PISD_HUMAN
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 03-AUG-2022, entry version 173.
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).
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. {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;
CC Evidence={ECO:0000255|HAMAP-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}; Single-pass membrane protein
CC {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}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side
CC {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial
CC inner membrane through its interaction with the integral membrane beta
CC chain. {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UG56-3; Sequence=Displayed;
CC Name=2;
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};
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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; 84.
DR IntAct; Q9UG56; 11.
DR STRING; 9606.ENSP00000371586; -.
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; Q9UG56; -.
DR PeptideAtlas; Q9UG56; -.
DR PRIDE; Q9UG56; -.
DR ProteomicsDB; 84200; -. [Q9UG56-3]
DR ProteomicsDB; 84201; -. [Q9UG56-2]
DR Antibodypedia; 34990; 278 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 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; AIEWQLH; -.
DR OrthoDB; 1226492at2759; -.
DR PhylomeDB; Q9UG56; -.
DR TreeFam; TF313148; -.
DR BioCyc; MetaCyc:HS01985-MON; -.
DR PathwayCommons; Q9UG56; -.
DR Reactome; R-HSA-1483213; Synthesis of PE.
DR SignaLink; Q9UG56; -.
DR UniPathway; UPA00558; -.
DR BioGRID-ORCS; 23761; 506 hits in 1090 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 188 other tissues.
DR ExpressionAtlas; Q9UG56; baseline and differential.
DR Genevisible; Q9UG56; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
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: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.
DR InterPro; IPR033661; PSD_type1_euk.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cataract; Deafness; Decarboxylase; Disease variant;
KW Dwarfism; Intellectual disability; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zymogen.
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; patient-
FT derived fibroblasts show fragmented mitochondrial
FT morphology around the nucleus; decreased cell viability
FT with increased CASP3 and CASP7 activation)"
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"
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
