ID PLS1_MOUSE Reviewed; 328 AA. AC Q9JJ00; O54730; O54731; Q9D1F8; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 174. DE RecName: Full=Phospholipid scramblase 1; DE Short=PL scramblase 1; DE AltName: Full=Ca(2+)-dependent phospholipid scramblase 1; DE AltName: Full=Mg(2+)-dependent nuclease {ECO:0000250|UniProtKB:O15162}; DE EC=3.1.-.- {ECO:0000250|UniProtKB:O15162}; DE AltName: Full=Transplantability-associated protein 1; DE Short=NOR1; DE Short=TRA1; GN Name=Plscr1; Synonyms=Tra1b, Tras1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10930526; DOI=10.1016/s0005-2736(00)00236-4; RA Wiedmer T., Zhou Q., Kwoh D.Y., Sims P.J.; RT "Identification of three new members of the phospholipid scramblase gene RT family."; RL Biochim. Biophys. Acta 1467:244-253(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-328, AND CHROMOSOMAL TRANSLOCATION. RC STRAIN=BALB/cJ; TISSUE=Kidney; RX PubMed=9108418; RA Kasukabe T., Okabe-Kado J., Honma Y.; RT "TRA1, a novel mRNA highly expressed in leukemogenic mouse monocytic RT sublines but not in nonleukemogenic sublines."; RL Blood 89:2975-2985(1997). RN [4] RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12010804; DOI=10.1182/blood-2001-12-0271; RA Zhou Q., Zhao J., Wiedmer T., Sims P.J.; RT "Normal hemostasis but defective hematopoietic response to growth factors RT in mice deficient in phospholipid scramblase 1."; RL Blood 99:4030-4038(2002). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP FUNCTION. RX PubMed=26745724; DOI=10.1371/journal.pone.0145617; RA Herate C., Ramdani G., Grant N.J., Marion S., Gasman S., Niedergang F., RA Benichou S., Bouchet J.; RT "Phospholipid Scramblase 1 Modulates FcR-Mediated Phagocytosis in RT Differentiated Macrophages."; RL PLoS ONE 11:e0145617-e0145617(2016). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TRPC1; TRPC4 AND TRPC5. RX PubMed=32110987; DOI=10.3390/cells9030547; RA Guo J., Li J., Xia L., Wang Y., Zhu J., Du J., Lu Y., Liu G., Yao X., RA Shen B.; RT "Transient Receptor Potential Canonical 5-Scramblase Signaling Complex RT Mediates Neuronal Phosphatidylserine Externalization and Apoptosis."; RL Cells 9:0-0(2020). RN [8] RP DISRUPTION PHENOTYPE. RX PubMed=35595813; DOI=10.1038/s41598-022-12598-3; RA Liu Y., Lin S., Xie Y., Zhao L., Du H., Yang S., Yin B., Li G., Zhao Z., RA Huang Z., Xu Z., Wu J.; RT "ILDR1 promotes influenza A virus replication through binding to PLSCR1."; RL Sci. Rep. 12:8515-8515(2022). CC -!- FUNCTION: Catalyzes calcium-induced ATP-independent rapid bidirectional CC and non-specific distribution of phospholipids (lipid scrambling or CC lipid flip-flop) between the inner and outer leaflet of the plasma CC membrane resulting in collapse of the phospholipid asymmetry which CC leads to phosphatidylserine externalization on the cell surface CC (PubMed:32110987). Mediates calcium-dependent phosphatidylserine CC externalization and apoptosis in neurons via its association with TRPC5 CC (PubMed:32110987). Also exhibits magnesium-dependent nuclease activity CC against double-stranded DNA and RNA but not single-stranded DNA and can CC enhance DNA decatenation mediated by TOP2A (By similarity). Negatively CC regulates FcR-mediated phagocytosis in differentiated macrophages CC (PubMed:26745724). May contribute to cytokine-regulated cell CC proliferation and differentiation (PubMed:12010804). CC {ECO:0000250|UniProtKB:O15162, ECO:0000269|PubMed:12010804, CC ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:32110987}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl- CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:O15162}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; CC Evidence={ECO:0000250|UniProtKB:O15162}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573; CC Evidence={ECO:0000250|UniProtKB:O15162}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2- CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:O15162}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896; CC Evidence={ECO:0000250|UniProtKB:O15162}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl- CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, CC ChEBI:CHEBI:57262; Evidence={ECO:0000305|PubMed:32110987}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664; CC Evidence={ECO:0000305|PubMed:32110987}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38665; CC Evidence={ECO:0000250|UniProtKB:O15162}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000250|UniProtKB:O15162}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:O15162}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:O15162}; CC Note=Magnesium. Can also use zinc with lower efficiency. CC {ECO:0000250|UniProtKB:O15162}; CC -!