ID PLAT1_HUMAN Reviewed; 168 AA. AC Q9HDD0; D2KX19; Q6X7C0; Q86WS9; X6R3D1; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 140. DE RecName: Full=Phospholipase A and acyltransferase 1 {ECO:0000312|HGNC:HGNC:14922}; DE EC=2.3.1.- {ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:27623847}; DE EC=3.1.1.32 {ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:27623847}; DE EC=3.1.1.4 {ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:27623847}; DE AltName: Full=HRAS-like suppressor 1; DE Short=HRSL1; DE AltName: Full=Phospholipid-metabolizing enzyme A-C1 {ECO:0000303|PubMed:21880860}; GN Name=PLAAT1 {ECO:0000312|HGNC:HGNC:14922}; Synonyms=HRASLS; 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] (ISOFORM 1). RA Kato S.; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RA Wu N., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.; RT "A new spermatogenesis-related gene."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), TISSUE RP SPECIFICITY (ISOFORM 1), AND CATALYTIC ACTIVITY (ISOFORM 1). RX PubMed=21880860; DOI=10.1194/jlr.m015081; RA Shinohara N., Uyama T., Jin X.H., Tsuboi K., Tonai T., Houchi H., Ueda N.; RT "Enzymological analysis of the tumor suppressor A-C1 reveals a novel group RT of phospholipid-metabolizing enzymes."; RL J. Lipid Res. 52:1927-1935(2011). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 [7] RP FUNCTION (ISOFORM 1), AND CATALYTIC ACTIVITY (ISOFORM 1). RX PubMed=22825852; DOI=10.1074/jbc.m112.368712; RA Uyama T., Ikematsu N., Inoue M., Shinohara N., Jin X.H., Tsuboi K., RA Tonai T., Tokumura A., Ueda N.; RT "Generation of N-acylphosphatidylethanolamine by members of the RT phospholipase A/acyltransferase (PLA/AT) family."; RL J. Biol. Chem. 287:31905-31919(2012). RN [8] RP REVIEW. RX PubMed=26503625; DOI=10.1186/s12929-015-0210-7; RA Mardian E.B., Bradley R.M., Duncan R.E.; RT "The HRASLS (PLA/AT) subfamily of enzymes."; RL J. Biomed. Sci. 22:99-99(2015). RN [9] RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION (ISOFORMS 1 AND 2), RP CATALYTIC ACTIVITY (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND RP 2), AND TISSUE SPECIFICITY (ISOFORM 2). RC TISSUE=Skeletal muscle; RX PubMed=27623847; DOI=10.1194/jlr.m071290; RA Hussain Z., Uyama T., Kawai K., Rahman I.A., Tsuboi K., Araki N., Ueda N.; RT "Comparative analyses of isoforms of the calcium-independent RT phosphatidylethanolamine N-acyltransferase PLAAT-1 in humans and mice."; RL J. Lipid Res. 57:2051-2060(2016). CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase CC activities (PubMed:21880860, PubMed:26503625). Shows phospholipase A1 CC (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent CC release of fatty acids from the sn-1 or sn-2 position of CC glycerophospholipids (PubMed:21880860, PubMed:22825852, CC PubMed:27623847). Shows O-acyltransferase activity, catalyzing the CC transfer of a fatty acyl group from glycerophospholipid to the hydroxyl CC group of lysophospholipid (PubMed:21880860). Shows N-acyltransferase CC activity, catalyzing the calcium-independent transfer of a fatty acyl CC group at the sn-1 position of phosphatidylcholine (PC) and other CC glycerophospholipids to the primary amine of phosphatidylethanolamine CC (PE), forming N-acylphosphatidylethanolamine (NAPE) which serves as CC precursor for N-acylethanolamines (NAEs) (PubMed:21880860, CC PubMed:22825852, PubMed:27623847). {ECO:0000269|PubMed:21880860, CC ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:27623847, CC ECO:0000303|PubMed:26503625}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; CC Evidence={ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852, CC ECO:0000269|PubMed:27623847}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; CC Evidence={ECO:0000269|PubMed:21880860}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; CC Evidence={ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852, CC