SRR_HUMAN
ID SRR_HUMAN Reviewed; 340 AA.
AC Q9GZT4; D3DTI5; Q6IA55;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serine racemase {ECO:0000303|PubMed:11054547};
DE EC=5.1.1.18 {ECO:0000269|PubMed:20106978};
DE AltName: Full=D-serine ammonia-lyase;
DE AltName: Full=D-serine dehydratase;
DE EC=4.3.1.18 {ECO:0000250|UniProtKB:Q9QZX7};
DE AltName: Full=L-serine ammonia-lyase;
DE AltName: Full=L-serine dehydratase;
DE EC=4.3.1.17 {ECO:0000250|UniProtKB:Q9QZX7};
GN Name=SRR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=11054547; DOI=10.1016/s0378-1119(00)00356-5;
RA De Miranda J., Santoro A., Engelender S., Wolosker H.;
RT "Human serine racemase: molecular cloning, genomic organization and
RT functional expression.";
RL Gene 256:183-188(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15193426; DOI=10.1016/j.molbrainres.2004.03.007;
RA Xia M., Liu Y., Figueroa D.J., Chiu C.S., Wei N., Lawlor A.M., Lu P.,
RA Sur C., Koblan K.S., Connolly T.M.;
RT "Characterization and localization of a human serine racemase.";
RL Brain Res. Mol. Brain Res. 125:96-104(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP PROTEIN SEQUENCE OF 97-114; 116-135; 206-221 AND 226-241, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 3-340 IN COMPLEX WITH MANGANESE
RP IONS; MALONATE AND PYRIDOXAL PHOSPHATE, COFACTOR, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=20106978; DOI=10.1074/jbc.m109.050062;
RA Smith M.A., Mack V., Ebneth A., Moraes I., Felicetti B., Wood M.,
RA Schonfeld D., Mather O., Cesura A., Barker J.;
RT "The structure of mammalian serine racemase: evidence for conformational
RT changes upon inhibitor binding.";
RL J. Biol. Chem. 285:12873-12881(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:11054547, ECO:0000269|PubMed:20106978}.
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:20106978};
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:0000250|UniProtKB:Q9QZX7};
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:0000250|UniProtKB:Q9QZX7};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20106978};
CC -!- ACTIVITY REGULATION: Allosterically activated by magnesium, and
CC possibly also other divalent metal cations. Allosterically activated by
CC ATP, ADP or GTP. Competitively inhibited by malonate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.5 mM for L-serine {ECO:0000269|PubMed:20106978};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20106978}.
CC -!- INTERACTION:
CC Q9GZT4; Q9H4P4: RNF41; NbExp=6; IntAct=EBI-9055653, EBI-2130266;
CC Q9GZT4; Q9GZT4: SRR; NbExp=5; IntAct=EBI-9055653, EBI-9055653;
CC -!- TISSUE SPECIFICITY: Brain: expressed at high levels in hippocampus and
CC corpus callosum, intermediate levels in substantia nigra and caudate,
CC and low levels in amygdala, thalamus, and subthalamic nuclei. Expressed
CC in heart, skeletal muscle, kidney and liver.
CC {ECO:0000269|PubMed:15193426}.
CC -!- PTM: S-nitrosylated, leading to decrease the enzyme activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; AF169974; AAG27081.1; -; mRNA.
DR EMBL; AY034081; AAK58495.1; -; mRNA.
DR EMBL; AK023169; BAB14442.1; -; mRNA.
DR EMBL; CR457300; CAG33581.1; -; mRNA.
DR EMBL; CH471108; EAW90553.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90554.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90555.1; -; Genomic_DNA.
DR EMBL; BC074728; AAH74728.1; -; mRNA.
DR CCDS; CCDS11017.1; -.
DR RefSeq; NP_068766.1; NM_021947.2.
DR RefSeq; XP_006721628.1; XM_006721565.3.
DR RefSeq; XP_006721629.1; XM_006721566.3.
DR RefSeq; XP_011522276.1; XM_011523974.2.
DR PDB; 3L6B; X-ray; 1.50 A; A=1-340.
DR PDB; 3L6R; X-ray; 1.70 A; A=1-340.
DR PDB; 5X2L; X-ray; 1.81 A; A/B=1-340.
DR PDB; 6SLH; X-ray; 1.89 A; AAA/BBB/CCC/DDD=1-340.
DR PDB; 6ZSP; X-ray; 1.60 A; AAA/BBB=1-340.
DR PDB; 6ZUJ; X-ray; 1.80 A; AAA/BBB/CCC/DDD=1-340.
DR PDB; 7NBC; X-ray; 1.71 A; AAA/BBB/CCC/DDD=1-340.
DR PDB; 7NBD; X-ray; 1.86 A; AAA/BBB/CCC/DDD=1-340.
DR PDB; 7NBF; X-ray; 1.60 A; AAA/BBB/CCC/DDD=1-340.
DR PDB; 7NBG; X-ray; 1.53 A; AAA/BBB/CCC/DDD=1-340.
DR PDB; 7NBH; X-ray; 1.77 A; AAA/BBB/CCC/DDD=1-340.
DR PDBsum; 3L6B; -.
DR PDBsum; 3L6R; -.
DR PDBsum; 5X2L; -.
DR PDBsum; 6SLH; -.
DR PDBsum; 6ZSP; -.
DR PDBsum; 6ZUJ; -.
