{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P48622","uniProtkbId":"FAD3D_ARATH","entryAudit":{"firstPublicDate":"1996-02-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-02-01","entryVersion":166,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Arabidopsis thaliana","commonName":"Mouse-ear cress","taxonId":3702,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12232435"}],"value":"Temperature-sensitive sn-2 acyl-lipid omega-3 desaturase (ferredoxin), chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12232435"}],"value":"1.14.19.35"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7846164"}],"value":"Temperature-sensitive omega-3 fatty acid desaturase 8, chloroplastic"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7846164"}],"value":"FAD8"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"Araport","id":"AT5G05580"}],"value":"At5g05580"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AED90892.1"}],"value":"MOP10.12"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7846164"}],"value":"Chloroplast omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 16:3 and 18:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycerol"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (7Z,10Z)-hexadecadienoyl-containing glycerolipid + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = a (7Z,10Z,13Z)-hexadecatrienoyl-containing glycerolipid + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46412"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:88268"},{"database":"ChEBI","id":"CHEBI:88269"}],"ecNumber":"1.14.19.35","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12232435"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = (9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46408"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:88351"},{"database":"ChEBI","id":"CHEBI:90078"}],"ecNumber":"1.14.19.35","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12232435"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7846164"}],"value":"Lipid metabolism; polyunsaturated fatty acid biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Plastid, chloroplast membrane","id":"SL-0053"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P48622-1"],"isoformSequenceStatus":"Displayed"}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"A number of isoforms are produced. According to EST sequences."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7846164"}],"value":"By low temperature"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"The histidine box domains may contain the active site and/or be involved in metal ion binding"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the fatty acid desaturase type 1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transit peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Chloroplast","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"Temperature-sensitive sn-2 acyl-lipid omega-3 desaturase (ferredoxin), chloroplastic","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":"PRO_0000007122"},{"type":"Transmembrane","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Motif","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Histidine box-1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Motif","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"Histidine box-2","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Motif","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Histidine box-3","evidences":[{"evidenceCode":"ECO:0000305"}]}],"keywords":[{"id":"KW-0025","category":"Coding sequence diversity","name":"Alternative splicing"},{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0809","category":"Domain","name":"Transit peptide"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"7846164","citationType":"journal article","authors":["Gibson S.","Arondel V.","Iba K.","Somerville C.R."],"citationCrossReferences":[{"database":"PubMed","id":"7846164"},{"database":"DOI","id":"10.1104/pp.106.4.1615"}],"title":"Cloning of a temperature-regulated gene encoding a chloroplast omega-3 desaturase from Arabidopsis thaliana.","publicationDate":"1994","journal":"Plant Physiol.","firstPage":"1615","lastPage":"1621","volume":"106"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]","FUNCTION","INDUCTION BY COLD"],"referenceComments":[{"value":"cv. Columbia","type":"STRAIN"},{"value":"Aerial part","type":"TISSUE"}]},{"referenceNumber":2,"citation":{"id":"7972507","citationType":"journal article","authors":["Watahiki M.C.","Yamamoto K.T."],"citationCrossReferences":[{"database":"PubMed","id":"7972507"},{"database":"DOI","id":"10.1104/pp.105.4.1451"}],"title":"A new isozyme of plastid omega-3 fatty acid desaturase in Arabidopsis thaliana.","publicationDate":"1994","journal":"Plant