ID PCY2_HUMAN Reviewed; 389 AA. AC Q99447; B7Z7A5; B7ZAS0; F5H8B1; Q6IBM3; Q96G08; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=Ethanolamine-phosphate cytidylyltransferase; DE EC=2.7.7.14 {ECO:0000269|PubMed:31637422, ECO:0000269|PubMed:9083101}; DE AltName: Full=CTP:phosphoethanolamine cytidylyltransferase; DE AltName: Full=Phosphorylethanolamine transferase; GN Name=PCYT2; 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 PATHWAY, AND TISSUE SPECIFICITY. RX PubMed=9083101; DOI=10.1074/jbc.272.14.9567; RA Nakashima A., Hosaka K., Nikawa J.; RT "Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase RT by complementation in vivo of a yeast mutant."; RL J. Biol. Chem. 272:9567-9572(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, 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). RN [11] RP INVOLVEMENT IN SPG82, VARIANTS SPG82 TYR-226; LEU-289 AND 359-ARG--PHE-389 RP DEL, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=31637422; DOI=10.1093/brain/awz291; RG Deciphering Developmental Disorders Study; RA Vaz F.M., McDermott J.H., Alders M., Wortmann S.B., Koelker S., RA Pras-Raves M.L., Vervaart M.A.T., van Lenthe H., Luyf A.C.M., Elfrink H.L., RA Metcalfe K., Cuvertino S., Clayton P.E., Yarwood R., Lowe M.P., Lovell S., RA Rogers R.C., van Kampen A.H.C., Ruiter J.P.N., Wanders R.J.A., RA Ferdinandusse S., van Weeghel M., Engelen M., Banka S.; RT "Mutations in PCYT2 disrupt etherlipid biosynthesis and cause a complex RT hereditary spastic paraplegia."; RL Brain 142:3382-3397(2019). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-356 IN COMPLEX WITH RP CYTIDINE-5'-MONOPHOSPHATE. RG Structural genomics consortium (SGC); RT "Human CTP:phosphoethanolamine cytidylyltransferase."; RL Submitted (JUL-2011) to the PDB data bank. CC -!- FUNCTION: Ethanolamine-phosphate cytidylyltransferase that catalyzes CC the second step in the synthesis of phosphatidylethanolamine (PE) from CC ethanolamine via the CDP-ethanolamine pathway (PubMed:9083101, CC PubMed:31637422). Phosphatidylethanolamine is a dominant inner-leaflet CC phospholipid in cell membranes, where it plays a role in membrane CC function by structurally stabilizing membrane-anchored proteins, and CC participates in important cellular processes such as cell division, CC cell fusion, blood coagulation, and apoptosis (PubMed:9083101). CC {ECO:0000269|PubMed:31637422, ECO:0000269|PubMed:9083101, CC ECO:0000303|PubMed:9083101}. CC -!- CATALYTIC ACTIVITY: CC Reaction=CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + CC diphosphate; Xref=Rhea:RHEA:24592, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57876, CC ChEBI:CHEBI:58190; EC=2.7.7.14; CC Evidence={ECO:0000269|PubMed:31637422, ECO:0000269|PubMed:9083101}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24593; CC Evidence={ECO:0000269|PubMed:31637422, ECO:0000269|PubMed:9083101}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3. CC {ECO:0000269|PubMed:31637422, ECO:0000269|PubMed:9083101}. CC -!- INTERACTION: CC Q99447; P55212: CASP6; NbExp=3; IntAct=EBI-750317, EBI-718729; CC Q99447; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-750317, EBI-12357161; CC Q99447; Q0VD86: INCA1; NbExp=3; IntAct=EBI-750317, EBI-6509505; CC Q99447; P13473-2: LAMP2; NbExp=3; IntAct=EBI-750317, EBI-21591415; CC Q99447; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-750317, EBI-5280197; CC Q99447; P25786: PSMA1; NbExp=3; IntAct=EBI-750317, EBI-359352; CC Q99447; Q04864-2: REL; NbExp=3; IntAct=EBI-750317, EBI-10829018; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q99447-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99447-2; Sequence=VSP_045131; CC Name=3; CC IsoId=Q99447-3; Sequence=VSP_046844; CC Name=4; CC IsoId=Q99447-4; Sequence=VSP_054615; CC -!- TISSUE SPECIFICITY: Strongest expression in liver, heart, and skeletal CC muscle. {ECO:0000269|PubMed:9083101}. CC -!