SRR_MOUSE
ID SRR_MOUSE Reviewed; 339 AA.
AC Q9QZX7; Q401M7; Q5SWE4; Q5SWE5; Q5SWE7; Q8BT19; Q8CD11;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Serine racemase {ECO:0000303|PubMed:10557334};
DE EC=5.1.1.18 {ECO:0000269|PubMed:10557334, ECO:0000269|PubMed:12393813, ECO:0000269|PubMed:12515328, ECO:0000269|PubMed:15536068};
DE AltName: Full=D-serine ammonia-lyase;
DE AltName: Full=D-serine dehydratase;
DE EC=4.3.1.18 {ECO:0000269|PubMed:15536068};
DE AltName: Full=L-serine ammonia-lyase;
DE AltName: Full=L-serine dehydratase;
DE EC=4.3.1.17 {ECO:0000269|PubMed:12393813, ECO:0000269|PubMed:12515328, ECO:0000269|PubMed:15536068};
GN Name=Srr;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RC STRAIN=BALB/cJ;
RX PubMed=10557334; DOI=10.1073/pnas.96.23.13409;
RA Wolosker H., Blackshaw S., Snyder S.H.;
RT "Serine racemase: a glial enzyme synthesizing D-serine to regulate
RT glutamate-N-methyl-D-aspartate neurotransmission.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13409-13414(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain cortex, Spleen, and Testis;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-56 (ISOFORMS 1/2/3).
RC TISSUE=Brain;
RA Ohba H., Ohnishi T., Yoshikawa T.;
RT "Multiple splice variants in 5'UTR of mouse serine racemase.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 15-40, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=12515328; DOI=10.1023/a:1021607715824;
RA Neidle A., Dunlop D.S.;
RT "Allosteric regulation of mouse brain serine racemase.";
RL Neurochem. Res. 27:1719-1724(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=12393813; DOI=10.1073/pnas.222421299;
RA De Miranda J., Panizzutti R., Foltyn V.N., Wolosker H.;
RT "Cofactors of serine racemase that physiologically stimulate the synthesis
RT of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14542-14547(2002).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15536068; DOI=10.1074/jbc.m405726200;
RA Foltyn V.N., Bendikov I., De Miranda J., Panizzutti R., Dumin E.,
RA Shleper M., Li P., Toney M.D., Kartvelishvily E., Wolosker H.;
RT "Serine racemase modulates intracellular D-serine levels through an
RT alpha,beta-elimination activity.";
RL J. Biol. Chem. 280:1754-1763(2005).
RN [10]
RP FUNCTION, S-NITROSYLATION AT CYS-113, ATP-BINDING, AND MUTAGENESIS OF
RP CYS-113.
RX PubMed=17293453; DOI=10.1073/pnas.0611620104;
RA Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T., Barrow R.K.,
RA Amzel L.M., Snyder S.H.;
RT "Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition
RT of D-serine formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, 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).
CC -!- FUNCTION: Catalyzes the synthesis of D-serine from L-serine. D-serine
CC is a key coagonist with glutamate at NMDA receptors. Has dehydratase
CC activity towards both L-serine and D-serine.
CC {ECO:0000269|PubMed:10557334, ECO:0000269|PubMed:12393813,
CC ECO:0000269|PubMed:12515328, ECO:0000269|PubMed:15536068,
CC ECO:0000269|PubMed:17293453}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; EC=5.1.1.18;
CC Evidence={ECO:0000269|PubMed:10557334, ECO:0000269|PubMed:12393813,
CC ECO:0000269|PubMed:12515328, ECO:0000269|PubMed:15536068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC Evidence={ECO:0000269|PubMed:15536068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC Evidence={ECO:0000269|PubMed:12393813, ECO:0000269|PubMed:12515328,
CC ECO:0000269|PubMed:15536068};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10557334, ECO:0000269|PubMed:12515328};
CC -!- ACTIVITY REGULATION: Allosterically activated by magnesium, and
CC possibly also other divalent metal cations. Allosterically activated by
CC ATP, ADP or GTP. {ECO:0000269|PubMed:12393813,
CC ECO:0000269|PubMed:12515328}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12515328}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QZX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QZX7-2; Sequence=VSP_025013;
CC Name=3;
CC IsoId=Q9QZX7-3; Sequence=VSP_025014;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Brain.
CC -!- PTM: S-nitrosylated, leading to decrease the enzyme activity.
CC {ECO:0000269|PubMed:17293453}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI24255.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF148321; AAF08701.1; -; mRNA.
DR EMBL; AK031687; BAC27514.1; -; mRNA.
DR EMBL; AK028034; BAC25712.1; -; mRNA.
DR EMBL; AK043738; BAC31637.1; -; mRNA.
DR EMBL; AK157122; BAE33968.1; -; mRNA.
DR EMBL; AK170096; BAE41561.1; -; mRNA.
DR EMBL; AL604066; CAI24252.1; -; Genomic_DNA.
DR EMBL; AL604066; CAI24253.1; -; Genomic_DNA.
DR EMBL; AL604066; CAI24254.1; -; Genomic_DNA.
DR EMBL; AL604066; CAI24255.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC011164; AAH11164.1; -; mRNA.
DR EMBL; AB232340; BAE19920.1; -; mRNA.
DR EMBL; AB232341; BAE19921.1; -; mRNA.
DR EMBL; AB232342; BAE19922.1; -; mRNA.
DR EMBL; AB232343; BAE19923.1; -; mRNA.
DR EMBL; AB235396; BAE44529.1; -; mRNA.
