ENTP5_HUMAN
ID ENTP5_HUMAN Reviewed; 428 AA.
AC O75356; A1L4C5; Q96RX0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Nucleoside diphosphate phosphatase ENTPD5 {ECO:0000305|PubMed:10400613, ECO:0000305|PubMed:15698960};
DE EC=3.6.1.6 {ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960};
DE AltName: Full=CD39 antigen-like 4;
DE AltName: Full=ER-UDPase;
DE AltName: Full=Ectonucleoside triphosphate diphosphohydrolase 5 {ECO:0000312|HGNC:HGNC:3367};
DE Short=NTPDase 5 {ECO:0000303|PubMed:15698960};
DE AltName: Full=Guanosine-diphosphatase ENTPD5 {ECO:0000305};
DE Short=GDPase ENTPD5;
DE AltName: Full=Inosine diphosphate phosphatase ENTPD5 {ECO:0000305};
DE AltName: Full=Nucleoside diphosphatase;
DE AltName: Full=Uridine-diphosphatase ENTPD5;
DE Short=UDPase ENTPD5;
DE Flags: Precursor;
GN Name=ENTPD5 {ECO:0000312|HGNC:HGNC:3367};
GN Synonyms=CD39L4 {ECO:0000303|PubMed:9676430}, PCPH;
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 TISSUE SPECIFICITY.
RC TISSUE=Leukemia;
RX PubMed=9676430; DOI=10.1006/geno.1998.5317;
RA Chadwick B.P., Frischauf A.-M.;
RT "The CD39-like gene family: identification of three new human members
RT (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the
RT gene family from Drosophila melanogaster.";
RL Genomics 50:357-367(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10708485;
RX DOI=10.1002/(sici)1098-2744(200003)27:3<229::aid-mc10>3.0.co;2-z;
RA Recio J.A., Zambrano N., Pena L., Reig J.A., Rhoads A., Rouzaut A.,
RA Notario V.;
RT "The human PCPH proto-oncogene: cDNA identification, primary structure,
RT chromosomal mapping, and expression in normal and tumor cells.";
RL Mol. Carcinog. 27:229-236(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF CYS-39.
RC TISSUE=Hippocampus;
RX PubMed=15698960; DOI=10.1016/j.bbapap.2004.11.017;
RA Murphy-Piedmonte D.M., Crawford P.A., Kirley T.L.;
RT "Bacterial expression, folding, purification and characterization of
RT soluble NTPDase5 (CD39L4) ecto-nucleotidase.";
RL Biochim. Biophys. Acta 1747:251-259(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10400613; DOI=10.1074/jbc.274.29.20064;
RA Mulero J.J., Yeung G., Nelken S.T., Ford J.E.;
RT "CD39-L4 is a secreted human apyrase, specific for the hydrolysis of
RT nucleoside diphosphates.";
RL J. Biol. Chem. 274:20064-20067(1999).
RN [8]
RP GLYCOSYLATION, AND SUBUNIT.
RX PubMed=11041857; DOI=10.1021/bi000960y;
RA Mulero J.J., Yeung G., Nelken S.T., Bright J.M., McGowan D.W., Ford J.E.;
RT "Biochemical characterization of CD39L4.";
RL Biochemistry 39:12924-12928(2000).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP INDUCTION.
RX PubMed=21074248; DOI=10.1016/j.cell.2010.10.010;
RA Fang M., Shen Z., Huang S., Zhao L., Chen S., Mak T.W., Wang X.;
RT "The ER UDPase ENTPD5 promotes protein N-glycosylation, the Warburg effect,
RT and proliferation in the PTEN pathway.";
RL Cell 143:711-724(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP,
CC IDP and UDP compared to ADP and CDP (PubMed:15698960, PubMed:10400613).
CC In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as
CC an end-product feedback inhibitor of the UDP-Glc:glycoprotein
CC glucosyltransferases. UMP can be transported back by an UDP-sugar
CC antiporter to the cytosol where it is consumed to regenerate UDP-
CC glucose. Therefore, it positively regulates protein reglucosylation by
CC clearing UDP from the ER lumen and by promoting the regeneration of
CC UDP-glucose. Protein reglucosylation is essential to proper
CC glycoprotein folding and quality control in the ER (By similarity).
