Biol. Chem. 271:33032-33038(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Prostate;
RX PubMed=9494101; DOI=10.1042/bj3301309;
RA Rice S.Q.J., Southan C., Boyd H.F., Terrett J.A., Macphee C.H., Moores K.,
RA Gloger I.S., Tew D.G.;
RT "Expression, purification and characterization of a human serine-dependent
RT phospholipase A2 with high specificity for oxidized phospholipids and
RT platelet activating factor.";
RL Biochem. J. 330:1309-1315(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 MRNA].
RC TISSUE=Eye;
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 REVIEW.
RX PubMed=9218411; DOI=10.1074/jbc.272.29.17895;
RA Stafforini D.M., McIntyre T.M., Zimmerman G.A., Prescott S.M.;
RT "Platelet-activating factor acetylhydrolases.";
RL J. Biol. Chem. 272:17895-17898(1997).
CC -!- FUNCTION: Catalyzes the hydrolyze of the acetyl group at the sn-2
CC position of platelet-activating factor (PAF) and its analogs, leading
CC to their inactivation (PubMed:9494101). Hydrolyzes propionyl and
CC butyroyl moieties approximately half as effectively as PAF (By
CC similarity). Also catalyzes transacetylation of the acetyl group from
CC platelet-activating factor (PAF) to lysoplasmalogen and to sphingosine,
CC producing plasmalogen analogs of PAF and N-acetylsphingosine (C2-
CC ceramide) respectively. Has a marked selectivity for phospholipids with
CC short acyl chains at the sn-2 position (By similarity).
CC {ECO:0000250|UniProtKB:P79106, ECO:0000250|UniProtKB:P83006,
CC ECO:0000269|PubMed:9494101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000269|PubMed:9494101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000269|PubMed:9494101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000250|UniProtKB:P83006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + 1-O-
CC hexadecyl-2-acetyl-sn-glycero-3-phosphocholine = 1-O-(1Z-alkenyl)-2-
CC acetyl-sn-glycero-3-phosphoethanolamine + 1-O-hexadecyl-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:41396, ChEBI:CHEBI:44811,
CC ChEBI:CHEBI:64496, ChEBI:CHEBI:77288, ChEBI:CHEBI:78419;
CC Evidence={ECO:0000250|UniProtKB:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41397;
CC Evidence={ECO:0000250|UniProtKB:P83006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + sphing-4-
CC enine = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + N-
CC (acetyl)-sphing-4-enine; Xref=Rhea:RHEA:41408, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:44811, ChEBI:CHEBI:46979, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41409;
CC Evidence={ECO:0000250|UniProtKB:P83006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-organyl-2-lyso-sn-glycero-3-phospholipid + a 1-O-alkyl-2-
CC acetyl-sn-glycero-3-phosphocholine = 1-O-alkyl-sn-glycero-3-
CC phosphocholine + 1-organyl-2-acetyl-sn-glycero-3-phospholipid;
CC Xref=Rhea:RHEA:11048, ChEBI:CHEBI:685, ChEBI:CHEBI:30909,
CC ChEBI:CHEBI:36707, ChEBI:CHEBI:76590; EC=2.3.1.149;
CC Evidence={ECO:0000250|UniProtKB:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11049;
CC Evidence={ECO:0000250|UniProtKB:P83006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-glutaryl-sn-glycero-3-phosphocholine + H2O =
CC 1-O-hexadecyl-sn-glycero-3-phosphocholine + glutarate + H(+);
CC Xref=Rhea:RHEA:41700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30921, ChEBI:CHEBI:64496, ChEBI:CHEBI:78371;
CC Evidence={ECO:0000250|UniProtKB:P79106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41701;
CC Evidence={ECO:0000250|UniProtKB:P79106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-succinyl-sn-glycero-3-phosphocholine + H2O =
CC 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + succinate;
CC Xref=Rhea:RHEA:41696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:64496, ChEBI:CHEBI:78369;
CC Evidence={ECO:0000250|UniProtKB:P79106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41697;
CC Evidence={ECO:0000250|UniProtKB:P79106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-butanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-O-hexadecyl-sn-glycero-3-phosphocholine + butanoate + H(+);
CC Xref=Rhea:RHEA:41692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17968, ChEBI:CHEBI:64496, ChEBI:CHEBI:78368;
CC Evidence={ECO:0000250|UniProtKB:P79106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41693;
CC Evidence={ECO:0000250|UniProtKB:P79106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-propanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + propanoate;
CC Xref=Rhea:RHEA:41688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17272, ChEBI:CHEBI:64496, ChEBI:CHEBI:78367;
CC Evidence={ECO:0000250|UniProtKB:P79106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41689;
CC Evidence={ECO:0000250|UniProtKB:P79106};
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride,
CC 3,4,dichloroisocoumarin, diisopropyl fluorophosphate (DFP) and diethyl
CC p-nitrophenyl phosphate (DENP). {ECO:0000269|PubMed:9494101}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42 uM for 2-O-acetyl-1-O-hexadecyl-sn-glycero-3-phosphocholine
CC (PAF) {ECO:0000269|PubMed:9494101};
CC KM=10 uM for 1-decanoyl-2-(4-nitrophenylglutaryl) phosphate (DNGP)
CC {ECO:0000269|PubMed:9494101};
CC Vmax=35 umol/min/mg enzyme with 2-O-acetyl-1-O-hexadecyl-sn-glycero-
CC 3-phosphocholine (PAF) as substrate {ECO:0000269|PubMed:9494101};
CC Vmax=1.7 umol/min/mg enzyme with 1-decanoyl-2-(4-nitrophenylglutaryl)
CC phosphate (DNGP) as substrate {ECO:0000269|PubMed:9494101};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:9494101}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9494101}. Membrane
CC {ECO:0000250|UniProtKB:P79106}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P79106}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P79106}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P79106}. Note=In resting cells, localizes to
CC intracellular membranes and cytoplasm. Translocates from the cytoplasm
CC to intracellular membranes upon oxidative stress.
