SGPL1_MOUSE
ID SGPL1_MOUSE Reviewed; 568 AA.
AC Q8R0X7; O54955; Q8C942;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Sphingosine-1-phosphate lyase 1 {ECO:0000305};
DE Short=S1PL;
DE Short=SP-lyase 1;
DE Short=SPL 1;
DE Short=mSPL {ECO:0000303|PubMed:15522238};
DE EC=4.1.2.27 {ECO:0000269|PubMed:9464245};
DE AltName: Full=Sphingosine-1-phosphate aldolase;
GN Name=Sgpl1 {ECO:0000312|MGI:MGI:1261415};
GN Synonyms=Spl {ECO:0000303|PubMed:15522238};
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=9464245; DOI=10.1006/bbrc.1997.7993;
RA Zhou J., Saba J.D.;
RT "Identification of the first mammalian sphingosine phosphate lyase gene and
RT its functional expression in yeast.";
RL Biochem. Biophys. Res. Commun. 242:502-507(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, TOPOLOGY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15522238; DOI=10.1016/j.bbrc.2004.10.036;
RA Ikeda M., Kihara A., Igarashi Y.;
RT "Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident,
RT integral membrane protein with the pyridoxal 5'-phosphate binding domain
RT exposed to the cytosol.";
RL Biochem. Biophys. Res. Commun. 325:338-343(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=20097939; DOI=10.1074/jbc.m109.081489;
RA Bektas M., Allende M.L., Lee B.G., Chen W., Amar M.J., Remaley A.T.,
RA Saba J.D., Proia R.L.;
RT "Sphingosine 1-phosphate lyase deficiency disrupts lipid homeostasis in
RT liver.";
RL J. Biol. Chem. 285:10880-10889(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21173151; DOI=10.1074/jbc.m110.171819;
RA Allende M.L., Bektas M., Lee B.G., Bonifacino E., Kang J., Tuymetova G.,
RA Chen W., Saba J.D., Proia R.L.;
RT "Sphingosine-1-phosphate lyase deficiency produces a pro-inflammatory
RT response while impairing neutrophil trafficking.";
RL J. Biol. Chem. 286:7348-7358(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28521611; DOI=10.1080/15548627.2017.1291471;
RA Mitroi D.N., Karunakaran I., Graeler M., Saba J.D., Ehninger D.,
RA Ledesma M.D., van Echten-Deckert G.;
RT "SGPL1 (sphingosine phosphate lyase 1) modulates neuronal autophagy via
RT phosphatidylethanolamine production.";
RL Autophagy 13:885-899(2017).
RN [9]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28165339; DOI=10.1172/jci89626;
RA Lovric S., Goncalves S., Gee H.Y., Oskouian B., Srinivas H., Choi W.I.,
RA Shril S., Ashraf S., Tan W., Rao J., Airik M., Schapiro D., Braun D.A.,
RA Sadowski C.E., Widmeier E., Jobst-Schwan T., Schmidt J.M., Girik V.,
RA Capitani G., Suh J.H., Lachaussee N., Arrondel C., Patat J., Gribouval O.,
RA Furlano M., Boyer O., Schmitt A., Vuiblet V., Hashmi S., Wilcken R.,
RA Bernier F.P., Innes A.M., Parboosingh J.S., Lamont R.E., Midgley J.P.,
RA Wright N., Majewski J., Zenker M., Schaefer F., Kuss N., Greil J.,
RA Giese T., Schwarz K., Catheline V., Schanze D., Franke I., Sznajer Y.,
RA Truant A.S., Adams B., Desir J., Biemann R., Pei Y., Ars E., Lloberas N.,
RA Madrid A., Dharnidharka V.R., Connolly A.M., Willing M.C., Cooper M.A.,
RA Lifton R.P., Simons M., Riezman H., Antignac C., Saba J.D., Hildebrandt F.;
RT "Mutations in sphingosine-1-phosphate lyase cause nephrosis with ichthyosis
RT and adrenal insufficiency.";
RL J. Clin. Invest. 127:912-928(2017).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=28165343; DOI=10.1172/jci90171;
RA Prasad R., Hadjidemetriou I., Maharaj A., Meimaridou E., Buonocore F.,
RA Saleem M., Hurcombe J., Bierzynska A., Barbagelata E., Bergada I.,
RA Cassinelli H., Das U., Krone R., Hacihamdioglu B., Sari E., Yesilkaya E.,
RA Storr H.L., Clemente M., Fernandez-Cancio M., Camats N., Ram N.,
RA Achermann J.C., Van Veldhoven P.P., Guasti L., Braslavsky D., Guran T.,
RA Metherell L.A.;
RT "Sphingosine-1-phosphate lyase mutations cause primary adrenal
RT insufficiency and steroid-resistant nephrotic syndrome.";
RL J. Clin. Invest. 127:942-953(2017).
RN [11]
RP FUNCTION.
