PLS1_MOUSE
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 03-AUG-2022, entry version 166.
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).
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 {ECO:0000250|UniProtKB:O15162, 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). {ECO:0000269|PubMed:12010804}.
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};
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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; Q9JJ00; -.
DR PRIDE; Q9JJ00; -.
DR ProteomicsDB; 289625; -.
DR DNASU; 22038; -.
DR Ensembl; ENSMUST00000093801; ENSMUSP00000091318; ENSMUSG00000032369.
DR Ensembl; ENSMUST00000186364; ENSMUSP00000139479; ENSMUSG00000032369.
DR GeneID; 22038; -.
DR KEGG; mmu:22038; -.
DR UCSC; uc009ram.2; mouse.
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; 1015148at2759; -.
DR PhylomeDB; Q9JJ00; -.
DR TreeFam; TF314939; -.
DR BRENDA; 7.6.2.1; 3474.
DR BioGRID-ORCS; 22038; 1 hit in 75 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 68 other tissues.
DR Genevisible; Q9JJ00; MM.
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:0005887; C:integral component of plasma membrane; 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:0032091; P:negative regulation of protein binding; IDA:MGI.
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; PTHR23248; 1.
DR Pfam; PF03803; Scramblase; 1.
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
