NAAA_MOUSE
ID NAAA_MOUSE Reviewed; 362 AA.
AC Q9D7V9; Q5KTC6; Q99KM3; Q9D6B4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=N-acylethanolamine-hydrolyzing acid amidase {ECO:0000305};
DE EC=3.5.1.60 {ECO:0000250|UniProtKB:Q5KTC7};
DE AltName: Full=Acylsphingosine deacylase NAAA {ECO:0000250|UniProtKB:Q5KTC7};
DE EC=3.5.1.23 {ECO:0000250|UniProtKB:Q5KTC7};
DE AltName: Full=N-acylsphingosine amidohydrolase-like;
DE Short=ASAH-like protein;
DE Contains:
DE RecName: Full=N-acylethanolamine-hydrolyzing acid amidase subunit alpha;
DE Contains:
DE RecName: Full=N-acylethanolamine-hydrolyzing acid amidase subunit beta;
DE Flags: Precursor;
GN Name=Naaa {ECO:0000303|PubMed:30301806, ECO:0000312|MGI:MGI:1914361};
GN Synonyms=Asahl;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=15655246; DOI=10.1074/jbc.m413473200;
RA Tsuboi K., Sun Y.-X., Okamoto Y., Araki N., Tonai T., Ueda N.;
RT "Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase,
RT a novel member of the choloylglycine hydrolase family with structural and
RT functional similarity to acid ceramidase.";
RL J. Biol. Chem. 280:11082-11092(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, Placenta, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, 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] {ECO:0007744|PDB:6DXY}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-126 AND 127-358 OF MUTANT
RP SER-112/SER-338, SUBUNIT, PROTEOLYTIC CLEAVAGE, GLYCOSYLATION AT ASN-42 AND
RP ASN-314, AND MUTAGENESIS OF ASN-112 AND ASN-338.
RX PubMed=30301806; DOI=10.1073/pnas.1811759115;
RA Gorelik A., Gebai A., Illes K., Piomelli D., Nagar B.;
RT "Molecular mechanism of activation of the immunoregulatory amidase NAAA.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E10032-E10040(2018).
CC -!- FUNCTION: Degrades bioactive fatty acid amides to their corresponding
CC acids, with the following preference: N-palmitoylethanolamine > N-
CC myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine >
CC N-linoleoylethanolamine > N-arachidonoylethanolamine.
CC {ECO:0000250|UniProtKB:Q5KTC7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine +
CC hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(long-chain fatty acyl)ethanolamine = a long-chain
CC fatty acid + ethanolamine; Xref=Rhea:RHEA:17505, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15897, ChEBI:CHEBI:57560, ChEBI:CHEBI:57603; EC=3.5.1.60;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17506;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine;
CC Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:85263;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetradecanoylethanolamine = ethanolamine +
CC tetradecanoate; Xref=Rhea:RHEA:45452, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57603, ChEBI:CHEBI:85262;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45453;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine;
CC Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72959;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72956;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292;
CC Evidence={ECO:0000250|UniProtKB:Q02083};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:Q02083}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit, produced by
CC autocatalytic cleavage. {ECO:0000269|PubMed:30301806}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q02083}. Membrane
CC {ECO:0000250|UniProtKB:Q02083}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q02083}.
CC -!- PTM: N-glycosylated (PubMed:30301806). Tunicamycin treatment causes a
CC reduction in specific activity against N-palmitoylethanolamine (By
CC similarity). {ECO:0000250|UniProtKB:Q02083,
CC ECO:0000269|PubMed:30301806}.
CC -!- PTM: Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and
CC beta subunit (PubMed:30301806). Cleavage gives rise to a conformation
CC change that activates the enzyme. The same catalytic Cys residue
CC mediates the autoproteolytic cleavage and subsequent hydrolysis of
CC lipid substrates (By similarity). {ECO:0000250|UniProtKB:Q02083,
CC ECO:0000269|PubMed:30301806}.
CC -!- SIMILARITY: Belongs to the acid ceramidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29350.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB162194; BAD88530.1; -; mRNA.
DR EMBL; AK008776; BAB25888.1; -; mRNA.
DR EMBL; AK014438; BAB29350.2; ALT_SEQ; mRNA.
DR EMBL; BC004572; AAH04572.1; -; mRNA.
DR CCDS; CCDS19428.1; -.
DR RefSeq; NP_001157159.1; NM_001163687.1.
DR RefSeq; NP_080248.2; NM_025972.4.
DR PDB; 6DXY; X-ray; 1.85 A; A/C=31-126, B/D=127-358.
DR PDBsum; 6DXY; -.
DR AlphaFoldDB; Q9D7V9; -.
DR SMR; Q9D7V9; -.
DR IntAct; Q9D7V9; 1.
DR STRING; 10090.ENSMUSP00000108726; -.
DR MEROPS; C89.002; -.
DR GlyGen; Q9D7V9; 4 sites.
DR iPTMnet; Q9D7V9; -.
