ID GPAT1_HUMAN Reviewed; 828 AA. AC Q9HCL2; Q5VW51; Q86TA3; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 3. DT 24-JAN-2024, entry version 182. DE RecName: Full=Glycerol-3-phosphate acyltransferase 1, mitochondrial {ECO:0000305}; DE Short=GPAT-1; DE EC=2.3.1.15 {ECO:0000269|PubMed:18238778}; DE Flags: Precursor; GN Name=GPAM {ECO:0000312|HGNC:HGNC:24865}; Synonyms=GPAT1, KIAA1560; 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]. RC TISSUE=Spinal cord; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-828. RC TISSUE=Brain; RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [5] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18238778; DOI=10.1074/jbc.m708151200; RA Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E., RA Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E., RA Konrad R.J., Beigneux A.P., Young S.G., Cao G.; RT "AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase."; RL J. Biol. Chem. 283:10048-10057(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [7] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19075029; DOI=10.1194/jlr.m800567-jlr200; RA Zhao Y., Chen Y.-Q., Li S., Konrad R.J., Cao G.; RT "The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin RT acyltransferase is an acyltransferase of multiple anionic RT lysophospholipids."; RL J. Lipid Res. 50:945-956(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of CC glycerol-3-phosphate, an essential step in glycerolipids biosynthesis CC such as triglycerides, phosphatidic acids and lysophosphatidic acids. CC {ECO:0000269|PubMed:18238778}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3- CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15; CC Evidence={ECO:0000269|PubMed:18238778}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326; CC Evidence={ECO:0000305|PubMed:18238778}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1- CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA; CC Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, CC ChEBI:CHEBI:57597, ChEBI:CHEBI:74547; CC Evidence={ECO:0000269|PubMed:18238778}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204; CC Evidence={ECO:0000305|PubMed:18238778}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z- CC octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597, CC ChEBI:CHEBI:74544; Evidence={ECO:0000269|PubMed:18238778}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200; CC Evidence={ECO:0000305|PubMed:18238778}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl- CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37195, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57597, CC ChEBI:CHEBI:74565; Evidence={ECO:0000269|PubMed:18238778}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196; CC Evidence={ECO:0000305|PubMed:18238778}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl- CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518, CC ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:18238778}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724; CC Evidence={ECO:0000305|PubMed:18238778}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn- CC glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682; CC Evidence={ECO:0000269|PubMed:18238778}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728; CC Evidence={ECO:0000305|PubMed:18238778}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA = CC 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA; CC Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, CC ChEBI:CHEBI:64716, ChEBI:CHEBI:64840; CC Evidence={ECO:0000269|PubMed:19075029}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204; CC Evidence={ECO:0000269|PubMed:19075029}; CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP- CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3. CC {ECO:0000269|PubMed:18238778}. CC -!- INTERACTION: CC Q9HCL2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-7600236, EBI-7062247; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000250|UniProtKB:P97564}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P97564}. CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and CC may constitute the binding site for the phosphate moiety of the CC glycerol-3-phosphate. