S15A4_MOUSE
ID S15A4_MOUSE Reviewed; 574 AA.
AC Q91W98; Q7TPL5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Solute carrier family 15 member 4 {ECO:0000305};
DE AltName: Full=Peptide/histidine transporter 1 {ECO:0000303|Ref.1};
GN Name=Slc15a4 {ECO:0000312|MGI:MGI:2140796};
GN Synonyms=Pht1 {ECO:0000303|Ref.1};
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].
RA Guo J.H., Yu L.;
RT "Cloning of a mouse gene encoding a product of peptide/histidine.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-299, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19570976; DOI=10.1074/jbc.m109.033670;
RA Lee J., Tattoli I., Wojtal K.A., Vavricka S.R., Philpott D.J.,
RA Girardin S.E.;
RT "pH-dependent internalization of muramyl peptides from early endosomes
RT enables Nod1 and Nod2 signaling.";
RL J. Biol. Chem. 284:23818-23829(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, 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.
RX PubMed=21045126; DOI=10.1073/pnas.1014051107;
RA Blasius A.L., Arnold C.N., Georgel P., Rutschmann S., Xia Y., Lin P.,
RA Ross C., Li X., Smart N.G., Beutler B.;
RT "Slc15a4, AP-3, and Hermansky-Pudlak syndrome proteins are required for
RT Toll-like receptor signaling in plasmacytoid dendritic cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19973-19978(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21277849; DOI=10.1053/j.gastro.2011.01.041;
RA Sasawatari S., Okamura T., Kasumi E., Tanaka-Furuyama K.,
RA Yanobu-Takanashi R., Shirasawa S., Kato N., Toyama-Sorimachi N.;
RT "The solute carrier family 15A4 regulates TLR9 and NOD1 functions in the
RT innate immune system and promotes colitis in mice.";
RL Gastroenterology 140:1513-1525(2011).
RN [8]
RP FUNCTION.
RX PubMed=23028315; DOI=10.1371/journal.ppat.1002915;
RA Blasius A.L., Krebs P., Sullivan B.M., Oldstone M.B., Popkin D.L.;
RT "Slc15a4, a gene required for pDC sensing of TLR ligands, is required to
RT control persistent viral infection.";
RL PLoS Pathog. 8:e1002915-e1002915(2012).
RN [9]
RP FUNCTION.
RX PubMed=23382217; DOI=10.1073/pnas.1222798110;
RA Baccala R., Gonzalez-Quintial R., Blasius A.L., Rimann I., Ozato K.,
RA Kono D.H., Beutler B., Theofilopoulos A.N.;
RT "Essential requirement for IRF8 and SLC15A4 implicates plasmacytoid
RT dendritic cells in the pathogenesis of lupus.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2940-2945(2013).
RN [10]
RP FUNCTION.
RX PubMed=25238095; DOI=10.1016/j.immuni.2014.08.011;
RA Kobayashi T., Shimabukuro-Demoto S., Yoshida-Sugitani R.,
RA Furuyama-Tanaka K., Karyu H., Sugiura Y., Shimizu Y., Hosaka T., Goto M.,
RA Kato N., Okamura T., Suematsu M., Yokoyama S., Toyama-Sorimachi N.;
RT "The histidine transporter SLC15A4 coordinates mTOR-dependent inflammatory
RT responses and pathogenic antibody production.";
RL Immunity 41:375-388(2014).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24695226; DOI=10.1038/nature13133;
RA Nakamura N., Lill J.R., Phung Q., Jiang Z., Bakalarski C., de Maziere A.,
RA Klumperman J., Schlatter M., Delamarre L., Mellman I.;
RT "Endosomes are specialized platforms for bacterial sensing and NOD2
RT signalling.";
RL Nature 509:240-244(2014).
RN [12]
RP FUNCTION.
RX PubMed=25310967; DOI=10.1038/icb.2014.82;
RA Dosenovic P., Adori M., Adams W.C., Pedersen G.K., Soldemo M., Beutler B.,
RA Karlsson Hedestam G.B.;
RT "Slc15a4 function is required for intact class switch recombination to
RT IgG2c in response to TLR9 stimulation.";
RL Immunol. Cell Biol. 93:136-146(2015).
