ID PISD_HUMAN Reviewed; 409 AA. AC Q9UG56; B1AKM7; O43207; O95535; Q6IC28; Q96GQ2; Q9UGA9; DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 4. DT 27-MAR-2024, entry version 182. DE RecName: Full=Phosphatidylserine decarboxylase proenzyme, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208}; DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:30858161}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_03208}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_03208}; DE Flags: Precursor; GN Name=PISD {ECO:0000255|HAMAP-Rule:MF_03208}; 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] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Neuroblastoma, and Rhabdomyosarcoma; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-409. RC TISSUE=Brain; RA Yu W., Sarginson J., Gibbs R.A.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [7] RP INVOLVEMENT IN LIBF. RX PubMed=31263216; DOI=10.1038/s41436-019-0595-x; RA Peter V.G., Quinodoz M., Pinto-Basto J., Sousa S.B., Di Gioia S.A., RA Soares G., Ferraz Leal G., Silva E.D., Pescini Gobert R., Miyake N., RA Matsumoto N., Engle E.C., Unger S., Shapiro F., Superti-Furga A., RA Rivolta C., Campos-Xavier B.; RT "The Liberfarb syndrome, a multisystem disorder affecting eye, ear, bone, RT and brain development, is caused by a founder pathogenic variant in thePISD RT gene."; RL Genet. Med. 21:2734-2743(2019). RN [8] RP INVOLVEMENT IN LIBF, VARIANT LIBF TYR-300, CHARACTERIZATION OF VARIANT LIBF RP TYR-300, AND FUNCTION. RX PubMed=30488656; DOI=10.1002/humu.23693; RA Girisha K.M., von Elsner L., Neethukrishna K., Muranjan M., Shukla A., RA Bhavani G.S., Nishimura G., Kutsche K., Mortier G.; RT "The homozygous variant c.797G>A/p.(Cys266Tyr) in PISD is associated with a RT Spondyloepimetaphyseal dysplasia with large epiphyses and disturbed RT mitochondrial function."; RL Hum. Mutat. 40:299-309(2019). RN [9] RP VARIANT LIBF GLN-277, CHARACTERIZATION OF VARIANTS LIBF GLN-277 AND RP TYR-300, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF SER-378. RX PubMed=30858161; DOI=10.26508/lsa.201900353; RG Care4Rare Canada Consortium; RA Zhao T., Goedhart C.M., Sam P.N., Sabouny R., Lingrell S., Cornish A.J., RA Lamont R.E., Bernier F.P., Sinasac D., Parboosingh J.S., Vance J.E., RA Claypool S.M., Innes A.M., Shutt T.E.; RT "PISD is a mitochondrial disease gene causing skeletal dysplasia, RT cataracts, and white matter changes."; RL Life. Sci Alliance 2:0-0(2019). RN [10] RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2). RX PubMed=33593792; DOI=10.1242/bio.058516; RA Kumar S., Chitraju C., Farese R.V. Jr., Walther T.C., Burd C.G.; RT "Conditional targeting of phosphatidylserine decarboxylase to lipid RT droplets."; RL Biol. Open 10:bio058516-bio058516(2021). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=33718843; DOI=10.1016/j.isci.2021.102196; RA Sam P.N., Calzada E., Acoba M.G., Zhao T., Watanabe Y., Nejatfard A., RA Trinidad J.C., Shutt T.E., Neal S.E., Claypool S.M.; RT "Impaired phosphatidylethanolamine metabolism activates a reversible stress RT response that detects and resolves mutant mitochondrial precursors."; RL IScience 24:102196-102196(2021). CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) CC from phosphatidylserine (PtdSer) (PubMed:30488656, PubMed:30858161). CC Plays a central role in phospholipid metabolism and in the CC interorganelle trafficking of phosphatidylserine. May be involved in CC lipid droplet biogenesis at the endoplasmic reticulum membrane (By CC similarity). {ECO:0000250|UniProtKB:A0A8H4BVL9, ECO:0000255|HAMAP- CC Rule:MF_03208, ECO:0000269|PubMed:30488656, CC ECO:0000269|PubMed:30858161}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2- CC diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, CC ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03208, ECO:0000269|PubMed:30858161}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20829; CC Evidence={ECO:0000269|PubMed:30858161}; CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03208}; CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP- CC Rule:MF_03208}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis. {ECO:0000269|PubMed:30858161}. CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP- CC Rule:MF_03208}. CC -!