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GPAT/DAPAT 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; AL833093; CAD89932.1; -; mRNA. DR EMBL; AL391986; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB046780; BAB13386.1; -; mRNA. DR CCDS; CCDS7570.1; -. DR RefSeq; NP_001231878.1; NM_001244949.1. DR RefSeq; NP_065969.3; NM_020918.5. DR RefSeq; XP_005270055.1; XM_005269998.1. DR PDB; 8E4Y; EM; 3.40 A; A=80-828. DR PDB; 8E50; EM; 3.67 A; A=80-828. DR PDBsum; 8E4Y; -. DR PDBsum; 8E50; -. DR AlphaFoldDB; Q9HCL2; -. DR EMDB; EMD-27898; -. DR EMDB; EMD-27899; -. DR SMR; Q9HCL2; -. DR BioGRID; 121707; 35. DR IntAct; Q9HCL2; 12. DR MINT; Q9HCL2; -. DR STRING; 9606.ENSP00000265276; -. DR BindingDB; Q9HCL2; -. DR ChEMBL; CHEMBL3734642; -. DR SwissLipids; SLP:000000094; -. DR GlyGen; Q9HCL2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9HCL2; -. DR PhosphoSitePlus; Q9HCL2; -. DR SwissPalm; Q9HCL2; -. DR BioMuta; GPAM; -. DR DMDM; 59803040; -. DR EPD; Q9HCL2; -. DR jPOST; Q9HCL2; -. DR MassIVE; Q9HCL2; -. DR MaxQB; Q9HCL2; -. DR PaxDb; 9606-ENSP00000265276; -. DR PeptideAtlas; Q9HCL2; -. DR ProteomicsDB; 81752; -. DR Pumba; Q9HCL2; -. DR Antibodypedia; 31772; 264 antibodies from 30 providers. DR DNASU; 57678; -. DR Ensembl; ENST00000348367.9; ENSP00000265276.4; ENSG00000119927.14. DR GeneID; 57678; -. DR KEGG; hsa:57678; -. DR MANE-Select; ENST00000348367.9; ENSP00000265276.4; NM_001244949.2; NP_001231878.1. DR UCSC; uc001kzp.4; human. DR AGR; HGNC:24865; -. DR CTD; 57678; -. DR DisGeNET; 57678; -. DR GeneCards; GPAM; -. DR HGNC; HGNC:24865; GPAM. DR HPA; ENSG00000119927; Tissue enhanced (adipose tissue, liver). DR MIM; 602395; gene. DR neXtProt; NX_Q9HCL2; -. DR OpenTargets; ENSG00000119927; -. DR PharmGKB; PA134983031; -. DR VEuPathDB; HostDB:ENSG00000119927; -. DR eggNOG; KOG3729; Eukaryota. DR GeneTree; ENSGT00520000055570; -. DR InParanoid; Q9HCL2; -. DR OMA; RCKHTNE; -. DR OrthoDB; 2874405at2759; -. DR PhylomeDB; Q9HCL2; -. DR TreeFam; TF313360; -. DR BioCyc; MetaCyc:57678-MONOMER; -. DR BRENDA; 2.3.1.15; 2681. DR PathwayCommons; Q9HCL2; -. DR Reactome; R-HSA-1483166; Synthesis of PA. DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP). DR Reactome; R-HSA-75109; Triglyceride biosynthesis. DR Reactome; R-HSA-8931987; RUNX1 regulates estrogen receptor mediated transcription. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR SignaLink; Q9HCL2; -. DR UniPathway; UPA00557; UER00612. DR BioGRID-ORCS; 57678; 11 hits in 1159 CRISPR screens. DR ChiTaRS; GPAM; human. DR GeneWiki; GPAM; -. DR GenomeRNAi; 57678; -. DR Pharos; Q9HCL2; Tbio. DR PRO; PR:Q9HCL2; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9HCL2; Protein. DR Bgee; ENSG00000119927; Expressed in pericardium and 181 other cell types or tissues. DR ExpressionAtlas; Q9HCL2; baseline and differential. DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central. DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IMP:UniProtKB. DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC. DR GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl. DR GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl. DR GO; GO:0006637; P:acyl-CoA metabolic process; IEA:Ensembl. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl. DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB. DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl. DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IEA:Ensembl. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IMP:UniProtKB. DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central. DR GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl. DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB. DR CDD; cd07993; LPLAT_DHAPAT-like; 1. DR InterPro; IPR022284; GPAT/DHAPAT. DR InterPro; IPR045520; GPAT/DHAPAT_C. DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT. DR InterPro; IPR028354; GPAT_PlsB. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1. DR PANTHER; PTHR12563:SF16; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 1, MITOCHONDRIAL; 1. DR Pfam; PF01553; Acyltransferase; 1. DR Pfam; PF19277; GPAT_C; 1. DR PIRSF; PIRSF500064; GPAT; 1. DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1. DR SMART; SM00563; PlsC; 1. DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1. DR Genevisible; Q9HCL2; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Lipid biosynthesis; KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein; KW Reference proteome; Transferase; Transit peptide; Transmembrane; KW Transmembrane helix. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..828 FT /note="Glycerol-3-phosphate acyltransferase 1, FT mitochondrial" FT /id="PRO_0000024690" FT TOPO_DOM ?..471 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 472..494 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 495..574 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 575..593 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 594..828 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT REGION 435..455 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 230..235 FT /note="HXXXXD motif" FT COMPBIAS 439..455 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 380 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97564" FT MOD_RES 688 