ENTP5_MOUSE
ID ENTP5_MOUSE Reviewed; 427 AA.
AC Q9WUZ9; O70214; Q544J4; Q8BR23; Q8CD29;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 5 {ECO:0000305|PubMed:10369669, ECO:0000305|PubMed:21074248};
DE Short=NTPDase 5;
DE EC=3.6.1.6 {ECO:0000269|PubMed:10369669, ECO:0000269|PubMed:21074248};
DE AltName: Full=CD39 antigen-like 4;
DE AltName: Full=ER-UDPase {ECO:0000303|PubMed:10369669};
DE AltName: Full=Guanosine-diphosphatase ENTPD5;
DE Short=GDPase ENTPD5;
DE AltName: Full=Nucleoside diphosphatase;
DE AltName: Full=Uridine-diphosphatase ENTPD5;
DE Short=UDPase ENTPD5;
DE Flags: Precursor;
GN Name=Entpd5; Synonyms=Cd39l4;
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].
RC TISSUE=Testis;
RX PubMed=9457681; DOI=10.1007/s003359900710;
RA Chadwick B.P., Williamson J., Sheer D., Frischauf A.-M.;
RT "cDNA cloning and chromosomal mapping of a mouse gene with homology to
RT NTPases.";
RL Mamm. Genome 9:162-164(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10369669; DOI=10.1093/emboj/18.12.3282;
RA Trombetta E.S., Helenius A.;
RT "Glycoprotein reglucosylation and nucleotide sugar utilization in the
RT secretory pathway: identification of a nucleoside diphosphatase in the
RT endoplasmic reticulum.";
RL EMBO J. 18:3282-3292(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=10506756;
RX DOI=10.1002/(sici)1098-2744(199910)26:2<130::aid-mc7>3.0.co;2-n;
RA Recio J.A., Zambrano N., de La Pena L., Powers C., Siwarski D., Huppi K.,
RA Notario V.;
RT "cDNA isolation, expression, and chromosomal localization of the mouse pcph
RT proto-oncogene.";
RL Mol. Carcinog. 26:130-136(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone, Corpora quadrigemina, Head, Kidney, Testis, Thymus, and
RC Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 DISRUPTION PHENOTYPE.
RX PubMed=19176496; DOI=10.1354/vp.08-vp-0201-r-am;
RA Read R., Hansen G., Kramer J., Finch R., Li L., Vogel P.;
RT "Ectonucleoside triphosphate diphosphohydrolase type 5 (Entpd5)-deficient
RT mice develop progressive hepatopathy, hepatocellular tumors, and
RT spermatogenic arrest.";
RL Vet. Pathol. 46:491-504(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, 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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP INDUCTION, ACTIVE SITE, AND MUTAGENESIS OF GLU-171.
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).
CC -!- FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP,
CC IDP and UDP compared to ADP and CDP (PubMed:10369669, PubMed:21074248).
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 (PubMed:21074248). Therefore, it positively regulates protein
CC reglucosylation by clearing UDP from the ER lumen and by promoting the
CC regeneration of UDP-glucose (PubMed:21074248). Protein reglucosylation
CC is essential to proper glycoprotein folding and quality control in the
CC ER (PubMed:21074248). {ECO:0000269|PubMed:10369669,
CC ECO:0000269|PubMed:21074248}.
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:10369669, ECO:0000269|PubMed:21074248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC Evidence={ECO:0000269|PubMed:10369669};
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:21074248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC Evidence={ECO:0000305|PubMed:21074248};
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:10369669, ECO:0000269|PubMed:21074248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC Evidence={ECO:0000305|PubMed:10369669};
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:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC Evidence={ECO:0000250|UniProtKB:O75356};
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:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC Evidence={ECO:0000250|UniProtKB:O75356};
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:0000250|UniProtKB:O75356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC Evidence={ECO:0000250|UniProtKB:O75356};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10369669};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10369669};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:10369669};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:21074248}.
CC -!- SUBUNIT: Monomer; active form. Homodimer; disulfide-linked. Homodimers
CC are enzymatically inactive. {ECO:0000250|UniProtKB:O75356}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:10369669}. Secreted {ECO:0000250|UniProtKB:O75356}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10369669}.
CC -!- INDUCTION: Expressed in response to phosphoinositide 3-kinase (PI3K)
CC signaling. Activation of PI3K results in FOXO phosphorylation by AKT1
CC and loss of ENTPD5 transcriptional repression. Up-regulated in PTEN-
CC deficient cells. {ECO:0000269|PubMed:21074248}.
CC -!- PTM: N-glycosylated; high-mannose type. {ECO:0000269|PubMed:10369669,
CC ECO:0000269|PubMed:21074248}.
CC -!- DISRUPTION PHENOTYPE: Mice display hepatopathy and aspermia. The
CC hepatopathy is progressive and characterized by centrilobular
CC hepatocyte hypertrophy, oval cell proliferation, bile staining of
CC Kupffer cells, and hepatocyte degeneration with increasing incidence
CC and severity of degenerative lesions, development of multiple foci of
CC cellular alteration, and hepatocellular neoplasia with age.
CC {ECO:0000269|PubMed:19176496}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF006482; AAC05181.1; -; mRNA.
DR EMBL; AJ238636; CAB45533.1; -; mRNA.
DR EMBL; AF136571; AAK82949.1; -; mRNA.
DR EMBL; AK002618; BAB22234.1; -; mRNA.
DR EMBL; AK031581; BAC27461.1; -; mRNA.