- SUBUNIT: Forms homooligomers in the presence of calcium (By CC similarity). Interacts with ABL (By similarity). Interacts with RELT, CC RELL1 and RELL2 (By similarity). Interacts with OXSR1 in the presence CC of RELT (By similarity). Interacts with OCLN, TOP2A and TOP2B (By CC similarity). Interacts with TRPC1, TRPC4 and TRPC5 (PubMed:32110987). CC Interacts with ILDR1 (By similarity). {ECO:0000250|UniProtKB:O15162, CC ECO:0000269|PubMed:32110987}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15162}; CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15162}. CC Cell membrane {ECO:0000250|UniProtKB:O15162}; Lipid-anchor CC {ECO:0000250|UniProtKB:O15162}; Cytoplasmic side. Nucleus CC {ECO:0000250|UniProtKB:O15162}. Cytoplasm CC {ECO:0000250|UniProtKB:O15162}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:O15162}. Note=Localizes to the perinuclear CC region in the presence of RELT. Palmitoylation regulates its CC localization to the cell membrane or the nucleus; trafficking to the CC cell membrane is dependent upon palmitoylation whereas in the absence CC of palmitoylation, localizes to the nucleus. CC {ECO:0000250|UniProtKB:O15162}. CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, lung, liver and bone CC marrow, slightly in spleen, heart and macrophage. CC -!- INDUCTION: Up-regulated by SCF/KITL and GCSF/CSF3. CC {ECO:0000269|PubMed:12010804}. CC -!- DOMAIN: The N-terminal proline-rich domain (PRD) is required for CC phospholipid scramblase activity. {ECO:0000250|UniProtKB:O15162}. CC -!- DOMAIN: The transmembrane domain is essential for membrane insertion, CC phospholipid scramblase activity and proper calcium-binding. CC {ECO:0000250|UniProtKB:O15162}. CC -!- PTM: Phosphorylation at Thr-170 by PKC/PKCD increases its phospholipid CC scramblase activity during both cell stimulation and apoptosis (By CC similarity). Phosphorylated by OXSR1 in the presence of RELT (By CC similarity). {ECO:0000250|UniProtKB:O15162}. CC -!- PTM: Palmitoylation is required for its phospholipid scramblase CC activity (By similarity). Palmitoylation regulates its localization to CC the cell membrane or the nucleus; trafficking to the cell membrane is CC dependent upon palmitoylation whereas in the absence of palmitoylation, CC localizes to the nucleus (By similarity). CC {ECO:0000250|UniProtKB:O15162}. CC -!- DISEASE: Note=Participates in a chromosomal translocation that produces CC MMTRA1A which is leukemogenic to syngenic SL mice and athymic nude CC mice. CC -!- DISRUPTION PHENOTYPE: Knockout newborn mice display a reduced CC granulocyte production (PubMed:12010804). Hematopoietic precursor cell CC from knockout mice display defective colony formation and impaired CC differentiation to mature granulocytes as stimulated by SCF/KITL and CC GCSF/CSF3 (PubMed:12010804). Deletion mutant mice start to die at 3 CC days post-infection after influenza H1N1 challenge, and the survival CC rate drops to 50% at 28 days post-infection showing lower survival rate CC than WT mice. {ECO:0000269|PubMed:12010804, CC ECO:0000269|PubMed:35595813}. CC -!- SIMILARITY: Belongs to the phospholipid scramblase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA23663.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA23664.1; Type=Frameshift; 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; AF159593; AAF77076.1; -; mRNA. DR EMBL; AK003628; BAB22897.1; -; mRNA. DR EMBL; D78354; BAA23663.1; ALT_INIT; mRNA. DR EMBL; D78355; BAA23664.1; ALT_FRAME; mRNA. DR CCDS; CCDS52886.1; -. DR RefSeq; NP_035766.2; NM_011636.2. DR RefSeq; XP_006511115.1; XM_006511052.3. DR AlphaFoldDB; Q9JJ00; -. DR BioGRID; 204311; 2. DR IntAct; Q9JJ00; 1. DR STRING; 10090.ENSMUSP00000091318; -. DR SwissLipids; SLP:000000348; -. DR iPTMnet; Q9JJ00; -. DR PhosphoSitePlus; Q9JJ00; -. DR SwissPalm; Q9JJ00; -. DR EPD; Q9JJ00; -. DR jPOST; Q9JJ00; -. DR MaxQB; Q9JJ00; -. DR PaxDb; 10090-ENSMUSP00000091318; -. DR ProteomicsDB; 289625; -. DR Pumba; Q9JJ00; -. DR DNASU; 22038; -. DR Ensembl; ENSMUST00000093801.10; ENSMUSP00000091318.4; ENSMUSG00000032369.14. DR Ensembl; ENSMUST00000186364.2; ENSMUSP00000139479.2; ENSMUSG00000032369.14. DR GeneID; 22038; -. DR KEGG; mmu:22038; -. DR UCSC; uc009ram.2; mouse. DR AGR; MGI:893575; -. DR CTD; 5359; -. DR MGI; MGI:893575; Plscr1. DR VEuPathDB; HostDB:ENSMUSG00000032369; -. DR eggNOG; KOG0621; Eukaryota. DR GeneTree; ENSGT00940000154435; -. DR