RN [13]
RP FUNCTION, TRANSPORTER ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27845049; DOI=10.1016/j.bcp.2016.11.012;
RA Wang X.X., Hu Y., Keep R.F., Toyama-Sorimachi N., Smith D.E.;
RT "A novel role for PHT1 in the disposition of l-histidine in brain: In vitro
RT slice and in vivo pharmacokinetic studies in wildtype and Pht1 null mice.";
RL Biochem. Pharmacol. 124:94-102(2017).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29155995; DOI=10.1093/intimm/dxx063;
RA Kobayashi T., Tsutsui H., Shimabukuro-Demoto S., Yoshida-Sugitani R.,
RA Karyu H., Furuyama-Tanaka K., Ohshima D., Kato N., Okamura T.,
RA Toyama-Sorimachi N.;
RT "Lysosome biogenesis regulated by the amino-acid transporter SLC15A4 is
RT critical for functional integrity of mast cells.";
RL Int. Immunol. 29:551-566(2017).
RN [15]
RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=29784761; DOI=10.4049/jimmunol.1800210;
RA Hu Y., Song F., Jiang H., Nunez G., Smith D.E.;
RT "SLC15A2 and SLC15A4 mediate the transport of bacterially derived
RT di/tripeptides to enhance the nucleotide-binding oligomerization domain-
RT dependent immune response in mouse bone marrow-derived macrophages.";
RL J. Immunol. 201:652-662(2018).
RN [16]
RP FUNCTION.
RX PubMed=29305823; DOI=10.1007/s11095-017-2322-0;
RA Wang X.X., Li Y.B., Feng M.R., Smith D.E.;
RT "Semi-mechanistic population pharmacokinetic modeling of L-histidine
RT disposition and brain uptake in wildtype and Pht1 null mice.";
RL Pharm. Res. 35:19-19(2018).
RN [17]
RP FUNCTION.
RX PubMed=30262916; DOI=10.1038/s41598-018-32668-9;
RA Griffith A.D., Zaidi A.K., Pietro A., Hadiono M., Yang J.S., Davis R.,
RA Popkin D.L.;
RT "A requirement for slc15a4 in imiquimod-induced systemic inflammation and
RT psoriasiform inflammation in mice.";
RL Sci. Rep. 8:14451-14451(2018).
CC -!- FUNCTION: Proton-coupled amino-acid transporter that mediates the
CC transmembrane transport of L-histidine and some di- and tripeptides
CC from inside the lysosome to the cytosol, and plays a key role in innate
CC immune response (PubMed:19570976, PubMed:21277849, PubMed:25238095,
CC PubMed:27845049, PubMed:29305823). Able to transport a variety of
CC di- and tripeptides, including carnosine and some peptidoglycans
CC (PubMed:29784761). Transporter activity is pH-dependent and maximized
CC in the acidic lysosomal environment (By similarity). Involved in the
CC detection of microbial pathogens by toll-like receptors (TLRs) and NOD-
CC like receptors (NLRs), probably by mediating transport of bacterial
CC peptidoglycans across the endolysosomal membrane: catalyzes the
CC transport of certain bacterial peptidoglycans, such as muramyl
CC dipeptide (MDP), the NOD2 ligand, and L-alanyl-gamma-D-glutamyl-meso-
CC 2,6-diaminoheptanedioate (tri-DAP), the NOD1 ligand (PubMed:19570976,
CC PubMed:23028315, PubMed:25238095, PubMed:24695226, PubMed:29784761).
CC Required for TLR7, TLR8 and TLR9-mediated type I interferon (IFN-I)
CC productions in plasmacytoid dendritic cells (pDCs) (PubMed:21045126,
CC PubMed:23382217, PubMed:25238095, PubMed:30262916). Independently of
CC its transporter activity, also promotes the recruitment of innate
CC immune adapter TASL to endolysosome downstream of TLR7, TLR8 and TLR9:
CC TASL recruitment leads to the specific recruitment and activation of
CC IRF5 (By similarity). Required for isotype class switch recombination
CC to IgG2c isotype in response to TLR9 stimulation (PubMed:25310967).
CC Required for mast cell secretory-granule homeostasis by limiting mast
CC cell functions and inflammatory responses (PubMed:29155995).