Physiol.","firstPage":"1451","lastPage":"1452","volume":"105"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]"],"referenceComments":[{"value":"cv. Columbia","type":"STRAIN"},{"value":"Hypocotyl","type":"TISSUE"}]},{"referenceNumber":3,"citation":{"id":"9330910","citationType":"journal article","authors":["Sato S.","Kotani H.","Nakamura Y.","Kaneko T.","Asamizu E.","Fukami M.","Miyajima N.","Tabata S."],"citationCrossReferences":[{"database":"PubMed","id":"9330910"},{"database":"DOI","id":"10.1093/dnares/4.3.215"}],"title":"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones.","publicationDate":"1997","journal":"DNA Res.","firstPage":"215","lastPage":"230","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"cv. Columbia","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"27862469","citationType":"journal article","authors":["Cheng C.Y.","Krishnakumar V.","Chan A.P.","Thibaud-Nissen F.","Schobel S.","Town C.D."],"citationCrossReferences":[{"database":"PubMed","id":"27862469"},{"database":"DOI","id":"10.1111/tpj.13415"}],"title":"Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.","publicationDate":"2017","journal":"Plant J.","firstPage":"789","lastPage":"804","volume":"89"},"referencePositions":["GENOME REANNOTATION"],"referenceComments":[{"value":"cv. Columbia","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"CI-CI4AM1G71UC0S","citationType":"submission","authoringGroup":["The Arabidopsis Information Resource (TAIR)"],"title":"Community-consensus reference genome of Arabidopsis thaliana Col-0.","publicationDate":"FEB-2026","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["GENOME REANNOTATION"],"referenceComments":[{"value":"cv. Columbia","type":"STRAIN"}]},{"referenceNumber":6,"citation":{"id":"14593172","citationType":"journal article","authors":["Yamada K.","Lim J.","Dale J.M.","Chen H.","Shinn P.","Palm C.J.","Southwick A.M.","Wu H.C.","Kim C.J.","Nguyen M.","Pham P.K.","Cheuk R.F.","Karlin-Newmann G.","Liu S.X.","Lam B.","Sakano H.","Wu T.","Yu G.","Miranda M.","Quach H.L.","Tripp M.","Chang C.H.","Lee J.M.","Toriumi M.J.","Chan M.M.","Tang C.C.","Onodera C.S.","Deng J.M.","Akiyama K.","Ansari Y.","Arakawa T.","Banh J.","Banno F.","Bowser L.","Brooks S.Y.","Carninci P.","Chao Q.","Choy N.","Enju A.","Goldsmith A.D.","Gurjal M.","Hansen N.F.","Hayashizaki Y.","Johnson-Hopson C.","Hsuan V.W.","Iida K.","Karnes M.","Khan S.","Koesema E.","Ishida J.","Jiang P.X.","Jones T.","Kawai J.","Kamiya A.","Meyers C.","Nakajima M.","Narusaka M.","Seki M.","Sakurai T.","Satou M.","Tamse R.","Vaysberg M.","Wallender E.K.","Wong C.","Yamamura Y.","Yuan S.","Shinozaki K.","Davis R.W.","Theologis A.","Ecker J.R."],"citationCrossReferences":[{"database":"PubMed","id":"14593172"},{"database":"DOI","id":"10.1126/science.1088305"}],"title":"Empirical analysis of transcriptional activity in the Arabidopsis genome.","publicationDate":"2003","journal":"Science","firstPage":"842","lastPage":"846","volume":"302"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]"],"referenceComments":[{"value":"cv. Columbia","type":"STRAIN"}]},{"referenceNumber":7,"citation":{"id":"12232435","citationType":"journal article","authors":["McConn M.","Hugly S.","Browse J.","Somerville C."],"citationCrossReferences":[{"database":"PubMed","id":"12232435"},{"database":"DOI","id":"10.1104/pp.106.4.1609"}],"title":"A Mutation at the fad8 Locus of Arabidopsis Identifies a Second Chloroplast [omega]-3 Desaturase.","publicationDate":"1994","journal":"Plant Physiol.","firstPage":"1609","lastPage":"1614","volume":"106"},"referencePositions":["FUNCTION","PATHWAY","CATALYTIC ACTIVITY"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"L27158","properties":[{"key":"ProteinId","value":"AAA65621.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"U08216","properties":[{"key":"ProteinId","value":"AAB60302.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"D17578","properties":[{"key":"ProteinId","value":"BAA04504.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AB005241","properties":[{"key":"ProteinId","value":"BAB11547.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"CP002688","properties":[{"key":"ProteinId","value":"AED90892.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"OZ408687","properties":[{"key":"ProteinId","value":"CAO7051172.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AF361837","properties":[{"key":"ProteinId","value":"AAK32849.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AY078043","properties":[{"key":"ProteinId","value":"AAL77744.