- INTERACTION: CC Q9UG56-2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-17870882, EBI-7062247; CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]: CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, CC ECO:0000305|PubMed:30858161, ECO:0000305|PubMed:33718843}; Single-pass CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side CC {ECO:0000255|HAMAP-Rule:MF_03208}. CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]: CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, CC ECO:0000305|PubMed:30858161, ECO:0000305|PubMed:33718843}; Peripheral CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side CC {ECO:0000255|HAMAP-Rule:MF_03208}. Cytoplasm CC {ECO:0000269|PubMed:33593792}. Note=Anchored to the mitochondrial inner CC membrane through its interaction with the integral membrane beta chain. CC {ECO:0000255|HAMAP-Rule:MF_03208}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane CC {ECO:0000269|PubMed:33593792}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane CC {ECO:0000269|PubMed:33593792}. Lipid droplet CC {ECO:0000269|PubMed:33593792}. Note=Predominantly localizes to lipid CC droplets in lipid-replete conditions, and to mitochondria in lipid- CC deplete conditions. {ECO:0000269|PubMed:33593792}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=PISD-M {ECO:0000303|PubMed:33593792}; CC IsoId=Q9UG56-3; Sequence=Displayed; CC Name=2; Synonyms=PISD-LD {ECO:0000303|PubMed:33593792}; CC IsoId=Q9UG56-2; Sequence=VSP_007540; CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of CC the active enzyme involves a self-maturation process in which the CC active site pyruvoyl group is generated from an internal serine residue CC via an autocatalytic post-translational modification. Two non-identical CC subunits are generated from the proenzyme in this reaction, and the CC pyruvate is formed at the N-terminus of the alpha chain, which is CC derived from the carboxyl end of the proenzyme. The autoendoproteolytic CC cleavage occurs by a canonical serine protease mechanism, in which the CC side chain hydroxyl group of the serine supplies its oxygen atom to CC form the C-terminus of the beta chain, while the remainder of the CC serine residue undergoes an oxidative deamination to produce ammonia CC and the pyruvoyl prosthetic group on the alpha chain. During this CC reaction, the Ser that is part of the protease active site of the CC proenzyme becomes the pyruvoyl prosthetic group, which constitutes an CC essential element of the active site of the mature decarboxylase. CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:30858161}. CC -!- DISEASE: Liberfarb syndrome (LIBF) [MIM:618889]: An autosomal recessive CC multisystem disorder affecting the eye, ear, bone, and brain CC development. Clinical features include early-onset retinal CC degeneration, congenital cataracts, sensorineural hearing loss, CC microcephaly, intellectual disability, white matter changes, mild CC facial dysmorphism, and skeletal dysplasia with platyspondyly, CC scoliosis and short stature. {ECO:0000269|PubMed:30488656, CC ECO:0000269|PubMed:30858161, ECO:0000269|PubMed:31263216}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000255|HAMAP- CC