CC {ECO:0000250|UniProtKB:O09014, ECO:0000250|UniProtKB:Q8N697,
CC ECO:0000269|PubMed:19570976, ECO:0000269|PubMed:21045126,
CC ECO:0000269|PubMed:21277849, ECO:0000269|PubMed:23028315,
CC ECO:0000269|PubMed:23382217, ECO:0000269|PubMed:24695226,
CC ECO:0000269|PubMed:25238095, ECO:0000269|PubMed:25310967,
CC ECO:0000269|PubMed:27845049, ECO:0000269|PubMed:29155995,
CC ECO:0000269|PubMed:29305823, ECO:0000269|PubMed:29784761,
CC ECO:0000269|PubMed:30262916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-histidine(out) = H(+)(in) + L-histidine(in);
CC Xref=Rhea:RHEA:37047, ChEBI:CHEBI:15378, ChEBI:CHEBI:57595;
CC Evidence={ECO:0000269|PubMed:21277849, ECO:0000269|PubMed:27845049,
CC ECO:0000269|PubMed:29784761};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37048;
CC Evidence={ECO:0000305|PubMed:21277849};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dipeptide(out) + H(+)(out) = a dipeptide(in) + H(+)(in);
CC Xref=Rhea:RHEA:64392, ChEBI:CHEBI:15378, ChEBI:CHEBI:90799;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-amino acid tripeptide(out) + H(+)(out) = an L-amino acid
CC tripeptide(in) + H(+)(in); Xref=Rhea:RHEA:64400, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155837; Evidence={ECO:0000250|UniProtKB:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64401;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + N-acetylmuramyl-L-alanyl-D-isoglutamine(out) =
CC H(+)(in) + N-acetylmuramyl-L-alanyl-D-isoglutamine(in);
CC Xref=Rhea:RHEA:64408, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830;
CC Evidence={ECO:0000269|PubMed:29784761};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64409;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-alanyl-gamma-D-glutamyl-meso-
CC diaminoheptanedioate(out) = H(+)(in) + L-alanyl-gamma-D-glutamyl-
CC meso-diaminoheptanedioate(in); Xref=Rhea:RHEA:64412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:61401;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64413;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-sarcosine(out) + H(+)(out) = glycyl-sarcosine(in) +
CC H(+)(in); Xref=Rhea:RHEA:64396, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155838; Evidence={ECO:0000250|UniProtKB:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carnosine(out) + H(+)(out) = carnosine(in) + H(+)(in);
CC Xref=Rhea:RHEA:64404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64405;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC -!- SUBUNIT: Interacts with TASL; leading to TASL recruitment to
CC endolysosome. {ECO:0000250|UniProtKB:Q8N697}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:21277849,
CC ECO:0000269|PubMed:24695226, ECO:0000269|PubMed:29155995}; Multi-pass
CC membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:24695226, ECO:0000269|PubMed:29784761}; Multi-pass
CC membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000269|PubMed:19570976}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in immune tissues,
CC including B-cells and dendritic cells (PubMed:21277849). Highly
CC expressed in macrophages (PubMed:29784761).
CC {ECO:0000269|PubMed:21277849, ECO:0000269|PubMed:29784761}.
CC -!- DISRUPTION PHENOTYPE: Mice are fertile and look healthy but display
CC impaired cytokine production in dendritic cells (PubMed:21277849).
CC Reduced uptake of L-histidine in brain (PubMed:27845049).
CC {ECO:0000269|PubMed:21277849, ECO:0000269|PubMed:27845049}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK95566.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY050630; AAK95566.1; ALT_FRAME; mRNA.
DR EMBL; BC016233; AAH16233.1; -; mRNA.
DR CCDS; CCDS19688.1; -.
DR RefSeq; NP_598656.1; NM_133895.1.
DR AlphaFoldDB; Q91W98; -.
DR SMR; Q91W98; -.
DR IntAct; Q91W98; 1.
DR STRING; 10090.ENSMUSP00000031367; -.
DR iPTMnet; Q91W98; -.
DR PhosphoSitePlus; Q91W98; -.
DR SwissPalm; Q91W98; -.
DR EPD; Q91W98; -.
DR jPOST; Q91W98; -.
DR MaxQB; Q91W98; -.
DR PaxDb; Q91W98; -.
DR PeptideAtlas; Q91W98; -.
