ID PA2GF_HUMAN Reviewed; 168 AA. AC Q9BZM2; Q5R385; Q8N217; Q9H506; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-JAN-2024, entry version 169. DE RecName: Full=Group IIF secretory phospholipase A2 {ECO:0000303|PubMed:11877435}; DE Short=GIIF sPLA2; DE Short=sPLA2-IIF; DE EC=3.1.1.4 {ECO:0000269|PubMed:11112443}; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2F; DE Flags: Precursor; GN Name=PLA2G2F; 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), FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY. RC TISSUE=Fetal lung, Heart, and Spleen; RX PubMed=11112443; DOI=10.1006/bbrc.2000.3908; RA Valentin E., Singer A.G., Ghomashchi F., Lazdunski M., Gelb M.H., RA Lambeau G.; RT "Cloning and recombinant expression of human group IIF-secreted RT phospholipase A(2)."; RL Biochem. Biophys. Res. Commun. 279:223-228(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Thymus; 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 [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 TISSUE SPECIFICITY. RX PubMed=11877435; DOI=10.1074/jbc.m112385200; RA Murakami M., Yoshihara K., Shimbara S., Lambeau G., Gelb M.H., Singer A.G., RA Sawada M., Inagaki N., Nagai H., Ishihara M., Ishikawa Y., Ishii T., RA Kudo I.; RT "Cellular arachidonate-releasing function and inflammation-associated RT expression of group IIF secretory phospholipase A2."; RL J. Biol. Chem. 277:19145-19155(2002). CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily CC targets extracellular phospholipids. Hydrolyzes the ester bond of the CC fatty acyl group attached at the sn-2 position of phospholipids CC (phospholipase A2 activity), the catalytic efficiency decreasing in the CC following order: phosphatidylglycerols > phosphatidylethanolamines > CC phosphatidylcholines > phosphatidylserines (PubMed:11112443). May play CC a role in lipid mediator production in inflammatory conditions, by CC providing arachidonic acid to downstream cyclooxygenases and CC lipoxygenases (By similarity). {ECO:0000250|UniProtKB:Q9QZT4, CC ECO:0000269|PubMed:11112443}. 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:0000255|PROSITE-ProRule:PRU10035, CC ECO:0000269|PubMed:11112443}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; CC Evidence={ECO:0000305|PubMed:11112443}; 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:11112443}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; CC Evidence={ECO:0000305|PubMed:11112443}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1- CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; CC Evidence={ECO:0000250|UniProtKB:Q9QZT4}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; CC Evidence={ECO:0000250|UniProtKB:Q9QZT4}; 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:0000250|UniProtKB:Q9QZT4}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; CC Evidence={ECO:0000250|UniProtKB:Q9QZT4}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3- CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:11112443}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; CC Evidence={ECO:0000305|PubMed:11112443}; 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:11112443}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41753; CC Evidence={ECO:0000305|PubMed:11112443}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:11112443}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11112443}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7-8. {ECO:0000269|PubMed:11112443}; CC -!- INTERACTION: CC Q9BZM2-2; P41271-2: NBL1; NbExp=3; IntAct=EBI-12826629, EBI-12135485; CC Q9BZM2-2; O95231: VENTX; NbExp=3; IntAct=EBI-12826629, EBI-10191303; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted CC {ECO:0000250|UniProtKB:Q9QZT4}. Cell membrane; Peripheral membrane CC protein {ECO:0000250|UniProtKB:Q9QZT4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BZM2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZM2-2; Sequence=VSP_037524; CC -!- TISSUE SPECIFICITY: Expressed at high levels in placenta, testis, CC thymus and at lower levels in heart, kidney, liver and prostate CC (PubMed:11112443). Highly expressed in rheumatoid arthritic tissues, CC including synovial lining cells in the intima, capillary endothelial CC cells and plasma cells (PubMed:11877435). {ECO:0000269|PubMed:11112443, CC ECO:0000269|PubMed:11877435}. CC -!- MISCELLANEOUS: [Isoform 2]: No signal peptide could be predicted in CC this isoform, challenging its subcellular location within the secretory CC pathway and hence the formation of disulfide bonds, which are required CC for its activity. