PCY2_HUMAN
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 03-AUG-2022, entry version 188.
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}.
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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. [Q99447-4]
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; 32.
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 UCD-2DPAGE; Q99447; -.
DR EPD; Q99447; -.
DR jPOST; Q99447; -.
DR MassIVE; Q99447; -.
DR MaxQB; Q99447; -.
DR PaxDb; Q99447; -.
DR PeptideAtlas; Q99447; -.
DR PRIDE; Q99447; -.
DR ProteomicsDB; 27734; -.
DR ProteomicsDB; 6845; -.
DR ProteomicsDB; 7083; -.
DR ProteomicsDB; 78273; -. [Q99447-1]
DR Antibodypedia; 19846; 131 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 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 PharmGKB; PA33101; -.
DR VEuPathDB; HostDB:ENSG00000185813; -.
DR eggNOG; KOG2803; Eukaryota.
DR GeneTree; ENSGT00550000075065; -.
DR InParanoid; Q99447; -.
DR OMA; VLQCKYI; -.
DR OrthoDB; 871204at2759; -.
DR PhylomeDB; Q99447; -.
DR TreeFam; TF106337; -.
DR BioCyc; MetaCyc:HS06840-MON; -.
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; 48 hits in 1082 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 178 other tissues.
DR ExpressionAtlas; Q99447; baseline and differential.
DR Genevisible; Q99447; HS.
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 Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR45780; PTHR45780; 1.
DR Pfam; PF01467; CTP_transf_like; 2.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 2.
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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31637422"
FT /id="VAR_083888"
FT VARIANT 289
FT /note="P -> L (in SPG82; unknown pathological 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