DR PRIDE; Q91W98; -.
DR ProteomicsDB; 260970; -.
DR Antibodypedia; 3084; 68 antibodies from 17 providers.
DR DNASU; 100561; -.
DR Ensembl; ENSMUST00000031367; ENSMUSP00000031367; ENSMUSG00000029416.
DR GeneID; 100561; -.
DR KEGG; mmu:100561; -.
DR UCSC; uc008zsb.1; mouse.
DR CTD; 121260; -.
DR MGI; MGI:2140796; Slc15a4.
DR VEuPathDB; HostDB:ENSMUSG00000029416; -.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000159361; -.
DR HOGENOM; CLU_009313_6_1_1; -.
DR InParanoid; Q91W98; -.
DR OMA; QMMGVWF; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q91W98; -.
DR TreeFam; TF330897; -.
DR Reactome; R-MMU-427975; Proton/oligopeptide cotransporters.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 100561; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Slc15a4; mouse.
DR PRO; PR:Q91W98; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q91W98; protein.
DR Bgee; ENSMUSG00000029416; Expressed in spermatocyte and 248 other tissues.
DR ExpressionAtlas; Q91W98; baseline and differential.
DR Genevisible; Q91W98; MM.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0036020; C:endolysosome membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0031303; C:integral component of endosome membrane; IDA:UniProtKB.
DR GO; GO:1905103; C:integral component of lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015333; F:peptide:proton symporter activity; IMP:UniProtKB.
DR GO; GO:0015647; F:peptidoglycan transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0015817; P:histidine transport; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0089708; P:L-histidine transmembrane export from vacuole; IMP:UniProtKB.
DR GO; GO:0033023; P:mast cell homeostasis; IMP:UniProtKB.
DR GO; GO:0015835; P:peptidoglycan transport; IDA:UniProtKB.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0070430; P:positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; IMP:UniProtKB.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IDA:UniProtKB.
DR GO; GO:0034157; P:positive regulation of toll-like receptor 7 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034161; P:positive regulation of toll-like receptor 8 signaling pathway; ISO:MGI.
DR GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048302; P:regulation of isotype switching to IgG isotypes; IMP:UniProtKB.
DR GO; GO:0070424; P:regulation of nucleotide-binding oligomerization domain containing signaling pathway; IMP:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW Endosome; Immunity; Innate immunity; Lysosome; Membrane; Peptide transport;
KW Phosphoprotein; Protein transport; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..574
FT /note="Solute carrier family 15 member 4"
FT /id="PRO_0000338600"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CONFLICT 218
FT /note="Y -> I (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="P -> L (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="S -> G (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="S -> N (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="R -> K (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="Y -> F (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="P -> L (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
FT CONFLICT 473..474
FT /note="GL -> RQ (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="G -> C (in Ref. 1; AAK95566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 62256 MW; 9AE338C1AF56AD05 CRC64;
MEGERAPLLG SRRPAVSAAS AVFAGRRAAC GAVLLAELLE RAAFYGVTAN LVLFLNGAPF
DWEGAQASQA LLLFMGLTYL GSPFGGWLAD ARLGRARAIL LSLALYLLGL LAFPLLAAPR
SRSFLCGDPR PELVRNCSAP FPNGSASCPE NAARRCAPAT FAGLVLVGLG VATVKANITP
FGADQVKDRG PEATRRFFNW FYWSINLGAI LSLGGIAYIQ QNVSFFTGYL IPTVCVAIAF
LVFLCGQSVF ITKPPDGSAF TDMFRILTYS CCSQRGGQRR SGEGLGVFQQ SSKHSLFDSC
KMSRGGPFTE DKVEDVKALV KIVPVFLALI PYWTVYFQMQ TTYALQSLHL KIPEISSITT
THHTLPAAWL TMFDAVLILL LIPLKDKLVD PVLRRHGLLP SSLKRIAVGM FFVMCSAFAA
GILESKRLDL VKEKTINQTI GGVVYHAADL PIWWQIPQYV LIGISEIFAS IAGLEFAYSA
APKSMQSAIM GLFFFFSGIG SFVGSGLLAL VSLKAIGWMS SHTDFGNINS CHLHYYFFLL
AAIQGATLLL FLIVSVKYDR QRARTDGGPA STRT