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61586" FT MOD_RES 695 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:24275569" FT MOD_RES 780 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61586" FT MOD_RES 784 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61586" FT VARIANT 4 FT /note="S -> Y (in dbSNP:rs11549703)" FT /id="VAR_050585" FT VARIANT 43 FT /note="I -> V (in dbSNP:rs2792751)" FT /id="VAR_050586" FT VARIANT 131 FT /note="E -> G (in dbSNP:rs10787428)" FT /id="VAR_050587" FT VARIANT 386 FT /note="I -> T (in dbSNP:rs35019520)" FT /id="VAR_050588" FT CONFLICT 204 FT /note="I -> F (in Ref. 1; CAD89932)" FT /evidence="ECO:0000305" FT CONFLICT 652 FT /note="Q -> R (in Ref. 1; CAD89932)" FT /evidence="ECO:0000305" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:8E4Y" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 104..108 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 110..115 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 129..134 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 137..150 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 163..175 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 183..200 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 208..219 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 224..228 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 235..244 FT /evidence="ECO:0007829|PDB:8E4Y" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 252..256 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 264..270 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 290..305 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 314..317 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 320..323 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 332..340 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 348..358 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 365..369 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 380..390 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 396..400 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 406..415 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 424..432 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 457..479 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 484..494 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 502..518 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 529..539 FT /evidence="ECO:0007829|PDB:8E4Y" FT TURN 540..543 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 544..548 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 554..559 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 563..573 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 574..576 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 577..594 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 612..625 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 626..630 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 635..637 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 639..652 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 655..658 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 705..708 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 712..724 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 726..738 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 739..741 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 748..764 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 771..774 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 777..789 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 791..796 FT /evidence="ECO:0007829|PDB:8E4Y" FT STRAND 798..805 FT /evidence="ECO:0007829|PDB:8E4Y" FT HELIX 812..823 FT /evidence="ECO:0007829|PDB:8E4Y" SQ SEQUENCE 828 AA; 93795 MW; 7AADD21BC8684693 CRC64; MDESALTLGT IDVSYLPHSS EYSVGRCKHT SEEWGECGFR PTIFRSATLK WKESLMSRKR PFVGRCCYSC TPQSWDKFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YVLFIQERDV HKGMFATNVT ENVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAVNKVKKKA KRILQEMVAT VSPAMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDV LYRALLHGHI VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS TNVIPDILII PVGISYDRII EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGCVRVDF AQPFSLKEYL ESQSQKPVSA LLSLEQALLP AILPSRPSDA ADEGRDTSIN ESRNATDESL RRRLIANLAE HILFTASKSC AIMSTHIVAC LLLYRHRQGI DLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL GNCVTITHTS RNDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSL YAVLNKRGLG GPTSTPPNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF IQYGILTVAE HDDQEDISPS LAEQQWDKKL PEPLSWRSDE EDEDSDFGEE QRDCYLKVSQ SKEHQQFITF LQRLLGPLLE AYSSAAIFVH NFSGPVPEPE YLQKLHKYLI TRTERNVAVY AESATYCLVK NAVKMFKDIG VFKETKQKRV SVLELSSTFL PQCNRQKLLE YILSFVVL //