DR CCDS; CCDS25038.1; -. [Q9QZX7-1]
DR CCDS; CCDS88190.1; -. [Q9QZX7-2]
DR RefSeq; NP_001156783.1; NM_001163311.1. [Q9QZX7-1]
DR RefSeq; NP_038789.1; NM_013761.4. [Q9QZX7-1]
DR RefSeq; XP_006533520.1; XM_006533457.3. [Q9QZX7-1]
DR RefSeq; XP_017170058.1; XM_017314569.1. [Q9QZX7-1]
DR RefSeq; XP_017170059.1; XM_017314570.1.
DR RefSeq; XP_017170060.1; XM_017314571.1. [Q9QZX7-1]
DR AlphaFoldDB; Q9QZX7; -.
DR SMR; Q9QZX7; -.
DR BioGRID; 205172; 9.
DR STRING; 10090.ENSMUSP00000113372; -.
DR BindingDB; Q9QZX7; -.
DR ChEMBL; CHEMBL1075306; -.
DR iPTMnet; Q9QZX7; -.
DR PhosphoSitePlus; Q9QZX7; -.
DR SwissPalm; Q9QZX7; -.
DR EPD; Q9QZX7; -.
DR jPOST; Q9QZX7; -.
DR MaxQB; Q9QZX7; -.
DR PaxDb; Q9QZX7; -.
DR PeptideAtlas; Q9QZX7; -.
DR PRIDE; Q9QZX7; -.
DR ProteomicsDB; 257407; -. [Q9QZX7-1]
DR ProteomicsDB; 257408; -. [Q9QZX7-2]
DR ProteomicsDB; 257409; -. [Q9QZX7-3]
DR Antibodypedia; 4201; 333 antibodies from 28 providers.
DR DNASU; 27364; -.
DR Ensembl; ENSMUST00000065211; ENSMUSP00000067552; ENSMUSG00000001323. [Q9QZX7-1]
DR Ensembl; ENSMUST00000108447; ENSMUSP00000104086; ENSMUSG00000001323. [Q9QZX7-2]
DR Ensembl; ENSMUST00000108448; ENSMUSP00000104087; ENSMUSG00000001323. [Q9QZX7-1]
DR Ensembl; ENSMUST00000121738; ENSMUSP00000113372; ENSMUSG00000001323. [Q9QZX7-1]
DR Ensembl; ENSMUST00000128556; ENSMUSP00000120012; ENSMUSG00000001323. [Q9QZX7-3]
DR GeneID; 27364; -.
DR KEGG; mmu:27364; -.
DR UCSC; uc007kcr.2; mouse. [Q9QZX7-1]
DR UCSC; uc011xzd.1; mouse. [Q9QZX7-2]
DR CTD; 63826; -.
DR MGI; MGI:1351636; Srr.
DR VEuPathDB; HostDB:ENSMUSG00000001323; -.
DR eggNOG; KOG1251; Eukaryota.
DR GeneTree; ENSGT00550000075026; -.
DR HOGENOM; CLU_021152_4_2_1; -.
DR InParanoid; Q9QZX7; -.
DR OMA; LIHPFDH; -.
DR OrthoDB; 943371at2759; -.
DR PhylomeDB; Q9QZX7; -.
DR TreeFam; TF313346; -.
DR BRENDA; 4.3.1.17; 3474.
DR BRENDA; 5.1.1.18; 3474.
DR Reactome; R-MMU-977347; Serine biosynthesis.
DR BioGRID-ORCS; 27364; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9QZX7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QZX7; protein.
DR Bgee; ENSMUSG00000001323; Expressed in CA1 field of hippocampus and 236 other tissues.
DR ExpressionAtlas; Q9QZX7; baseline and differential.
DR Genevisible; Q9QZX7; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016594; F:glycine binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IMP:MGI.
DR GO; GO:0030378; F:serine racemase activity; IDA:MGI.
DR GO; GO:0018114; F:threonine racemase activity; IDA:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0070179; P:D-serine biosynthetic process; IDA:MGI.
DR GO; GO:0070178; P:D-serine metabolic process; ISO:MGI.
DR GO; GO:0006563; P:L-serine metabolic process; IDA:MGI.
DR GO; GO:0042866; P:pyruvate biosynthetic process; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0009069; P:serine family amino acid metabolic process; IDA:MGI.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Alternative splicing; ATP-binding;
KW Direct protein sequencing; Isomerase; Lyase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; S-nitrosylation.
FT CHAIN 1..339
FT /note="Serine racemase"
FT /id="PRO_0000185651"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 238..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 113
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:17293453"
FT VAR_SEQ 174..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025013"
FT VAR_SEQ 183..339
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_025014"
FT MUTAGEN 51
FT /note="K->A: Impairs ATP-binding inducing a 80% decrease in
FT enzyme activity."
FT MUTAGEN 113
FT /note="C->S: Abolishes S-nitrosylation."
FT /evidence="ECO:0000269|PubMed:17293453"
FT CONFLICT 111
FT /note="P -> T (in Ref. 2; BAC25712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 36359 MW; B9AE9A9336358728 CRC64;
MCAQYCISFA DVEKAHINIQ DSIHLTPVLT SSILNQIAGR NLFFKCELFQ KTGSFKIRGA
LNAIRGLIPD TPEEKPKAVV THSSGNHGQA LTYAAKLEGI PAYIVVPQTA PNCKKLAIQA
YGASIVYCDP SDESREKVTQ RIMQETEGIL VHPNQEPAVI AGQGTIALEV LNQVPLVDAL
VVPVGGGGMV AGIAITIKAL KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV
KSSIGLNTWP IIRDLVDDVF TVTEDEIKYA TQLVWGRMKL LIEPTAGVAL AAVLSQHFQT
VSPEVKNVCI VLSGGNVDLT SLNWVGQAER PAPYQTVSV