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phospholipase A2 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; AF306566; AAG50242.1; -; mRNA. DR EMBL; AK093645; BAC04210.1; -; mRNA. DR EMBL; AL158172; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z98257; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS204.2; -. [Q9BZM2-2] DR RefSeq; NP_073730.3; NM_022819.3. [Q9BZM2-2] DR RefSeq; XP_011540258.1; XM_011541956.1. [Q9BZM2-2] DR AlphaFoldDB; Q9BZM2; -. DR SMR; Q9BZM2; -. DR BioGRID; 122219; 4. DR IntAct; Q9BZM2; 2. DR STRING; 9606.ENSP00000364243; -. DR BindingDB; Q9BZM2; -. DR ChEMBL; CHEMBL4278; -. DR GuidetoPHARMACOLOGY; 1420; -. DR SwissLipids; SLP:000000654; -. [Q9BZM2-1] DR GlyCosmos; Q9BZM2; 4 sites, No reported glycans. DR GlyGen; Q9BZM2; 4 sites. DR iPTMnet; Q9BZM2; -. DR PhosphoSitePlus; Q9BZM2; -. DR BioMuta; PLA2G2F; -. DR DMDM; 20139134; -. DR PaxDb; 9606-ENSP00000364243; -. DR Antibodypedia; 68368; 5 antibodies from 3 providers. DR DNASU; 64600; -. DR Ensembl; ENST00000375102.4; ENSP00000364243.4; ENSG00000158786.5. [Q9BZM2-2] DR GeneID; 64600; -. DR KEGG; hsa:64600; -. DR MANE-Select; ENST00000375102.4; ENSP00000364243.4; NM_022819.4; NP_073730.3. [Q9BZM2-2] DR UCSC; uc009vpp.2; human. [Q9BZM2-1] DR AGR; HGNC:30040; -. DR CTD; 64600; -. DR GeneCards; PLA2G2F; -. DR HGNC; HGNC:30040; PLA2G2F. DR HPA; ENSG00000158786; Group enriched (lymphoid tissue, skin, urinary bladder). DR neXtProt; NX_Q9BZM2; -. DR OpenTargets; ENSG00000158786; -. DR PharmGKB; PA134931043; -. DR VEuPathDB; HostDB:ENSG00000158786; -. DR eggNOG; KOG4087; Eukaryota. DR GeneTree; ENSGT00940000161819; -. DR HOGENOM; CLU_090683_2_0_1; -. DR InParanoid; Q9BZM2; -. DR OMA; ETECDKQ; -. DR OrthoDB; 638584at2759; -. DR PhylomeDB; Q9BZM2; -. DR TreeFam; TF319283; -. DR PathwayCommons; Q9BZM2; -. DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC. DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS. DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE. DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI. DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG. DR Reactome; R-HSA-1483166; Synthesis of PA. DR SignaLink; Q9BZM2; -. DR BioGRID-ORCS; 64600; 9 hits in 1144 CRISPR screens. DR GenomeRNAi; 64600; -. DR Pharos; Q9BZM2; Tchem. DR PRO; PR:Q9BZM2; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BZM2; Protein. DR Bgee; ENSG00000158786; Expressed in skin of leg and 45 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:0004623; F:phospholipase A2 activity; NAS:UniProtKB. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central. DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB. DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB. DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; IDA:UniProtKB. DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; IDA:UniProtKB. DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central. DR CDD; cd00125; PLA2c; 1. DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR016090; PLipase_A2_dom. DR InterPro; IPR036444; PLipase_A2_dom_sf. DR InterPro; IPR033113; PLipase_A2_His_AS. DR PANTHER; PTHR11716:SF8; GROUP IIF SECRETORY PHOSPHOLIPASE A2; 1. DR PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1. DR PROSITE; PS00118; PA2_HIS; 1. DR Genevisible; Q9BZM2; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell membrane; Disulfide bond; Glycoprotein; KW Hydrolase; Immunity; Innate immunity; Lipid degradation; Lipid metabolism; KW Membrane; Metal-binding; Reference proteome; Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..168 FT /note="Group IIF secretory phospholipase A2" FT /id="PRO_0000022759" FT REGION 139..168 FT /note="Required for localization on the plasma membrane" FT /evidence="ECO:0000250|UniProtKB:Q9QZT4" FT ACT_SITE 67 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035" FT ACT_SITE 114 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035" FT BINDING 47 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 49 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 51 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 68 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT CARBOHYD 92 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 144 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 46..138 FT /evidence="ECO:0000250" FT DISULFID 48..64 FT /evidence="ECO:0000250" FT DISULFID 63..120 FT /evidence="ECO:0000250" FT DISULFID 69..145 FT /evidence="ECO:0000250" FT DISULFID 70..113 FT /evidence="ECO:0000250" FT DISULFID 79..106 FT /evidence="ECO:0000250" FT DISULFID 98..111 FT /evidence="ECO:0000250" FT VAR_SEQ 1 FT /note="M -> MADGAKANPKGFKKKVLDRCFSGWRGPRFGASCPSRTSRSSLGM FT (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_037524" FT CONFLICT 149 FT /note="E -> G (in Ref. 2; BAC04210)" FT /evidence="ECO:0000305" SQ SEQUENCE 168 AA; 18658 MW; 35B159298246A762 CRC64; MKKFFTVAIL AGSVLSTAHG SLLNLKAMVE AVTGRSAILS FVGYGCYCGL GGRGQPKDEV DWCCHAHDCC YQELFDQGCH PYVDHYDHTI ENNTEIVCSD LNKTECDKQT CMCDKNMVLC LMNQTYREEY RGFLNVYCQG PTPNCSIYEP PPEEVTCSHQ SPAPPAPP //