HOGENOM; CLU_053024_2_0_1; -. DR InParanoid; Q9JJ00; -. DR OMA; QNWHLWR; -. DR OrthoDB; 4390at2759; -. DR PhylomeDB; Q9JJ00; -. DR TreeFam; TF314939; -. DR BRENDA; 7.6.2.1; 3474. DR BioGRID-ORCS; 22038; 1 hit in 80 CRISPR screens. DR ChiTaRS; Plscr1; mouse. DR PRO; PR:Q9JJ00; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q9JJ00; Protein. DR Bgee; ENSMUSG00000032369; Expressed in ileum and 70 other cell types or tissues. DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0042609; F:CD4 receptor binding; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0032791; F:lead ion binding; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0045340; F:mercury ion binding; ISS:UniProtKB. DR GO; GO:0004518; F:nuclease activity; ISS:UniProtKB. DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB. DR GO; GO:0001618; F:virus receptor activity; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0006953; P:acute-phase response; IEP:UniProtKB. DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEP:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB. DR GO; GO:0006955; P:immune response; ISO:MGI. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:UniProtKB. DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI. DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB. DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IDA:UniProtKB. DR GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; IDA:MGI. DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI. DR GO; GO:1905820; P:positive regulation of chromosome separation; ISS:UniProtKB. DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB. DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB. DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; ISS:UniProtKB. DR GO; GO:0033003; P:regulation of mast cell activation; ISS:UniProtKB. DR GO; GO:0035455; P:response to interferon-alpha; IMP:UniProtKB. DR InterPro; IPR005552; Scramblase. DR PANTHER; PTHR23248:SF38; PHOSPHOLIPID SCRAMBLASE 1; 1. DR PANTHER; PTHR23248; PHOSPHOLIPID SCRAMBLASE-RELATED; 1. DR Pfam; PF03803; Scramblase; 1. DR Genevisible; Q9JJ00; MM. PE 1: Evidence at protein level; KW Calcium; Cell membrane; Chromosomal rearrangement; Cytoplasm; DNA-binding; KW Hydrolase; Lipid transport; Lipoprotein; Membrane; Nuclease; Nucleus; KW Palmitate; Phosphoprotein; Reference proteome; Repeat; SH3-binding; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..328 FT /note="Phospholipid scramblase 1" FT /id="PRO_0000100785" FT TOPO_DOM 1..297 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O15162" FT TRANSMEM 298..314 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 315..328 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:O15162" FT REGION 1..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1..93 FT /note="Proline-rich domain (PRD)" FT /evidence="ECO:0000250|UniProtKB:O15162" FT MOTIF 18..26 FT /note="SH3-binding 1" FT /evidence="ECO:0000255" FT MOTIF 22..25 FT /note="PPxY motif" FT /evidence="ECO:0000255" FT MOTIF 56..64 FT /note="SH3-binding 2" FT /evidence="ECO:0000255" FT MOTIF 93..101 FT /note="SH3-binding 3" FT /evidence="ECO:0000255" FT MOTIF 269..275 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:O15162" FT COMPBIAS 16..30 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 45..65 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 127..128 FT /note="Breakpoint for translocation to form MMTRA1A" FT MOD_RES 83 FT /note="Phosphotyrosine; by ABL" FT /evidence="ECO:0000250|UniProtKB:O15162" FT MOD_RES 170 FT /note="Phosphothreonine; by PKC/PRKCD" FT /evidence="ECO:0000250|UniProtKB:O15162" FT LIPID 193 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:O15162" FT LIPID 194 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:O15162" FT LIPID 197 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:O15162" FT LIPID 198 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:O15162" FT CONFLICT 24..27 FT /note="PYPP -> GLCV (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="T -> A (in Ref. 2; BAB22897)" FT /evidence="ECO:0000305" FT CONFLICT 267 FT /note="K -> R (in Ref. 2; BAB22897)" FT /evidence="ECO:0000305" SQ SEQUENCE 328 AA; 35914 MW; 6CA35DF8DBF72ACF CRC64; MENHSKQTEA PHPGTYMPAG YPPPYPPAAF QGPSDHAAYP IPQAGYQGPP GPYPGPQPGY PVPPGGYAGG GPSGFPVQNQ PAYNHPGGPG GTPWMPAPPP PLNCPPGLEY LAQIDQLLVH QQIELLEVLT GFETNNKYEI KNSLGQRVYF AVEDTDCCTR NCCGASRPFT LRILDNLGRE VMTLERPLRC SSCCFPCCLQ EIEIQAPPGV PVGYVTQTWH PCLPKFTLQN EKKQDVLKVV GPCVVCSCCS DIDFELKSLD EESVVGKISK QWSGFVREAF TDADNFGIQF PLDLDVKMKA VMLGACFLID FMFFERTGNE EQRSGAWQ //