Rule:MF_03208}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB43678.2; Type=Erroneous translation; Evidence={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; CR456540; CAG30426.1; -; mRNA. DR EMBL; AL050371; CAB43678.2; ALT_SEQ; Transcribed_RNA. DR EMBL; AL096768; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031255; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471095; EAW59984.1; -; Genomic_DNA. DR EMBL; BC001482; AAH01482.1; -; mRNA. DR EMBL; BC009315; AAH09315.1; -; mRNA. DR EMBL; AF035304; AAB88186.1; -; mRNA. DR CCDS; CCDS13899.1; -. [Q9UG56-2] DR CCDS; CCDS87016.1; -. [Q9UG56-3] DR RefSeq; NP_001313340.1; NM_001326411.1. [Q9UG56-3] DR RefSeq; NP_001313344.1; NM_001326415.1. [Q9UG56-2] DR RefSeq; NP_001313345.1; NM_001326416.1. [Q9UG56-2] DR RefSeq; NP_001313346.1; NM_001326417.1. [Q9UG56-2] DR RefSeq; NP_055153.1; NM_014338.3. [Q9UG56-2] DR RefSeq; NP_821141.1; NM_178022.1. [Q9UG56-2] DR AlphaFoldDB; Q9UG56; -. DR SMR; Q9UG56; -. DR BioGRID; 117262; 92. DR IntAct; Q9UG56; 12. DR MINT; Q9UG56; -. DR STRING; 9606.ENSP00000391739; -. DR DrugBank; DB00144; Phosphatidyl serine. DR iPTMnet; Q9UG56; -. DR PhosphoSitePlus; Q9UG56; -. DR BioMuta; PISD; -. DR DMDM; 311033492; -. DR EPD; Q9UG56; -. DR jPOST; Q9UG56; -. DR MassIVE; Q9UG56; -. DR MaxQB; Q9UG56; -. DR PaxDb; 9606-ENSP00000371586; -. DR PeptideAtlas; Q9UG56; -. DR ProteomicsDB; 84200; -. [Q9UG56-3] DR ProteomicsDB; 84201; -. [Q9UG56-2] DR Pumba; Q9UG56; -. DR Antibodypedia; 34990; 326 antibodies from 27 providers. DR DNASU; 23761; -. DR Ensembl; ENST00000266095.9; ENSP00000266095.5; ENSG00000241878.12. [Q9UG56-2] DR Ensembl; ENST00000382151.6; ENSP00000371586.2; ENSG00000241878.12. [Q9UG56-2] DR Ensembl; ENST00000439502.7; ENSP00000391739.2; ENSG00000241878.12. [Q9UG56-3] DR GeneID; 23761; -. DR KEGG; hsa:23761; -. DR MANE-Select; ENST00000439502.7; ENSP00000391739.2; NM_001326411.2; NP_001313340.1. DR UCSC; uc003alk.3; human. [Q9UG56-3] DR AGR; HGNC:8999; -. DR CTD; 23761; -. DR DisGeNET; 23761; -. DR GeneCards; PISD; -. DR HGNC; HGNC:8999; PISD. DR HPA; ENSG00000241878; Low tissue specificity. DR MalaCards; PISD; -. DR MIM; 612770; gene. DR MIM; 618889; phenotype. DR neXtProt; NX_Q9UG56; -. DR OpenTargets; ENSG00000241878; -. DR Orphanet; 589442; Short stature-skeletal dysplasia-retinal degeneration-intellectual disability-sensorineural hearing loss syndrome. DR PharmGKB; PA33333; -. DR VEuPathDB; HostDB:ENSG00000241878; -. DR eggNOG; KOG2420; Eukaryota. DR GeneTree; ENSGT00390000013484; -. DR HOGENOM; CLU_029061_3_0_1; -. DR InParanoid; Q9UG56; -. DR OMA; KDYHHYH; -. DR OrthoDB; 1216391at2759; -. DR PhylomeDB; Q9UG56; -. DR TreeFam; TF313148; -. DR BioCyc; MetaCyc:HS01985-MONOMER; -. DR PathwayCommons; Q9UG56; -. DR Reactome; R-HSA-1483213; Synthesis of PE. DR SignaLink; Q9UG56; -. DR UniPathway; UPA00558; -. DR BioGRID-ORCS; 23761; 532 hits in 1169 CRISPR screens. DR ChiTaRS; PISD; human. DR GeneWiki; PISD_(gene); -. DR GenomeRNAi; 23761; -. DR Pharos; Q9UG56; Tbio. DR PRO; PR:Q9UG56; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q9UG56; Protein. DR Bgee; ENSG00000241878; Expressed in cerebellar hemisphere and 190 other cell types or tissues. DR ExpressionAtlas; Q9UG56; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:LIFEdb. DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IMP:UniProtKB. DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB. DR GO; GO:0035694; P:mitochondrial protein catabolic process; IMP:UniProtKB. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:UniProtKB. DR GO; GO:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule. DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB. DR HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1. DR InterPro; IPR003817; PS_Dcarbxylase. DR InterPro; IPR033177; PSD-B. DR InterPro; IPR033661; PSD_type1_euk. DR NCBIfam; TIGR00163; PS_decarb; 1. DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1. DR PANTHER; PTHR10067:SF6; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL; 1. DR Pfam; PF02666; PS_Dcarbxylase; 1. DR Genevisible; Q9UG56; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cataract; Cytoplasm; Deafness; Decarboxylase; KW Disease variant; Dwarfism; Intellectual disability; Lipid biosynthesis; KW Lipid droplet; Lipid metabolism; Lyase; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Pyruvate; Reference proteome; Transit peptide; KW Transmembrane; Transmembrane helix. FT TRANSIT 1..52 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 53..409 FT /note="Phosphatidylserine decarboxylase proenzyme, FT mitochondrial" FT /id="PRO_0000435571" FT CHAIN 53..377 FT /note="Phosphatidylserine decarboxylase beta chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT /id="PRO_0000029835" FT CHAIN 378..409 FT /note="Phosphatidylserine decarboxylase alpha chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT /id="PRO_0000029836" FT TOPO_DOM 53..63 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT TRANSMEM 64..82 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT TOPO_DOM 83..409 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT ACT_SITE 191 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT ACT_SITE 267 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT ACT_SITE 378 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT ACT_SITE 378 FT /note="Schiff-base intermediate with substrate; via pyruvic FT acid; for decarboxylase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT SITE 377..378 FT /note="Cleavage (non-hydrolytic); by autocatalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT MOD_RES 378 FT /note="Pyruvic acid (Ser); by autocatalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208" FT VAR_SEQ 1..107 FT /note="MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARK FT IHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWE -> FT MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGA FT LRPLSRVGWRPVSR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007540" FT VARIANT 277 FT /note="R -> Q (in LIBF; loss of autocatalytic processing; FT decreased protein abundance; decreased phosphatidylserine FT decarboxylase activity; changed mitochondrion organization; FT dbSNP:rs147371584)" FT /evidence="ECO:0000269|PubMed:30858161" FT /id="VAR_084458" FT VARIANT 300 FT /note="C -> Y (in LIBF; loss of autocatalytic processing; FT probably decreased phosphatidylserine decarboxylase FT activity; changed mitochondrion organization; FT patient-derived fibroblasts show fragmented mitochondrial FT morphology around the nucleus; decreased cell viability FT with increased CASP3 and CASP7 activation; FT dbSNP:rs2072505076)" FT /evidence="ECO:0000269|PubMed:30488656, FT ECO:0000269|PubMed:30858161" FT /id="VAR_084459" FT MUTAGEN 378 FT /note="S->A: Loss of autocatalytic processing." FT /evidence="ECO:0000269|PubMed:30858161" FT REGION Q9UG56-2:36..103 FT /note="Necessary for localization to both lipid droplets FT and mitochondria" FT /evidence="ECO:0000269|PubMed:33593792" SQ SEQUENCE 409 AA; 46672 MW; 6A5148265369D9DF CRC64; MATSVGHRCL GLLHGVAPWR SSLHPCEITA LSQSLQPLRK LPFRAFRTDA RKIHTAPART MFLLRPLPIL LVTGGGYAGY RQYEKYRERE LEKLGLEIPP KLAGHWEVAL YKSVPTRLLS RAWGRLNQVE LPHWLRRPVY SLYIWTFGVN MKEAAVEDLH HYRNLSEFFR RKLKPQARPV CGLHSVISPS DGRILNFGQV KNCEVEQVKG VTYSLESFLG PRMCTEDLPF PPAASCDSFK NQLVTREGNE LYHCVIYLAP GDYHCFHSPT DWTVSHRRHF PGSLMSVNPG MARWIKELFC HNERVVLTGD WKHGFFSLTA VGATNVGSIR IYFDRDLHTN SPRHSKGSYN DFSFVTHTNR EGVPMRKGEH LGEFNLGSTI VLIFEAPKDF NFQLKTGQKI RFGEALGSL //