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"RefSeq","id":"NP_196177.1","properties":[{"key":"NucleotideSequenceId","value":"NM_120640.4"}],"isoformId":"P48622-1"},{"database":"AlphaFoldDB","id":"P48622","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P48622","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"15720","properties":[{"key":"Interactions","value":"2"}]},{"database":"FunCoup","id":"P48622","properties":[{"key":"Number of interactors","value":"604"}]},{"database":"STRING","id":"3702.P48622","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"3702-P48622","properties":[{"key":"Description","value":"-"}]},{"database":"ProteomicsDB","id":"222315","properties":[{"key":"Description","value":"-"}],"isoformId":"P48622-1"},{"database":"GeneID","id":"830441","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ath:AT5G05580","properties":[{"key":"Description","value":"-"}]},{"database":"Araport","id":"AT5G05580","properties":[{"key":"Description","value":"-"}]},{"database":"TAIR","id":"AT5G05580","properties":[{"key":"GeneName","value":"FAD8"}]},{"database":"eggNOG","id":"ENOG502QQQ2","properties":[{"key":"ToxonomicScope","value":"Eukaryota"}]},{"database":"InParanoid","id":"P48622","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"NSVMGHI","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"1461976at2759","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P48622","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"ARA:AT5G05580-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:AT5G05580-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.14.19.35","properties":[{"key":"OrganismId","value":"399"}]},{"database":"BRENDA","id":"1.14.19.36","properties":[{"key":"OrganismId","value":"399"}]},{"database":"UniPathway","id":"UPA00658","properties":[{"key":"RectionId","value":"-"}]},{"database":"PRO","id":"PR:P48622","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000006548","properties":[{"key":"Component","value":"Chromosome 5"}]},{"database":"ExpressionAtlas","id":"P48622","properties":[{"key":"ExpressionPatterns","value":"baseline and differential"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"ISS:TAIR"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"PubMed","id":"7846164"}]},{"database":"GO","id":"GO:0009941","properties":[{"key":"GoTerm","value":"C:chloroplast envelope"},{"key":"GoEvidenceType","value":"HDA:TAIR"}],"evidences":[{"evidenceCode":"ECO:0007005","source":"PubMed","id":"12938931"}]},{"database":"GO","id":"GO:0031969","properties":[{"key":"GoTerm","value":"C:chloroplast membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"HDA:TAIR"}],"evidences":[{"evidenceCode":"ECO:0007005","source":"PubMed","id":"28887381"}]},{"database":"GO","id":"GO:0042389","properties":[{"key":"GoTerm","value":"F:omega-3 fatty acid desaturase activity"},{"key":"GoEvidenceType","value":"IMP:TAIR"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"7846164"}]},{"database":"GO","id":"GO:0102993","properties":[{"key":"GoTerm","value":"F:sn-2 acyl-lipid omega-3 desaturase (ferredoxin) activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12232435"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IMP:TAIR"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"7846164"}]},{"database":"GO","id":"GO:0009266","properties":[{"key":"GoTerm","value":"P:response to temperature stimulus"},{"key":"GoEvidenceType","value":"IEP:TIGR"}],"evidences":[{"evidenceCode":"ECO:0000270","source":"PubMed","id":"7846164"}]},{"database":"GO","id":"GO:0006636","properties":[{"key":"GoTerm","value":"P:unsaturated fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd03507","properties":[{"key":"EntryName","value":"Delta12-FADS-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005804","properties":[{"key":"EntryName","value":"FA_desaturase_dom"}]},{"database":"InterPro","id":"IPR021863","properties":[{"key":"EntryName","value":"FAS_N"}]},{"database":"InterPro","id":"IPR012171","properties":[{"key":"EntryName","value":"Fatty_acid_desaturase"}]},{"database":"PANTHER","id":"PTHR32100","properties":[{"key":"EntryName","value":"OMEGA-6 FATTY ACID DESATURASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11960","properties":[{"key":"EntryName","value":"DUF3474"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00487","properties":[{"key":"EntryName","value":"FA_desaturase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MASSVLSECGFRPLPRFYPKHTTSFASNPKPTFKFNPPLKPPSSLLNSRYGFYSKTRNWALNVATPLTTLQSPSEEDTERFDPGAPPPFNLADIRAAIPKHCWVKNPWMSMSYVVRDVAIVFGLAAVAAYFNNWLLWPLYWFAQGTMFWALFVLGHDCGHGSFSNDPRLNSVAGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLPESIYKNLEKTTQMFRFTLPFPMLAYPFYLWNRSPGKQGSHYHPDSDLFLPKEKKDVLTSTACWTAMAALLVCLNFVMGPIQMLKLYGIPYWIFVMWLDFVTYLHHHGHEDKLPWYRGKEWSYLRGGLTTLDRDYGWINNIHHDIGTHVIHHLFPQIPHYHLVEATEAAKPVLGKYYREPKNSGPLPLHLLGSLIKSMKQDHFVSDTGDVVYYEADPKLNGQRT","length":435,"molWeight":50136,"crc64":"3D77A8035A6214E1","md5":"C602BA82ED092902DF870986D30964E0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"ALTERNATIVE PRODUCTS":1,"INDUCTION":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Transit peptide":1,"Chain":1,"Transmembrane":4,"Motif":3},"uniParcId":"UPI0000000EE4"}}