- DISEASE: Spastic paraplegia 82, autosomal recessive (SPG82) CC [MIM:618770]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness and CC spasticity of the lower limbs. Rate of progression and the severity of CC symptoms are quite variable. Initial symptoms may include difficulty CC with balance, weakness and stiffness in the legs, muscle spasms, and CC dragging the toes when walking. In some forms of the disorder, bladder CC symptoms (such as incontinence) may appear, or the weakness and CC stiffness may spread to other parts of the body. SPG82 is a complicated CC form characterized by global developmental delay with regression, CC spastic para- or tetraparesis, epilepsy and progressive cerebral and CC cerebellar atrophy. {ECO:0000269|PubMed:31637422}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the cytidylyltransferase 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; D84307; BAA12311.1; -; mRNA. DR EMBL; CR456779; CAG33060.1; -; mRNA. DR EMBL; AK301723; BAH13541.1; -; mRNA. DR EMBL; AK316385; BAH14756.1; -; mRNA. DR EMBL; AC145207; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471099; EAW89705.1; -; Genomic_DNA. DR EMBL; BC000351; AAH00351.1; -; mRNA. DR EMBL; BC010075; AAH10075.1; -; mRNA. DR CCDS; CCDS11791.1; -. [Q99447-1] DR CCDS; CCDS54178.1; -. [Q99447-3] DR CCDS; CCDS58610.1; -. [Q99447-2] DR CCDS; CCDS62364.1; -. [Q99447-4] DR RefSeq; NP_001171846.1; NM_001184917.2. [Q99447-3] DR RefSeq; NP_001243364.1; NM_001256435.2. [Q99447-2] DR RefSeq; NP_001269132.1; NM_001282203.1. [Q99447-2] DR RefSeq; NP_001269133.1; NM_001282204.1. [Q99447-4] DR RefSeq; NP_002852.1; NM_002861.4. [Q99447-1] DR RefSeq; XP_016880400.1; XM_017024911.1. DR PDB; 3ELB; X-ray; 2.00 A; A=18-356. DR PDB; 4XSV; X-ray; 2.70 A; A=18-356. DR PDBsum; 3ELB; -. DR PDBsum; 4XSV; -. DR AlphaFoldDB; Q99447; -. DR SMR; Q99447; -. DR BioGRID; 111791; 41. DR IntAct; Q99447; 17. DR MINT; Q99447; -. DR STRING; 9606.ENSP00000442050; -. DR DrugBank; DB00709; Lamivudine. DR iPTMnet; Q99447; -. DR PhosphoSitePlus; Q99447; -. DR BioMuta; PCYT2; -. DR DMDM; 12585314; -. DR EPD; Q99447; -. DR jPOST; Q99447; -. DR MassIVE; Q99447; -. DR MaxQB; Q99447; -. DR PaxDb; 9606-ENSP00000442050; -. DR PeptideAtlas; Q99447; -. DR ProteomicsDB; 27734; -. DR ProteomicsDB; 6845; -. DR ProteomicsDB; 7083; -. DR ProteomicsDB; 78273; -. [Q99447-1] DR Pumba; Q99447; -. DR Antibodypedia; 19846; 148 antibodies from 25 providers. DR DNASU; 5833; -. DR Ensembl; ENST00000331285.7; ENSP00000331719.3; ENSG00000185813.11. [Q99447-2] DR Ensembl; ENST00000538721.6; ENSP00000442050.2; ENSG00000185813.11. [Q99447-3] DR Ensembl; ENST00000538936.7; ENSP00000439245.3; ENSG00000185813.11. [Q99447-1] DR Ensembl; ENST00000570388.5; ENSP00000458330.1; ENSG00000185813.11. [Q99447-2] DR Ensembl; ENST00000570391.5; ENSP00000461190.1; ENSG00000185813.11. [Q99447-4] DR GeneID; 5833; -. DR KEGG; hsa:5833; -. DR MANE-Select; ENST00000538936.7; ENSP00000439245.3; NM_002861.5; NP_002852.1. DR UCSC; uc002kce.4; human. [Q99447-1] DR AGR; HGNC:8756; -. DR CTD; 5833; -. DR DisGeNET; 5833; -. DR GeneCards; PCYT2; -. DR HGNC; HGNC:8756; PCYT2. DR HPA; ENSG00000185813; Tissue enhanced (liver, testis). DR MalaCards; PCYT2; -. DR MIM; 602679; gene. DR MIM; 618770; phenotype. DR neXtProt; NX_Q99447; -. DR OpenTargets; ENSG00000185813; -. DR Orphanet; 631073; Autosomal recessive spastic paraplegia type 82. DR PharmGKB; PA33101; -. DR VEuPathDB; HostDB:ENSG00000185813; -. DR eggNOG; KOG2803; Eukaryota. DR GeneTree; ENSGT00550000075065; -. DR InParanoid; Q99447; -. DR OMA; QCKYINA; -. DR OrthoDB; 5474784at2759; -. DR PhylomeDB; Q99447; -. DR TreeFam; TF106337; -. DR BioCyc; MetaCyc:HS06840-MONOMER; -. DR BRENDA; 2.7.7.14; 2681. DR PathwayCommons; Q99447; -. DR Reactome; R-HSA-1483213; Synthesis of PE. DR SignaLink; Q99447; -. DR UniPathway; UPA00558; UER00742. DR BioGRID-ORCS; 5833; 52 hits in 1160 CRISPR screens. DR EvolutionaryTrace; Q99447; -. DR GenomeRNAi; 5833; -. DR Pharos; Q99447; Tbio. DR PRO; PR:Q99447; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q99447; Protein. DR Bgee; ENSG00000185813; Expressed in left testis and 180 other cell types or tissues. DR ExpressionAtlas; Q99447; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; IMP:UniProtKB. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:UniProtKB. DR GO; GO:0008654; P:phospholipid biosynthetic process; TAS:UniProtKB. DR CDD; cd02174; CCT; 1. DR CDD; cd02173; ECT; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR InterPro; IPR041723; CCT. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR044608; Ect1/PCYT2. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00125; cyt_tran_rel; 2. DR PANTHER; PTHR45780; ETHANOLAMINE-PHOSPHATE CYTIDYLYLTRANSFERASE; 1. DR PANTHER; PTHR45780:SF2; ETHANOLAMINE-PHOSPHATE CYTIDYLYLTRANSFERASE; 1. DR Pfam; PF01467; CTP_transf_like; 2. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 2. DR UCD-2DPAGE; Q99447; -. DR Genevisible; Q99447; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; KW Hereditary spastic paraplegia; Lipid biosynthesis; Lipid metabolism; KW Neurodegeneration; Nucleotidyltransferase; Phospholipid biosynthesis; KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..389 FT /note="Ethanolamine-phosphate cytidylyltransferase" FT /id="PRO_0000208461" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 221..222 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT BINDING 229..232 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT BINDING 259 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT BINDING 307..310 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT BINDING 336..340 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT MOD_RES 338 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 341 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 342 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O88637" FT VAR_SEQ 1..78 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045131" FT VAR_SEQ 1..32 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054615" FT VAR_SEQ 179 FT /note="K -> KPPHPIPAGDILSSEGCSQ (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_046844" FT VARIANT 226 FT /note="H -> Y (in SPG82; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31637422" FT /id="VAR_083888" FT VARIANT 289 FT /note="P -> L (in SPG82; uncertain significance; FT dbSNP:rs1204173741)" FT /evidence="ECO:0000269|PubMed:31637422" FT /id="VAR_083889" FT VARIANT 359..389 FT /note="Missing (in SPG82; decreased protein abundance; loss FT of ethanolamine-phosphate cytidylyltransferase activity)" FT /evidence="ECO:0000269|PubMed:31637422" FT /id="VAR_083890" FT CONFLICT 244 FT /note="Y -> H (in Ref. 6; AAH10075)" FT /evidence="ECO:0000305" FT STRAND 24..29 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 36..47 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 49..56 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 59..65 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 73..82 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 99..104 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 146..154 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 197..203 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 214..220 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 227..237 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 240..250 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 252..259 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 268..276 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 294..299 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 303..307 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 323..328 FT /evidence="ECO:0007829|PDB:3ELB" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:3ELB" FT HELIX 342..350 FT /evidence="ECO:0007829|PDB:3ELB" SQ SEQUENCE 389 AA; 43835 MW; 13FE8EAEB7FFAF7F CRC64; MIRNGRGAAG GAEQPGPGGR RAVRVWCDGC YDMVHYGHSN QLRQARAMGD YLIVGVHTDE EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE TLDKYNCDFC VHGNDITLTV DGRDTYEEVK QAGRYRECKR TQGVSTTDLV GRMLLVTKAH HSSQEMSSEY REYADSFGKC PGGRNPWTGV SQFLQTSQKI IQFASGKEPQ PGETVIYVAG AFDLFHIGHV DFLEKVHRLA ERPYIIAGLH FDQEVNHYKG KNYPIMNLHE RTLSVLACRY VSEVVIGAPY AVTAELLSHF KVDLVCHGKT EIIPDRDGSD PYQEPKRRGI FRQIDSGSNL TTDLIVQRII TNRLEYEARN QKKEAKELAF LEAARQQAAQ PLGERDGDF //