CC {ECO:0000250|UniProtKB:P79106}.
CC -!- TISSUE SPECIFICITY: Broadly expressed in different tissues, but high in
CC B- and T-lymphocytes. In brain, expression is restricted to amygdala
CC and frontal cortex. {ECO:0000269|PubMed:8955149,
CC ECO:0000269|PubMed:9494101}.
CC -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}.
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DR EMBL; D87845; BAA13468.1; -; mRNA.
DR EMBL; U89386; AAC39707.1; -; mRNA.
DR EMBL; AL592064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07852.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07853.1; -; Genomic_DNA.
DR EMBL; BC001158; AAH01158.1; -; mRNA.
DR CCDS; CCDS270.1; -.
DR RefSeq; NP_000428.2; NM_000437.3.
DR RefSeq; XP_006710733.1; XM_006710670.3.
DR AlphaFoldDB; Q99487; -.
DR SMR; Q99487; -.
DR BioGRID; 111088; 15.
DR STRING; 9606.ENSP00000363400; -.
DR ESTHER; human-PAFAH2; PAF-Acetylhydrolase.
DR iPTMnet; Q99487; -.
DR PhosphoSitePlus; Q99487; -.
DR SwissPalm; Q99487; -.
DR BioMuta; PAFAH2; -.
DR DMDM; 6647691; -.
DR EPD; Q99487; -.
DR jPOST; Q99487; -.
DR MassIVE; Q99487; -.
DR MaxQB; Q99487; -.
DR PaxDb; Q99487; -.
DR PeptideAtlas; Q99487; -.
DR PRIDE; Q99487; -.
DR ProteomicsDB; 78290; -.
DR Antibodypedia; 622; 143 antibodies from 22 providers.
DR DNASU; 5051; -.
DR Ensembl; ENST00000374282.8; ENSP00000363400.3; ENSG00000158006.14.
DR Ensembl; ENST00000374284.5; ENSP00000363402.1; ENSG00000158006.14.
DR GeneID; 5051; -.
DR KEGG; hsa:5051; -.
DR MANE-Select; ENST00000374282.8; ENSP00000363400.3; NM_000437.4; NP_000428.2.
DR UCSC; uc001bld.4; human.
DR CTD; 5051; -.
DR DisGeNET; 5051; -.
DR GeneCards; PAFAH2; -.
DR HGNC; HGNC:8579; PAFAH2.
DR HPA; ENSG00000158006; Tissue enhanced (lymphoid).
DR MIM; 602344; gene.
DR neXtProt; NX_Q99487; -.
DR OpenTargets; ENSG00000158006; -.
DR PharmGKB; PA32910; -.
DR VEuPathDB; HostDB:ENSG00000158006; -.
DR eggNOG; KOG3847; Eukaryota.
DR GeneTree; ENSGT00390000005233; -.
DR HOGENOM; CLU_022501_0_0_1; -.
DR InParanoid; Q99487; -.
DR OMA; GNWIGKF; -.
DR OrthoDB; 1189747at2759; -.
DR PhylomeDB; Q99487; -.
DR TreeFam; TF313831; -.
DR BRENDA; 3.1.1.47; 2681.
DR PathwayCommons; Q99487; -.
DR Reactome; R-HSA-418346; Platelet homeostasis.
DR BioGRID-ORCS; 5051; 17 hits in 1081 CRISPR screens.
DR ChiTaRS; PAFAH2; human.
DR GeneWiki; PAFAH2; -.
DR GenomeRNAi; 5051; -.
DR Pharos; Q99487; Tbio.
DR PRO; PR:Q99487; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99487; protein.
DR Bgee; ENSG00000158006; Expressed in body of pancreas and 130 other tissues.
DR ExpressionAtlas; Q99487; baseline and differential.
DR Genevisible; Q99487; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005065; PAF_acetylhydro-like.
DR InterPro; IPR016715; PAF_acetylhydro_eucaryote.
DR PANTHER; PTHR10272; PTHR10272; 1.
DR Pfam; PF03403; PAF-AH_p_II; 1.
DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lipoprotein; Membrane; Myristate; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..392
FT /note="Platelet-activating factor acetylhydrolase 2,
FT cytoplasmic"
FT /id="PRO_0000090383"
FT ACT_SITE 236
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P79106"
FT ACT_SITE 259
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 314
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P79106"
FT CONFLICT 212
FT /note="L -> F (in Ref. 2; AAC39707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 44036 MW; 690FB7E6F5B68317 CRC64;
MGVNQSVGFP PVTGPHLVGC GDVMEGQNLQ GSFFRLFYPC QKAEETMEQP LWIPRYEYCT
GLAEYLQFNK RCGGLLFNLA VGSCRLPVSW NGPFKTKDSG YPLIIFSHGL GAFRTLYSAF
CMELASRGFV VAVPEHRDRS AATTYFCKQA PEENQPTNES LQEEWIPFRR VEEGEKEFHV
RNPQVHQRVS ECLRVLKILQ EVTAGQTVFN ILPGGLDLMT LKGNIDMSRV AVMGHSFGGA
TAILALAKET QFRCAVALDA WMFPLERDFY PKARGPVFFI NTEKFQTMES VNLMKKICAQ
HEQSRIITVL GSVHRSQTDF AFVTGNLIGK FFSTETRGSL DPYEGQEVMV RAMLAFLQKH
LDLKEDYNQW NNLIEGIGPS LTPGAPHHLS SL