CC {ECO:0000250|UniProtKB:Q9WUZ9, ECO:0000269|PubMed:10400613,
CC ECO:0000269|PubMed:15698960}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC Evidence={ECO:0000305|PubMed:15698960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:15698960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC Evidence={ECO:0000305|PubMed:15698960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:15698960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC Evidence={ECO:0000305|PubMed:15698960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:15698960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC Evidence={ECO:0000305|PubMed:15698960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:10400613};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC Evidence={ECO:0000305|PubMed:10400613};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:10400613};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC Evidence={ECO:0000305|PubMed:10400613};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for GDP {ECO:0000269|PubMed:15698960};
CC Vmax=34 mmol/h/mg enzyme with GDP as substrate
CC {ECO:0000269|PubMed:15698960};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:15698960};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9WUZ9}.
CC -!- SUBUNIT: Monomer; active form (PubMed:12508121). Homodimer; disulfide-
CC linked. Homodimers are enzymatically inactive.
CC {ECO:0000269|PubMed:11041857, ECO:0000269|PubMed:12508121}.
CC -!- INTERACTION:
CC O75356; P42858: HTT; NbExp=3; IntAct=EBI-7416931, EBI-466029;
CC O75356; P50539: MXI1; NbExp=3; IntAct=EBI-7416931, EBI-752241;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000269|PubMed:10400613,
CC ECO:0000269|PubMed:15698960}.
CC -!- TISSUE SPECIFICITY: Expressed in adult liver, kidney, prostate, testis
CC and colon. Much weaker expression in other tissues.
CC {ECO:0000269|PubMed:9676430}.
CC -!- INDUCTION: Up-regulated in cell lines and primary tumor samples with
CC active AKT1. {ECO:0000269|PubMed:21074248}.
CC -!- PTM: N-glycosylated; high-mannose type (By similarity). Glycosylation
CC is not essential for enzymatic activity. {ECO:0000250|UniProtKB:Q9WUZ9,
CC ECO:0000269|PubMed:11041857, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19159218}.
CC -!- MISCELLANEOUS: May mediate some of the cancer-related phenotypes
CC associated with AKT1 activation: its up-regulation by AKT1 leads to the
CC elevation of aerobic glycolysis seen in tumor cells, a phenomenon known
CC as the Warburg effect. {ECO:0000305|PubMed:21074248}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF039918; AAC39885.1; -; mRNA.
DR EMBL; AF136572; AAK82950.1; -; mRNA.
DR EMBL; AY430094; AAR06666.1; -; mRNA.
DR EMBL; AC005480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81153.1; -; Genomic_DNA.
DR EMBL; BC130485; AAI30486.1; -; mRNA.
DR EMBL; BC130487; AAI30488.1; -; mRNA.
DR CCDS; CCDS9825.1; -.
DR RefSeq; NP_001240.1; NM_001249.3.
DR RefSeq; NP_001308914.1; NM_001321985.1.
DR RefSeq; NP_001308915.1; NM_001321986.1.
DR RefSeq; NP_001308916.1; NM_001321987.1.
DR RefSeq; NP_001308917.1; NM_001321988.1.
DR RefSeq; XP_005268281.1; XM_005268224.3.
DR RefSeq; XP_016877302.1; XM_017021813.1.
DR AlphaFoldDB; O75356; -.
DR SMR; O75356; -.
DR BioGRID; 107395; 10.
DR IntAct; O75356; 7.
DR MINT; O75356; -.
DR STRING; 9606.ENSP00000335246; -.
DR ChEMBL; CHEMBL4523151; -.
DR DrugBank; DB00152; Thiamine.
DR GlyConnect; 1194; 3 N-Linked glycans (1 site).
DR GlyGen; O75356; 2 sites, 3 N-linked glycans (1 site).
DR iPTMnet; O75356; -.
DR PhosphoSitePlus; O75356; -.
DR BioMuta; ENTPD5; -.
