ABHGA_MOUSE
ID ABHGA_MOUSE Reviewed; 558 AA.
AC Q9Z1Q2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphatidylserine lipase ABHD16A {ECO:0000305};
DE EC=3.1.-.- {ECO:0000269|PubMed:25580854};
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 16A {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 16A {ECO:0000305};
DE AltName: Full=HLA-B-associated transcript 5 {ECO:0000303|PubMed:25290914};
DE Short=mBAT5 {ECO:0000303|PubMed:25290914};
DE AltName: Full=Monoacylglycerol lipase ABHD16A {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000269|PubMed:25290914};
GN Name=Abhd16a {ECO:0000312|MGI:MGI:99476};
GN Synonyms=Bat5 {ECO:0000303|PubMed:25290914}, Ng26;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PROTEIN SEQUENCE OF 418-426, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25290914; DOI=10.1371/journal.pone.0109869;
RA Savinainen J.R., Patel J.Z., Parkkari T., Navia-Paldanius D.,
RA Marjamaa J.J., Laitinen T., Nevalainen T., Laitinen J.T.;
RT "Biochemical and pharmacological characterization of the human lymphocyte
RT antigen B-associated transcript 5 (BAT5/ABHD16A).";
RL PLoS ONE 9:E109869-E109869(2014).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25580854; DOI=10.1038/nchembio.1721;
RA Kamat S.S., Camara K., Parsons W.H., Chen D.H., Dix M.M., Bird T.D.,
RA Howell A.R., Cravatt B.F.;
RT "Immunomodulatory lysophosphatidylserines are regulated by ABHD16A and
RT ABHD12 interplay.";
RL Nat. Chem. Biol. 11:164-171(2015).
CC -!- FUNCTION: Phosphatidylserine (PS) lipase that mediates the hydrolysis
CC of phosphatidylserine to generate lysophosphatidylserine (LPS)
CC (PubMed:25580854). LPS constitutes a class of signaling lipids that
CC regulates immunological and neurological processes (PubMed:25580854).
CC Has no activity towards diacylglycerol, triacylglycerol or
CC lysophosphatidylserine lipase (By similarity). Also has
CC monoacylglycerol lipase activity, with preference for 1-(9Z,12Z-
CC octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-Delta(12,14)-
CC prostaglandin J2 (15d-PGJ(2)-G) (PubMed:25290914).
CC {ECO:0000250|UniProtKB:O95870, ECO:0000269|PubMed:25290914,
CC ECO:0000269|PubMed:25580854}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoserine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC heptadecanoyl-sn-glycero-3-phosphoserine + H(+);
CC Xref=Rhea:RHEA:44500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:84461, ChEBI:CHEBI:84462;
CC Evidence={ECO:0000269|PubMed:25580854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44501;
CC Evidence={ECO:0000269|PubMed:25580854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:75029; Evidence={ECO:0000269|PubMed:25580854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41753;
CC Evidence={ECO:0000269|PubMed:25580854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoserine + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-
CC glycero-3-phosphoserine + H(+); Xref=Rhea:RHEA:44516,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:84466, ChEBI:CHEBI:84467;
CC Evidence={ECO:0000269|PubMed:25580854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44517;
CC Evidence={ECO:0000269|PubMed:25580854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC heptadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:44520, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:74340, ChEBI:CHEBI:84470;
CC Evidence={ECO:0000269|PubMed:25580854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44521;
CC Evidence={ECO:0000269|PubMed:25580854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472,
CC ChEBI:CHEBI:84475; Evidence={ECO:0000269|PubMed:25580854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000269|PubMed:25580854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-
CC myo-inositol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1D-myo-inositol) + H(+); Xref=Rhea:RHEA:44528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72833, ChEBI:CHEBI:72837;
CC Evidence={ECO:0000269|PubMed:25580854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44529;
CC Evidence={ECO:0000269|PubMed:25580854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC heptadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:44540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:84489, ChEBI:CHEBI:84490;
CC Evidence={ECO:0000269|PubMed:25580854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44541;
CC Evidence={ECO:0000269|PubMed:25580854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000269|PubMed:25580854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000269|PubMed:25580854};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75457;
CC Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612;
CC Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin D2-1-glycerol ester = glycerol + H(+) +
CC prostaglandin D2; Xref=Rhea:RHEA:45412, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57406,
CC ChEBI:CHEBI:85232; Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-oxo-5Z,9,12E,14E-prostatetraenoate + H2O = 15-deoxy-
CC Delta(12,14)-prostaglandin J2 + glycerol + H(+);
CC Xref=Rhea:RHEA:45416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:85236, ChEBI:CHEBI:85238;
CC Evidence={ECO:0000269|PubMed:25290914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45417;
CC Evidence={ECO:0000269|PubMed:25290914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75568;
CC Evidence={ECO:0000269|PubMed:25290914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48429;
CC Evidence={ECO:0000269|PubMed:25290914};
CC -!- ACTIVITY REGULATION: Specifically inhibited by alpha-alkylidene-beta-
CC lactone KC01 ((Z)-6-(2-Oxo-4-tridecyloxetan-3-ylidene)hexanamide).
