ABHD4_HUMAN
ID ABHD4_HUMAN Reviewed; 342 AA.
AC Q8TB40; B4DDH7; Q9H9E0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=(Lyso)-N-acylphosphatidylethanolamine lipase {ECO:0000305};
DE EC=3.1.1.-;
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 4 {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 4 {ECO:0000312|HGNC:HGNC:20154};
DE AltName: Full=Alpha/beta-hydrolase 4;
GN Name=ABHD4 {ECO:0000312|HGNC:HGNC:20154};
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] (ISOFORMS 1 AND 2).
RC TISSUE=Adrenal gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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).
CC -!- FUNCTION: Lysophospholipase selective for N-acyl
CC phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-
CC acyl ethanolamines, including the endocannabinoid anandamide by
CC hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl
CC phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl
CC ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine
CC biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated,
CC polyunsaturated N-acyl chains. Shows no significant activity towards
CC other lysophospholipids, including lysophosphatidylcholine,
CC lysophosphatidylethanolamine and lysophosphatidylserine.
CC {ECO:0000250|UniProtKB:Q8VD66}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a
CC fatty acid + H(+) + N,1-diacyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:62537, ChEBI:CHEBI:85216;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45461;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45384,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:85217, ChEBI:CHEBI:85226;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45385;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-octadecanoyl-sn-
CC glycero-3-phospho-ethanolamine; Xref=Rhea:RHEA:45388,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:85219, ChEBI:CHEBI:85227;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45389;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-eicosanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-eicosanoyl-sn-
CC glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:85221, ChEBI:CHEBI:85228;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45393;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45396,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:85222, ChEBI:CHEBI:85229;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45397;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-
CC sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:85223, ChEBI:CHEBI:85230;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45401;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(N-
CC hexadecanoyl)-serine + H2O = (9Z)-octadecenoate + 1-octadecanoyl-2-
CC hydroxy-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H(+);
CC Xref=Rhea:RHEA:55236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:138661, ChEBI:CHEBI:138662;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55237;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC N-hexadecanoyl-ethanolamine + H2O = (9Z)-octadecenoate + 1-O-(1Z-
CC octadecenyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H(+);
CC Xref=Rhea:RHEA:55240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:137009, ChEBI:CHEBI:138663;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55241;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a fatty
CC acid + H(+) + N-acyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:85216, ChEBI:CHEBI:85225;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45421;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- INTERACTION:
CC Q8TB40; Q9NWT8: AURKAIP1; NbExp=3; IntAct=EBI-7131019, EBI-448665;
CC Q8TB40; Q12982: BNIP2; NbExp=3; IntAct=EBI-7131019, EBI-752094;
CC Q8TB40; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-7131019, EBI-11522780;
CC Q8TB40; P29400-2: COL4A5; NbExp=3; IntAct=EBI-7131019, EBI-12211159;
CC Q8TB40; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-7131019, EBI-398977;
CC Q8TB40; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-7131019, EBI-12831978;
CC Q8TB40; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-7131019, EBI-12937691;
CC Q8TB40; P24593: IGFBP5; NbExp=3; IntAct=EBI-7131019, EBI-720480;
CC Q8TB40; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-7131019, EBI-8503746;
CC Q8TB40; O60664: PLIN3; NbExp=3; IntAct=EBI-7131019, EBI-725795;
CC Q8TB40; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-7131019, EBI-712367;
CC Q8TB40; Q00765: REEP5; NbExp=3; IntAct=EBI-7131019, EBI-1549827;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TB40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TB40-2; Sequence=VSP_056924, VSP_056925;
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Thr-291 is present instead of the conserved His which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; AK022878; BAB14289.1; -; mRNA.
DR EMBL; AK293198; BAG56738.1; -; mRNA.
DR EMBL; AL160314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024779; AAH24779.1; -; mRNA.
DR CCDS; CCDS9572.1; -. [Q8TB40-1]
DR RefSeq; NP_071343.2; NM_022060.2. [Q8TB40-1]
DR AlphaFoldDB; Q8TB40; -.
DR SMR; Q8TB40; -.
DR BioGRID; 121967; 15.
DR IntAct; Q8TB40; 15.
DR MINT; Q8TB40; -.
DR STRING; 9606.ENSP00000414558; -.