DR PhosphoSitePlus; Q9D7V9; -.
DR EPD; Q9D7V9; -.
DR MaxQB; Q9D7V9; -.
DR PaxDb; Q9D7V9; -.
DR PRIDE; Q9D7V9; -.
DR ProteomicsDB; 287556; -.
DR Antibodypedia; 24722; 193 antibodies from 25 providers.
DR DNASU; 67111; -.
DR Ensembl; ENSMUST00000113102; ENSMUSP00000108726; ENSMUSG00000029413.
DR GeneID; 67111; -.
DR KEGG; mmu:67111; -.
DR UCSC; uc008ycq.2; mouse.
DR CTD; 27163; -.
DR MGI; MGI:1914361; Naaa.
DR VEuPathDB; HostDB:ENSMUSG00000029413; -.
DR eggNOG; ENOG502QT7H; Eukaryota.
DR GeneTree; ENSGT00530000063548; -.
DR InParanoid; Q9D7V9; -.
DR OMA; GQDHINM; -.
DR OrthoDB; 745108at2759; -.
DR PhylomeDB; Q9D7V9; -.
DR TreeFam; TF313219; -.
DR BRENDA; 3.5.1.4; 3474.
DR BRENDA; 3.5.1.60; 3474.
DR Reactome; R-MMU-112310; Neurotransmitter release cycle.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 67111; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Naaa; mouse.
DR PRO; PR:Q9D7V9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D7V9; protein.
DR Bgee; ENSMUSG00000029413; Expressed in ventricular system choroidal fissure and 201 other tissues.
DR ExpressionAtlas; Q9D7V9; baseline and differential.
DR Genevisible; Q9D7V9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0017064; F:fatty acid amide hydrolase activity; ISS:UniProtKB.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; ISO:MGI.
DR GO; GO:0047412; F:N-(long-chain-acyl)ethanolamine deacylase activity; ISS:UniProtKB.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0006670; P:sphingosine metabolic process; ISS:UniProtKB.
DR InterPro; IPR016699; Acid_ceramidase-like.
DR InterPro; IPR029130; Acid_ceramidase_N.
DR InterPro; IPR029132; CBAH/NAAA_C.
DR Pfam; PF02275; CBAH; 1.
DR Pfam; PF15508; NAAA-beta; 1.
DR PIRSF; PIRSF017632; Acid_ceramidase-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Fatty acid metabolism; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Lysosome; Membrane;
KW Reference proteome; Signal; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000250"
FT CHAIN 34..362
FT /note="N-acylethanolamine-hydrolyzing acid amidase"
FT /id="PRO_0000002319"
FT CHAIN 34..130
FT /note="N-acylethanolamine-hydrolyzing acid amidase subunit
FT alpha"
FT /evidence="ECO:0000305|PubMed:30301806"
FT /id="PRO_0000419652"
FT CHAIN 131..362
FT /note="N-acylethanolamine-hydrolyzing acid amidase subunit
FT beta"
FT /evidence="ECO:0000305|PubMed:30301806"
FT /id="PRO_0000419653"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:30301806"
FT SITE 147
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q02083"
FT SITE 292
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q02083"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30301806,
FT ECO:0007744|PDB:6DXY"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30301806,
FT ECO:0007744|PDB:6DXY"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 112
FT /note="N->S: Loss of one glycosylation site."
FT /evidence="ECO:0000269|PubMed:30301806"
FT MUTAGEN 338
FT /note="N->S: Loss of one glycosylation site."
FT /evidence="ECO:0000269|PubMed:30301806"
FT CONFLICT 5
FT /note="A -> D (in Ref. 2; BAB25888)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="A -> V (in Ref. 3; AAH04572)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="H -> R (in Ref. 3; AAH04572)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="N -> D (in Ref. 3; AAH04572)"
FT /evidence="ECO:0000305"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6DXY"
FT TURN 49..53
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 62..76
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:6DXY"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:6DXY"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:6DXY"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:6DXY"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6DXY"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:6DXY"
SQ SEQUENCE 362 AA; 40075 MW; 49480CCA1630699F CRC64;
MGTLATRAAC HGAHLALALL LLLSLSGPWL SAVVPGTPPL FNVSLDAAPE QRWLPMLRHY
DPDFLRTAVA QVIGDRVPQW VLGMVGEIVS KVESFLPQPF TDEIRSICDS LNLSLADGIL
VNLAYEASAF CTSIVAQDSQ GHIYHGRNLD YPFGKILRKL TANVQFIKNG QIAFTGTTFV
GYVGLWTGQS PHKFTISGDE RDKGWWWENM IAALSLGHSP ISWLIRKTLS ESESFEAAVY
TLAKTPLIAD VYYIVGGTSP KEGVVITRDR GGPADIWPLD PLNGEWFRVE TNYDHWKPAP
KVDDRRTPAI KALNATGQAH LNLETLFQVL SLFPVYNNYT IYTTVMSAAE PDKYLTMIRN
PS