CC {ECO:0000269|PubMed:25580854}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoserine {ECO:0000269|PubMed:25580854};
CC Vmax=35 nmol/min/mg enzyme with 1-octadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphoserine as substrate
CC {ECO:0000269|PubMed:25580854};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:25580854}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mice were born at a much lower frequency than
CC expected and are smaller than wild-type mice throughout development and
CC life (PubMed:25580854). Despite their smaller size, mice appear normal
CC (PubMed:25580854). Metabolomic characterization of brain tissue show
CC decreased lysophosphatidylserines (PubMed:25580854).
CC {ECO:0000269|PubMed:25580854}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD16 family.
CC {ECO:0000305}.
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DR EMBL; AF109905; AAC84159.1; -; Genomic_DNA.
DR EMBL; BC029114; AAH29114.1; -; mRNA.
DR CCDS; CCDS28681.1; -.
DR RefSeq; NP_848707.1; NM_178592.3.
DR AlphaFoldDB; Q9Z1Q2; -.
DR SMR; Q9Z1Q2; -.
DR BioGRID; 228757; 4.
DR STRING; 10090.ENSMUSP00000007251; -.
DR ChEMBL; CHEMBL5184; -.
DR SwissLipids; SLP:000001040; -.
DR ESTHER; mouse-Abhd16a; ABHD16.
DR MEROPS; S09.022; -.
DR iPTMnet; Q9Z1Q2; -.
DR PhosphoSitePlus; Q9Z1Q2; -.
DR SwissPalm; Q9Z1Q2; -.
DR CPTAC; non-CPTAC-3683; -.
DR EPD; Q9Z1Q2; -.
DR MaxQB; Q9Z1Q2; -.
DR PaxDb; Q9Z1Q2; -.
DR PeptideAtlas; Q9Z1Q2; -.
DR PRIDE; Q9Z1Q2; -.
DR ProteomicsDB; 285829; -.
DR Antibodypedia; 27504; 96 antibodies from 19 providers.
DR DNASU; 193742; -.
DR Ensembl; ENSMUST00000007251; ENSMUSP00000007251; ENSMUSG00000007036.
DR GeneID; 193742; -.
DR KEGG; mmu:193742; -.
DR UCSC; uc008cfq.1; mouse.
DR CTD; 7920; -.
DR MGI; MGI:99476; Abhd16a.
DR VEuPathDB; HostDB:ENSMUSG00000007036; -.
DR eggNOG; KOG1553; Eukaryota.
DR GeneTree; ENSGT00940000160908; -.
DR HOGENOM; CLU_040705_2_0_1; -.
DR InParanoid; Q9Z1Q2; -.
DR OMA; THCTQLP; -.
DR OrthoDB; 580247at2759; -.
DR PhylomeDB; Q9Z1Q2; -.
DR TreeFam; TF314267; -.
DR BioGRID-ORCS; 193742; 5 hits in 71 CRISPR screens.
DR PRO; PR:Q9Z1Q2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z1Q2; protein.
DR Bgee; ENSMUSG00000007036; Expressed in cerebellar cortex and 260 other tissues.
DR ExpressionAtlas; Q9Z1Q2; baseline and differential.
DR Genevisible; Q9Z1Q2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0006660; P:phosphatidylserine catabolic process; IDA:UniProtKB.
DR GO; GO:1905344; P:prostaglandin catabolic process; IDA:BHF-UCL.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR026604; ABHD16A.
DR PANTHER; PTHR12277:SF54; PTHR12277:SF54; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..558
FT /note="Phosphatidylserine lipase ABHD16A"
FT /id="PRO_0000064834"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25580854"
FT DOMAIN 281..406
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 355
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 430
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 507
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
SQ SEQUENCE 558 AA; 63086 MW; 2DF1890F79E2EE63 CRC64;
MAKLLSCVLG PRLYKIYRER DTDRAASSVP ETPTAVPAAS SSSWDTYYQP RALEKHADSI
LALASVFWSI SYYSSPFAFF YLYRKGYLSL SKVVPFSHYA GTLLLLLAGV ACLRGIGRWT
NPQYRQFITI LEATHRNQSA ENKRQLANYN FDFRSWPVDF HWEEPSSRKG SRGGPSRRGV
ALLRPEPLHR GTADTFLNRV KKLPCQITSY LVAHTLGRRM LYPGSVYLLQ KALMPVLLQG
QARLVEECNG RRAKLLACDG NEIDTMFVDR RGTAEPQGQK LVICCEGNAG FYEVGCVSTP
LEAGYSVLGW NHPGFAGSTG VPFPQNEANA MDVVVQFAIH RLGFQPQDIV IYAWSIGGFT
ATWAAMSYPD ISAVILDASF DDLVPLALKV MPDSWRALVT RTVRQHLNLN NSEQLCRFQG
PVLLVRRTKD EIITTTVPED IMSNRGNDLL LKLLQFRYPR VMVEEGLRAV RQWLEASSQL
EEASIYSRWE VEEDWCVSVL RSYQAEHGPD FPWSVGEDMS ADGRRQLALF LARKHLHNFE
ATHCTPLPAQ HFQMPWHL