ECO:0000269|PubMed:27623847}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; CC Evidence={ECO:0000269|PubMed:21880860}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2- CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; CC Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; CC Evidence={ECO:0000269|PubMed:21880860}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488; CC Evidence={ECO:0000269|PubMed:21880860}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1- CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; CC Evidence={ECO:0000269|PubMed:21880860}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; CC Evidence={ECO:0000269|PubMed:21880860}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn- CC glycero-3-phosphoethanolamine + H(+) + hexadecanoate; CC Xref=Rhea:RHEA:41348, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73009, ChEBI:CHEBI:76091; CC Evidence={ECO:0000269|PubMed:21880860}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349; CC Evidence={ECO:0000269|PubMed:21880860}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; CC Evidence={ECO:0000269|PubMed:21880860}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; CC Evidence={ECO:0000269|PubMed:21880860}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + CC 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H(+) + hexadecanoyl- CC sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z- CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:41360, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999, CC ChEBI:CHEBI:74986, ChEBI:CHEBI:78097; CC Evidence={ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361; CC Evidence={ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + a 2-acyl-sn- CC glycero-3-phosphocholine = 1-hexadecanoyl-2-acyl-sn-glycero-3- CC phosphocholine + 2-hexadecanoyl-sn-glycero-3-phosphocholine; CC Xref=Rhea:RHEA:41364, ChEBI:CHEBI:57875, ChEBI:CHEBI:72999, CC ChEBI:CHEBI:76078, ChEBI:CHEBI:77369; CC Evidence={ECO:0000269|PubMed:21880860}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41365; CC Evidence={ECO:0000269|PubMed:21880860}; CC -!- INTERACTION: CC Q9HDD0; Q8IW40: CCDC103; NbExp=3; IntAct=EBI-12387058, EBI-10261970; CC Q9HDD0; O95872: GPANK1; NbExp=3; IntAct=EBI-12387058, EBI-751540; CC Q9HDD0; O14964: HGS; NbExp=3; IntAct=EBI-12387058, EBI-740220; CC Q9HDD0; P78424: POU6F2; NbExp=3; IntAct=EBI-12387058, EBI-12029004; CC Q9HDD0; O43711: TLX3; NbExp=3; IntAct=EBI-12387058, EBI-3939165; CC Q9HDD0; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12387058, EBI-741480; CC Q9HDD0; Q15915: ZIC1; NbExp=3; IntAct=EBI-12387058, EBI-11963196; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Single-pass CC membrane protein {ECO:0000255}. Cytoplasm CC {ECO:0000269|PubMed:27623847}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus CC {ECO:0000269|PubMed:27623847}. Cytoplasm {ECO:0000269|PubMed:27623847}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=PLAAT-1S {ECO:0000303|PubMed:27623847}; CC IsoId=Q9HDD0-1; Sequence=Displayed; CC Name=2; Synonyms=PLAAT-1L {ECO:0000303|PubMed:27623847}; CC IsoId=Q9HDD0-2; Sequence=VSP_060190; CC -!- TISSUE SPECIFICITY: [Isoform 1]: Abundantly expressed in testis, CC skeletal muscle, brain, and heart. {ECO:0000269|PubMed:21880860}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Highly expressed in the testis, CC skeletal muscle, brain, heart, and thyroid. CC {ECO:0000269|PubMed:27623847}. CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB030816; BAB08110.1; -; mRNA. DR EMBL; AY251533; AAP20056.1; -; mRNA. DR EMBL; AB510981; BAI63210.1; -; mRNA. DR EMBL; AC105057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092966; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78078.