RX PubMed=28262793; DOI=10.1038/srep43575;
RA Vienken H., Mabrouki N., Grabau K., Claas R.F., Rudowski A., Schoemel N.,
RA Pfeilschifter J., Luetjohann D., van Echten-Deckert G.,
RA Meyer Zu Heringdorf D.;
RT "Characterization of cholesterol homeostasis in sphingosine-1-phosphate
RT lyase-deficient fibroblasts reveals a Niemann-Pick disease type C-like
RT phenotype with enhanced lysosomal Ca2+ storage.";
RL Sci. Rep. 7:43575-43575(2017).
CC -!- FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as
CC sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine
CC (PubMed:9464245, PubMed:20097939). Elevates stress-induced ceramide
CC production and apoptosis (PubMed:9464245). Required for global lipid
CC homeostasis in liver and cholesterol homeostasis in fibroblasts
CC (PubMed:20097939, PubMed:28262793). Involved in the regulation of pro-
CC inflammatory response and neutrophil trafficking (PubMed:21173151).
CC Modulates neuronal autophagy via phosphoethanolamine production which
CC regulates accumulation of aggregate-prone proteins such as APP
CC (PubMed:28521611). Seems to play a role in establishing neuronal
CC contact sites and axonal maintenance (By similarity).
CC {ECO:0000250|UniProtKB:Q9V7Y2, ECO:0000269|PubMed:20097939,
CC ECO:0000269|PubMed:21173151, ECO:0000269|PubMed:28262793,
CC ECO:0000269|PubMed:28521611, ECO:0000269|PubMed:9464245}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinganine 1-phosphate = hexadecanal + phosphoethanolamine;
CC Xref=Rhea:RHEA:18593, ChEBI:CHEBI:17600, ChEBI:CHEBI:57939,
CC ChEBI:CHEBI:58190; EC=4.1.2.27;
CC Evidence={ECO:0000269|PubMed:9464245};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphing-4-enine 1-phosphate = (2E)-hexadecenal +
CC phosphoethanolamine; Xref=Rhea:RHEA:33507, ChEBI:CHEBI:17585,
CC ChEBI:CHEBI:58190, ChEBI:CHEBI:60119; EC=4.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:O95470};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:O95470};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:9464245}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15522238, ECO:0000269|PubMed:28165339}; Single-pass
CC type III membrane protein {ECO:0000269|PubMed:15522238}; Cytoplasmic
CC side {ECO:0000269|PubMed:15522238}.
CC -!- TISSUE SPECIFICITY: Highest levels are found in liver, small intestine
CC and thymus, followed by kidney, lung, heart, spleen and brain (at
CC protein level). Also detected in stomach, testis and skeletal muscle
CC (at protein level). {ECO:0000269|PubMed:15522238,
CC ECO:0000269|PubMed:20097939, ECO:0000269|PubMed:28165339,
CC ECO:0000269|PubMed:9464245}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout mouse embryogenesis.A
CC transient increase is observed from 5.5 dpc to 7.5 dpc.
CC {ECO:0000269|PubMed:15522238}.
CC -!- DISRUPTION PHENOTYPE: Mutant animals have a shortened lifespan
CC (PubMed:21173151). Mutant mice show an increase of sphingoid base
CC phosphates, but also other sphingolipids (including sphingosine,
CC ceramide, and sphingomyelin) in the serum and/or liver, resulting in
CC changes in the levels of serum and liver lipids not directly within the
CC sphingolipid pathway, including phospholipids, triacyglycerol,
CC diacylglycerol, and cholesterol (PubMed:20097939). They are deficient
CC in B and T lymphocytes yet have high blood levels of neutrophils and
CC monocytes along with elevated expression of pro-inflammatory cytokines.
CC Their tissues are largely clear of infiltrating leukocytes and their
CC neutrophils are defective in migration to chemotactic stimulus
CC (PubMed:21173151). Mice lacking Sgpl1 exhibit complete podocyte foot
CC process effacement and absence of slit diaphragms in kidney
CC (PubMed:9464245, PubMed:28165339). They display hypoalbuminemia and an
CC elevated urinary albumin/creatinine ratio (PubMed:28165339). They also
CC display abnormal adrenal gland morphology and defective expression of
CC enzymes involved in steroidogenesis in this tissue (PubMed:28165343).
CC Conditional knockout in brain significantly reduces phosphoethanolamine
CC levels with alterations in basal and stimulated autophagy involving
CC decreased conversion of LC3-I to LC3-II, increased levels of lysosomal
CC markers and aggregate-prone proteins such as APP and SNCA. Animals show
CC profound deficits in cognitive skills (PubMed:28521611).
CC {ECO:0000269|PubMed:20097939, ECO:0000269|PubMed:21173151,
CC ECO:0000269|PubMed:28165339, ECO:0000269|PubMed:28165343,
CC ECO:0000269|PubMed:28521611, ECO:0000269|PubMed:9464245}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000305}.
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DR EMBL; AF036894; AAC03768.1; -; mRNA.
DR EMBL; AK036747; BAC29562.1; -; mRNA.
DR EMBL; AK037789; BAC29872.1; -; mRNA.
DR EMBL; AK043024; BAC31437.1; -; mRNA.
DR EMBL; AK049342; BAC33695.1; -; mRNA.