DR EMBL; AK036641; BAC29515.1; -; mRNA.
DR EMBL; AK037736; BAC29861.1; -; mRNA.
DR EMBL; AK045828; BAC32507.1; -; mRNA.
DR EMBL; AK079267; BAC37592.1; -; mRNA.
DR EMBL; AK080265; BAC37862.1; -; mRNA.
DR EMBL; AK081435; BAC38219.1; -; mRNA.
DR EMBL; AK088455; BAC40362.1; -; mRNA.
DR EMBL; AK160950; BAE36110.1; -; mRNA.
DR EMBL; CH466590; EDL02793.1; -; Genomic_DNA.
DR EMBL; CH466590; EDL02796.1; -; Genomic_DNA.
DR EMBL; CH466590; EDL02797.1; -; Genomic_DNA.
DR EMBL; BC015247; AAH15247.1; -; mRNA.
DR CCDS; CCDS26045.1; -.
DR RefSeq; NP_001021385.1; NM_001026214.2.
DR RefSeq; NP_001272978.1; NM_001286049.1.
DR RefSeq; NP_001272987.1; NM_001286058.1.
DR RefSeq; NP_031673.2; NM_007647.3.
DR AlphaFoldDB; Q9WUZ9; -.
DR SMR; Q9WUZ9; -.
DR STRING; 10090.ENSMUSP00000071939; -.
DR ChEMBL; CHEMBL4523501; -.
DR GlyGen; Q9WUZ9; 1 site.
DR iPTMnet; Q9WUZ9; -.
DR PhosphoSitePlus; Q9WUZ9; -.
DR EPD; Q9WUZ9; -.
DR jPOST; Q9WUZ9; -.
DR MaxQB; Q9WUZ9; -.
DR PaxDb; Q9WUZ9; -.
DR PRIDE; Q9WUZ9; -.
DR ProteomicsDB; 277878; -.
DR Antibodypedia; 148; 260 antibodies from 31 providers.
DR DNASU; 12499; -.
DR Ensembl; ENSMUST00000021662; ENSMUSP00000021662; ENSMUSG00000021236.
DR Ensembl; ENSMUST00000110272; ENSMUSP00000105901; ENSMUSG00000021236.
DR Ensembl; ENSMUST00000117286; ENSMUSP00000114011; ENSMUSG00000021236.
DR Ensembl; ENSMUST00000120942; ENSMUSP00000112516; ENSMUSG00000021236.
DR Ensembl; ENSMUST00000122194; ENSMUSP00000113106; ENSMUSG00000021236.
DR GeneID; 12499; -.
DR KEGG; mmu:12499; -.
DR UCSC; uc007ofd.2; mouse.
DR CTD; 957; -.
DR MGI; MGI:1321385; Entpd5.
DR VEuPathDB; HostDB:ENSMUSG00000021236; -.
DR eggNOG; KOG1385; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_0_2_1; -.
DR InParanoid; Q9WUZ9; -.
DR OMA; DKPIVQY; -.
DR OrthoDB; 1337265at2759; -.
DR Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 12499; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Entpd5; mouse.
DR PRO; PR:Q9WUZ9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9WUZ9; protein.
DR Bgee; ENSMUSG00000021236; Expressed in proximal tubule and 252 other tissues.
DR ExpressionAtlas; Q9WUZ9; baseline and differential.
DR Genevisible; Q9WUZ9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; ISO:MGI.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; ISO:MGI.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:1990003; F:inosine-diphosphatase activity; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
DR GO; GO:0006256; P:UDP catabolic process; IDA:UniProtKB.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IMP: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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..427
FT /note="Ectonucleoside triphosphate diphosphohydrolase 5"
FT /id="PRO_0000019910"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21074248"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 271..302
FT /evidence="ECO:0000250"
FT DISULFID 362..376
FT /evidence="ECO:0000250"
FT MUTAGEN 171
FT /note="E->A: Loss of nucleoside-diphosphatase activity."
FT /evidence="ECO:0000305|PubMed:21074248"
FT CONFLICT 218
FT /note="Q -> K (in Ref. 4; BAC27461)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="F -> L (in Ref. 1; AAC05181)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..427
FT /note="DGTLLQLTKKVNNIETGWALGATFHLLQSLGITS -> ERHPLTAHKESEQH
FT RDWLGLGGHLSPAPVSGHHQLRPSSTSEACISEPVFSQEGVDSETFSDLSGKAWPETR
FT (in Ref. 1; AAC05181)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 47102 MW; 2F9DA2C342C55577 CRC64;
MATSWGAVFM LIIACVGSTV FYREQQTWFE GVFLSSMCPI NVSAGTFYGI MFDAGSTGTR
IHVYTFVQKT AGQLPFLEGE IFDSVKPGLS AFVDQPKQGA ETVQELLEVA KDSIPRSHWE
RTPVVLKATA GLRLLPEQKA QALLLEVEEI FKNSPFLVPD GSVSIMDGSY EGILAWVTVN
FLTGQLHGRG QETVGTLDLG GASTQITFLP QFEKTLEQTP RGYLTSFEMF NSTFKLYTHS
YLGFGLKAAR LATLGALEAK GTDGHTFRSA CLPRWLEAEW IFGGVKYQYG GNQEGEMGFE
PCYAEVLRVV QGKLHQPEEV RGSAFYAFSY YYDRAADTHL IDYEKGGVLK VEDFERKARE
VCDNLGSFSS GSPFLCMDLT YITALLKDGF GFADGTLLQL TKKVNNIETG WALGATFHLL
QSLGITS