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78079.1; -; Genomic_DNA. DR EMBL; BC048095; AAH48095.1; -; mRNA. DR CCDS; CCDS3303.3; -. [Q9HDD0-1] DR RefSeq; NP_065119.2; NM_020386.4. [Q9HDD0-1] DR RefSeq; XP_016862412.1; XM_017006923.1. DR AlphaFoldDB; Q9HDD0; -. DR SMR; Q9HDD0; -. DR IntAct; Q9HDD0; 7. DR STRING; 9606.ENSP00000498228; -. DR SwissLipids; SLP:000000688; -. DR PhosphoSitePlus; Q9HDD0; -. DR BioMuta; HRASLS; -. DR DMDM; 20138344; -. DR PaxDb; 9606-ENSP00000264735; -. DR Antibodypedia; 33880; 48 antibodies from 15 providers. DR DNASU; 57110; -. DR Ensembl; ENST00000264735.4; ENSP00000264735.4; ENSG00000127252.7. [Q9HDD0-1] DR Ensembl; ENST00000650797.1; ENSP00000498228.1; ENSG00000127252.7. [Q9HDD0-2] DR GeneID; 57110; -. DR KEGG; hsa:57110; -. DR MANE-Select; ENST00000264735.4; ENSP00000264735.4; NM_020386.5; NP_065119.3. DR UCSC; uc003fta.5; human. DR AGR; HGNC:14922; -. DR CTD; 57110; -. DR DisGeNET; 57110; -. DR GeneCards; PLAAT1; -. DR HGNC; HGNC:14922; PLAAT1. DR HPA; ENSG00000127252; Group enriched (skeletal muscle, testis, tongue). DR MIM; 606487; gene. DR neXtProt; NX_Q9HDD0; -. DR OpenTargets; ENSG00000127252; -. DR PharmGKB; PA29445; -. DR VEuPathDB; HostDB:ENSG00000127252; -. DR eggNOG; ENOG502QU0S; Eukaryota. DR GeneTree; ENSGT00940000156634; -. DR HOGENOM; CLU_1019273_0_0_1; -. DR InParanoid; Q9HDD0; -. DR OrthoDB; 3059772at2759; -. DR PhylomeDB; Q9HDD0; -. DR TreeFam; TF330836; -. DR BioCyc; MetaCyc:ENSG00000127252-MONOMER; -. DR PathwayCommons; Q9HDD0; -. DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE. DR SignaLink; Q9HDD0; -. DR BioGRID-ORCS; 57110; 15 hits in 1149 CRISPR screens. DR ChiTaRS; HRASLS; human. DR GenomeRNAi; 57110; -. DR Pharos; Q9HDD0; Tbio. DR PRO; PR:Q9HDD0; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9HDD0; Protein. DR Bgee; ENSG00000127252; Expressed in sperm and 162 other cell types or tissues. DR ExpressionAtlas; Q9HDD0; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005764; C:lysosome; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005641; C:nuclear envelope lumen; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0016410; F:N-acyltransferase activity; IDA:UniProtKB. DR GO; GO:0008374; F:O-acyltransferase activity; IDA:UniProtKB. DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB. DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IDA:UniProtKB. DR GO; GO:1903008; P:organelle disassembly; ISS:UniProtKB. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB. DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1. DR InterPro; IPR007053; LRAT_dom. DR PANTHER; PTHR13943; HRAS-LIKE SUPPRESSOR - RELATED; 1. DR PANTHER; PTHR13943:SF37; PHOSPHOLIPASE A AND ACYLTRANSFERASE 1; 1. DR Pfam; PF04970; LRAT; 1. DR PROSITE; PS51934; LRAT; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Hydrolase; Lipid degradation; KW Lipid metabolism; Membrane; Nucleus; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..168 FT /note="Phospholipase A and acyltransferase 1" FT /id="PRO_0000152481" FT TOPO_DOM 1..138 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 139..159 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 160..168 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 20..135 FT /note="LRAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283" FT ACT_SITE 30 FT /evidence="ECO:0000250|UniProtKB:P53816" FT ACT_SITE 119 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000250|UniProtKB:P53816" FT VAR_SEQ 1 FT /note="M -> MVRASCRLGSARTPSPARRPPGVRASQSRGGAAGTVSAWRRWCWRWP FT WRTAPSDGWRLPPGCLPGTDGVVPRPPAARSAAARPRETPGHTQLPPGARRRPRLESEM FT (in isoform 2)" FT /id="VSP_060190" FT CONFLICT 58 FT /note="S -> P (in Ref. 2; AAP20056)" FT /evidence="ECO:0000305" FT CONFLICT 118 FT /note="N -> D (in Ref. 6; AAH48095)" FT /evidence="ECO:0000305" SQ SEQUENCE 168 AA; 18750 MW; 11844F8B5963D39B CRC64; MAFNDCFSLN YPGNPCPGDL IEVFRPGYQH WALYLGDGYV INIAPVDGIP ASFTSAKSVF SSKALVKMQL LKDVVGNDTY RINNKYDETY PPLPVEEIIK RSEFVIGQEV AYNLLVNNCE HFVTLLRYGE GVSEQANRAI STVEFVTAAV GVFSFLGLFP KGQRAKYY //