DR EMBL; BC026135; AAH26135.1; -; mRNA.
DR CCDS; CCDS35914.1; -.
DR PIR; JC5923; JC5923.
DR RefSeq; NP_001303602.1; NM_001316673.1.
DR RefSeq; NP_001303603.1; NM_001316674.1.
DR RefSeq; NP_033189.2; NM_009163.4.
DR RefSeq; XP_017169349.1; XM_017313860.1.
DR AlphaFoldDB; Q8R0X7; -.
DR SMR; Q8R0X7; -.
DR BioGRID; 203199; 13.
DR IntAct; Q8R0X7; 1.
DR MINT; Q8R0X7; -.
DR STRING; 10090.ENSMUSP00000112975; -.
DR BindingDB; Q8R0X7; -.
DR ChEMBL; CHEMBL5009; -.
DR SwissLipids; SLP:000000935; -.
DR iPTMnet; Q8R0X7; -.
DR PhosphoSitePlus; Q8R0X7; -.
DR SwissPalm; Q8R0X7; -.
DR EPD; Q8R0X7; -.
DR jPOST; Q8R0X7; -.
DR MaxQB; Q8R0X7; -.
DR PaxDb; Q8R0X7; -.
DR PRIDE; Q8R0X7; -.
DR ProteomicsDB; 256988; -.
DR Antibodypedia; 14941; 180 antibodies from 23 providers.
DR DNASU; 20397; -.
DR Ensembl; ENSMUST00000092498; ENSMUSP00000090155; ENSMUSG00000020097.
DR Ensembl; ENSMUST00000122259; ENSMUSP00000112975; ENSMUSG00000020097.
DR GeneID; 20397; -.
DR KEGG; mmu:20397; -.
DR UCSC; uc007ffk.2; mouse.
DR CTD; 8879; -.
DR MGI; MGI:1261415; Sgpl1.
DR VEuPathDB; HostDB:ENSMUSG00000020097; -.
DR eggNOG; KOG1383; Eukaryota.
DR GeneTree; ENSGT00390000000046; -.
DR HOGENOM; CLU_028929_1_1_1; -.
DR InParanoid; Q8R0X7; -.
DR OMA; FKDHQFT; -.
DR OrthoDB; 517323at2759; -.
DR PhylomeDB; Q8R0X7; -.
DR TreeFam; TF300777; -.
DR BRENDA; 4.1.2.27; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 20397; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Sgpl1; mouse.
DR PRO; PR:Q8R0X7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R0X7; protein.
DR Bgee; ENSMUSG00000020097; Expressed in urinary bladder urothelium and 253 other tissues.
DR ExpressionAtlas; Q8R0X7; baseline and differential.
DR Genevisible; Q8R0X7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; ISS:UniProtKB.
DR GO; GO:0008209; P:androgen metabolic process; IMP:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0008210; P:estrogen metabolic process; IMP:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0008585; P:female gonad development; IMP:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
DR GO; GO:0001553; P:luteinization; IMP:MGI.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0030149; P:sphingolipid catabolic process; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Endoplasmic reticulum; Lipid metabolism; Lyase;
KW Membrane; Nitration; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Signal-anchor; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..568
FT /note="Sphingosine-1-phosphate lyase 1"
FT /id="PRO_0000147013"
FT TOPO_DOM 1..40
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000269|PubMed:15522238"
FT TOPO_DOM 62..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15522238"
FT MOD_RES 353
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 353
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O95470"
FT MOD_RES 356
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95470"
FT MOD_RES 366
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95470"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95470"
FT CONFLICT 305
FT /note="A -> T (in Ref. 1; AAC03768)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="N -> K (in Ref. 2; BAC31437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 63677 MW; FA5D52E4E49DF09E CRC64;
MPGTDLLKLK DFEPYLEILE SYSTKAKNYV NGYCTKYEPW QLIAWSVLCT LLIVWVYELI
FQPESLWSRF KKKLFKLIRK MPFIGRKIEQ QVSKAKKDLV KNMPFLKVDK DYVKTLPAQG
MGTAEVLERL KEYSSMDGSW QEGKASGAVY NGEPKLTELL VQAYGEFTWS NPLHPDIFPG
LRKLEAEIVR MTCSLFNGGP DSCGCVTSGG TESILMACKA YRDLALEKGI KTPEIVAPES
AHAAFDKAAH YFGMKIVRVA LKKNMEVDVQ AMKRAISRNT AMLVCSTPQF PHGVMDPVPE
VAKLAVRYKI PLHVDACLGG FLIVFMEKAG YPLEKPFDFR VKGVTSISAD THKYGYAPKG
SSVVMYSNEK YRTYQFFVGA DWQGGVYASP SIAGSRPGGI IAACWAALMH FGENGYVEAT
KQIIKTARFL KSELENIKNI FIFGDPQLSV IALGSNDFDI YRLSNMMSAK GWNFNYLQFP
RSIHFCITLV HTRKRVAIQF LKDIRESVTQ IMKNPKAKTT GMGAIYGMAQ ATIDRKLVAE
ISSVFLDCLY TTDPVTQGNQ MNGSPKPR