DR ESTHER; human-ABHD4; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.013; -.
DR iPTMnet; Q8TB40; -.
DR PhosphoSitePlus; Q8TB40; -.
DR BioMuta; ABHD4; -.
DR DMDM; 74762601; -.
DR EPD; Q8TB40; -.
DR jPOST; Q8TB40; -.
DR MassIVE; Q8TB40; -.
DR MaxQB; Q8TB40; -.
DR PaxDb; Q8TB40; -.
DR PeptideAtlas; Q8TB40; -.
DR PRIDE; Q8TB40; -.
DR ProteomicsDB; 3863; -.
DR ProteomicsDB; 73960; -. [Q8TB40-1]
DR Antibodypedia; 4; 231 antibodies from 31 providers.
DR DNASU; 63874; -.
DR Ensembl; ENST00000418446.6; ENSP00000388751.2; ENSG00000100439.11. [Q8TB40-2]
DR Ensembl; ENST00000428304.7; ENSP00000414558.2; ENSG00000100439.11. [Q8TB40-1]
DR GeneID; 63874; -.
DR KEGG; hsa:63874; -.
DR MANE-Select; ENST00000428304.7; ENSP00000414558.2; NM_022060.3; NP_071343.2.
DR UCSC; uc001wgm.4; human. [Q8TB40-1]
DR CTD; 63874; -.
DR GeneCards; ABHD4; -.
DR HGNC; HGNC:20154; ABHD4.
DR HPA; ENSG00000100439; Low tissue specificity.
DR MIM; 619728; gene.
DR neXtProt; NX_Q8TB40; -.
DR OpenTargets; ENSG00000100439; -.
DR PharmGKB; PA128394705; -.
DR VEuPathDB; HostDB:ENSG00000100439; -.
DR eggNOG; KOG4409; Eukaryota.
DR GeneTree; ENSGT00390000016277; -.
DR HOGENOM; CLU_017361_0_0_1; -.
DR InParanoid; Q8TB40; -.
DR OMA; SFSFGWA; -.
DR OrthoDB; 1555935at2759; -.
DR PhylomeDB; Q8TB40; -.
DR TreeFam; TF314196; -.
DR BioCyc; MetaCyc:ENSG00000100439-MON; -.
DR PathwayCommons; Q8TB40; -.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR SignaLink; Q8TB40; -.
DR BioGRID-ORCS; 63874; 6 hits in 1077 CRISPR screens.
DR ChiTaRS; ABHD4; human.
DR GenomeRNAi; 63874; -.
DR Pharos; Q8TB40; Tbio.
DR PRO; PR:Q8TB40; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8TB40; protein.
DR Bgee; ENSG00000100439; Expressed in lower esophagus mucosa and 159 other tissues.
DR ExpressionAtlas; Q8TB40; baseline and differential.
DR Genevisible; Q8TB40; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; TAS:Reactome.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..342
FT /note="(Lyso)-N-acylphosphatidylethanolamine lipase"
FT /id="PRO_0000080864"
FT DOMAIN 70..201
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT VAR_SEQ 163..181
FT /note="VKHLILVDPWGFPLRPTNP -> AWSGAAIPAGLQTQVCRLL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056924"
FT VAR_SEQ 182..342
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056925"
FT CONFLICT 183..185
FT /note="EIR -> GIC (in Ref. 1; BAB14289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38794 MW; 867EA9E0092559CB CRC64;
MADDLEQQSQ GWLSSWLPTW RPTSMSQLKN VEARILQCLQ NKFLARYVSL PNQNKIWTVT
VSPEQNDRTP LVMVHGFGGG VGLWILNMDS LSARRTLHTF DLLGFGRSSR PAFPRDPEGA
EDEFVTSIET WRETMGIPSM ILLGHSLGGF LATSYSIKYP DRVKHLILVD PWGFPLRPTN
PSEIRAPPAW VKAVASVLGR SNPLAVLRVA GPWGPGLVQR FRPDFKRKFA DFFEDDTISE
YIYHCNAQNP SGETAFKAMM ESFGWARRPM LERIHLIRKD VPITMIYGSD TWIDTSTGKK
VKMQRPDSYV RDMEIKGASH HVYADQPHIF NAVVEEICDS VD