DR PDBsum; 7NBC; -.
DR PDBsum; 7NBD; -.
DR PDBsum; 7NBF; -.
DR PDBsum; 7NBG; -.
DR PDBsum; 7NBH; -.
DR AlphaFoldDB; Q9GZT4; -.
DR SMR; Q9GZT4; -.
DR BioGRID; 121963; 28.
DR IntAct; Q9GZT4; 8.
DR MINT; Q9GZT4; -.
DR STRING; 9606.ENSP00000339435; -.
DR BindingDB; Q9GZT4; -.
DR ChEMBL; CHEMBL4460; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB00133; Serine.
DR iPTMnet; Q9GZT4; -.
DR PhosphoSitePlus; Q9GZT4; -.
DR BioMuta; SRR; -.
DR DMDM; 20139924; -.
DR EPD; Q9GZT4; -.
DR jPOST; Q9GZT4; -.
DR MassIVE; Q9GZT4; -.
DR MaxQB; Q9GZT4; -.
DR PaxDb; Q9GZT4; -.
DR PeptideAtlas; Q9GZT4; -.
DR PRIDE; Q9GZT4; -.
DR ProteomicsDB; 80131; -.
DR Antibodypedia; 4201; 333 antibodies from 28 providers.
DR DNASU; 63826; -.
DR Ensembl; ENST00000344595.10; ENSP00000339435.5; ENSG00000167720.13.
DR GeneID; 63826; -.
DR KEGG; hsa:63826; -.
DR MANE-Select; ENST00000344595.10; ENSP00000339435.5; NM_021947.3; NP_068766.1.
DR UCSC; uc002fue.2; human.
DR CTD; 63826; -.
DR DisGeNET; 63826; -.
DR GeneCards; SRR; -.
DR HGNC; HGNC:14398; SRR.
DR HPA; ENSG00000167720; Low tissue specificity.
DR MIM; 606477; gene.
DR neXtProt; NX_Q9GZT4; -.
DR OpenTargets; ENSG00000167720; -.
DR PharmGKB; PA37877; -.
DR VEuPathDB; HostDB:ENSG00000167720; -.
DR eggNOG; KOG1251; Eukaryota.
DR GeneTree; ENSGT00550000075026; -.
DR HOGENOM; CLU_021152_4_2_1; -.
DR InParanoid; Q9GZT4; -.
DR OMA; LIHPFDH; -.
DR OrthoDB; 943371at2759; -.
DR PhylomeDB; Q9GZT4; -.
DR TreeFam; TF313346; -.
DR BioCyc; MetaCyc:HS09614-MON; -.
DR BRENDA; 5.1.1.18; 2681.
DR PathwayCommons; Q9GZT4; -.
DR Reactome; R-HSA-977347; Serine biosynthesis.
DR SABIO-RK; Q9GZT4; -.
DR SignaLink; Q9GZT4; -.
DR SIGNOR; Q9GZT4; -.
DR BioGRID-ORCS; 63826; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; SRR; human.
DR EvolutionaryTrace; Q9GZT4; -.
DR GeneWiki; Serine_racemase; -.
DR GenomeRNAi; 63826; -.
DR Pharos; Q9GZT4; Tbio.
DR PRO; PR:Q9GZT4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9GZT4; protein.
DR Bgee; ENSG00000167720; Expressed in ganglionic eminence and 169 other tissues.
DR ExpressionAtlas; Q9GZT4; baseline and differential.
DR Genevisible; Q9GZT4; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016594; F:glycine binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0030378; F:serine racemase activity; IDA:UniProtKB.
DR GO; GO:0018114; F:threonine racemase activity; ISS:UniProtKB.
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:UniProtKB.
DR GO; GO:0070178; P:D-serine metabolic process; IDA:UniProtKB.
DR GO; GO:0006563; P:L-serine metabolic process; IDA:UniProtKB.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:UniProtKB.
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; ISS:UniProtKB.
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 3D-structure; Allosteric enzyme; ATP-binding; Direct protein sequencing;
KW Isomerase; Lyase; Magnesium; Metal-binding; Nucleotide-binding;
KW Pyridoxal phosphate; Reference proteome; S-nitrosylation.
FT CHAIN 1..340
FT /note="Serine racemase"
FT /id="PRO_0000185650"
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:0000250"
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:0000305"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 238..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-(pyridoxal phosphate)lysine"
FT MOD_RES 113
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZX7"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 157..173
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:3L6B"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3L6B"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3L6B"
SQ SEQUENCE 340 AA; 36566 MW; 873342C62D5D7B9D CRC64;
MCAQYCISFA DVEKAHINIR DSIHLTPVLT SSILNQLTGR NLFFKCELFQ KTGSFKIRGA
LNAVRSLVPD ALERKPKAVV THSSGNHGQA LTYAAKLEGI PAYIVVPQTA PDCKKLAIQA
YGASIVYCEP SDESRENVAK RVTEETEGIM VHPNQEPAVI AGQGTIALEV LNQVPLVDAL
VVPVGGGGML AGIAITVKAL KPSVKVYAAE PSNADDCYQS KLKGKLMPNL YPPETIADGV
KSSIGLNTWP IIRDLVDDIF TVTEDEIKCA TQLVWERMKL LIEPTAGVGV AAVLSQHFQT
VSPEVKNICI VLSGGNVDLT SSITWVKQAE RPASYQSVSV