DR EPD; O75356; -.
DR jPOST; O75356; -.
DR MassIVE; O75356; -.
DR MaxQB; O75356; -.
DR PaxDb; O75356; -.
DR PeptideAtlas; O75356; -.
DR PRIDE; O75356; -.
DR ProteomicsDB; 49923; -.
DR Antibodypedia; 148; 260 antibodies from 31 providers.
DR DNASU; 957; -.
DR Ensembl; ENST00000334696.11; ENSP00000335246.6; ENSG00000187097.13.
DR GeneID; 957; -.
DR KEGG; hsa:957; -.
DR MANE-Select; ENST00000334696.11; ENSP00000335246.6; NM_001249.5; NP_001240.1.
DR UCSC; uc010tuo.3; human.
DR CTD; 957; -.
DR DisGeNET; 957; -.
DR GeneCards; ENTPD5; -.
DR HGNC; HGNC:3367; ENTPD5.
DR HPA; ENSG00000187097; Tissue enhanced (intestine, kidney, liver).
DR MalaCards; ENTPD5; -.
DR MIM; 603162; gene.
DR neXtProt; NX_O75356; -.
DR OpenTargets; ENSG00000187097; -.
DR PharmGKB; PA27802; -.
DR VEuPathDB; HostDB:ENSG00000187097; -.
DR eggNOG; KOG1385; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_0_2_1; -.
DR InParanoid; O75356; -.
DR OMA; DKPIVQY; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; O75356; -.
DR TreeFam; TF315029; -.
DR PathwayCommons; O75356; -.
DR Reactome; R-HSA-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SignaLink; O75356; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 957; 7 hits in 1077 CRISPR screens.
DR ChiTaRS; ENTPD5; human.
DR GeneWiki; ENTPD5; -.
DR GenomeRNAi; 957; -.
DR Pharos; O75356; Tbio.
DR PRO; PR:O75356; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O75356; protein.
DR Bgee; ENSG00000187097; Expressed in mucosa of sigmoid colon and 181 other tissues.
DR ExpressionAtlas; O75356; baseline and differential.
DR Genevisible; O75356; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:1990003; F:inosine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; ISS:UniProtKB.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006256; P:UDP catabolic process; ISS:UniProtKB.
DR GO; GO:0006011; P:UDP-glucose metabolic process; ISS:UniProtKB.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Magnesium; Proto-oncogene; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..428
FT /note="Nucleoside diphosphate phosphatase ENTPD5"
FT /id="PRO_0000019908"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WUZ9"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..303
FT /evidence="ECO:0000250"
FT DISULFID 363..377
FT /evidence="ECO:0000250"
FT VARIANT 314
FT /note="K -> R (in dbSNP:rs17094434)"
FT /id="VAR_050308"
FT MUTAGEN 39
FT /note="C->S: No effect on protein stability. No effect on
FT nucleoside-diphosphatase activity."
FT /evidence="ECO:0000269|PubMed:15698960"
SQ SEQUENCE 428 AA; 47517 MW; 830437A155DE4DDD CRC64;
MATSWGTVFF MLVVSCVCSA VSHRNQQTWF EGIFLSSMCP INVSASTLYG IMFDAGSTGT
RIHVYTFVQK MPGQLPILEG EVFDSVKPGL SAFVDQPKQG AETVQGLLEV AKDSIPRSHW
KKTPVVLKAT AGLRLLPEHK AKALLFEVKE IFRKSPFLVP KGSVSIMDGS DEGILAWVTV
NFLTGQLHGH RQETVGTLDL GGASTQITFL PQFEKTLEQT PRGYLTSFEM FNSTYKLYTH
SYLGFGLKAA RLATLGALET EGTDGHTFRS ACLPRWLEAE WIFGGVKYQY GGNQEGEVGF
EPCYAEVLRV VRGKLHQPEE VQRGSFYAFS YYYDRAVDTD MIDYEKGGIL KVEDFERKAR
EVCDNLENFT SGSPFLCMDL SYITALLKDG FGFADSTVLQ LTKKVNNIET GWALGATFHL
LQSLGISH
