UPP2_HUMAN
ID UPP2_HUMAN Reviewed; 317 AA.
AC O95045; B3KV87;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Uridine phosphorylase 2 {ECO:0000303|PubMed:12849978};
DE Short=UPase 2 {ECO:0000303|PubMed:12849978};
DE Short=UrdPase 2 {ECO:0000303|PubMed:12849978};
DE EC=2.4.2.3 {ECO:0000269|PubMed:12849978, ECO:0000269|PubMed:21855639};
GN Name=UPP2;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=12849978; DOI=10.1016/s0006-291x(03)01062-3;
RA Johansson M.;
RT "Identification of a novel human uridine phosphorylase.";
RL Biochem. Biophys. Res. Commun. 307:41-46(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5] {ECO:0007744|PDB:2XRF}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 23-317 IN COMPLEX WITH URACIL,
RP AND SUBUNIT.
RA Welin M., Moche M., Arrowsmith C.H., Berglund H., Bountra C., Collins R.,
RA Edwards A.M., Flodin S., Flores A., Graslund S., Hammarstrom M.,
RA Johansson I., Karlberg T., Kol S., Kotenyova T., Kouznetsova E., Nyman T.,
RA Persson C., Schuler H., Schutz P., Siponen M.I., Thorsell A.G.,
RA Tresaugues L., Van Der Berg S., Wahlberg E., Weigelt J., Nordlund P.;
RT "Crystal structure of human uridine phosphorylase 2.";
RL Submitted (SEP-2010) to the PDB data bank.
RN [6] {ECO:0007744|PDB:3P0E, ECO:0007744|PDB:3P0F}
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-314 IN COMPLEX WITH PHOSPHATE
RP AND INHIBITOR BAU, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=21855639; DOI=10.1016/j.jsb.2011.08.002;
RA Roosild T.P., Castronovo S., Villoso A., Ziemba A., Pizzorno G.;
RT "A novel structural mechanism for redox regulation of uridine phosphorylase
RT 2 activity.";
RL J. Struct. Biol. 176:229-237(2011).
CC -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine
CC and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate
CC (PubMed:12849978, PubMed:21855639). The produced molecules are then
CC utilized as carbon and energy sources or in the rescue of pyrimidine
CC bases for nucleotide synthesis (Probable). Shows broad substrate
CC specificity and accepts uridine, deoxyuridine, and thymidine as well as
CC the two pyrimidine nucleoside analogs 5-fluorouridine and 5-fluoro-
CC 2(')-deoxyuridine as substrates (PubMed:12849978).
CC {ECO:0000269|PubMed:12849978, ECO:0000269|PubMed:21855639,
CC ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3;
CC Evidence={ECO:0000269|PubMed:12849978, ECO:0000269|PubMed:21855639};
CC -!- ACTIVITY REGULATION: A conditional disulfide bridge can form within the
CC protein that dislocates a critical phosphate-coordinating arginine Arg-
CC 100 away from the active site, disabling the enzyme.
CC {ECO:0000269|PubMed:21855639}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=76 uM for uridine {ECO:0000269|PubMed:12849978};
CC KM=300 uM for deoxyuridine {ECO:0000269|PubMed:12849978};
CC KM=73 uM for thymidine {ECO:0000269|PubMed:12849978};
CC KM=24 uM for 5-fluorouridine {ECO:0000269|PubMed:12849978};
CC KM=427 uM for 5-fluoro-2(')-deoxyuridine
CC {ECO:0000269|PubMed:12849978};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC uracil from uridine (phosphorylase route): step 1/1.
CC {ECO:0000269|PubMed:12849978}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21855639, ECO:0000269|Ref.5}.
CC -!- INTERACTION:
CC O95045; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-10191025, EBI-747107;
CC O95045; O95045: UPP2; NbExp=3; IntAct=EBI-10191025, EBI-10191025;
CC O95045-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11528386, EBI-739832;
CC O95045-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11528386, EBI-16439278;
CC O95045-2; Q13084: MRPL28; NbExp=3; IntAct=EBI-11528386, EBI-723426;
CC O95045-2; Q8IUQ4-2: SIAH1; NbExp=6; IntAct=EBI-11528386, EBI-11522811;
CC O95045-2; A0A0S2Z6U5: UPP2; NbExp=3; IntAct=EBI-11528386, EBI-16432858;
CC O95045-2; O95045-2: UPP2; NbExp=6; IntAct=EBI-11528386, EBI-11528386;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95045-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95045-2; Sequence=VSP_043756;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney.
CC {ECO:0000269|PubMed:12849978}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33529.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY225131; AAO61681.1; -; mRNA.
DR EMBL; AK122743; BAG53699.1; -; mRNA.
DR EMBL; AC005539; AAD12227.1; -; Genomic_DNA.
DR EMBL; BC033529; AAH33529.1; ALT_INIT; mRNA.
DR CCDS; CCDS2207.1; -. [O95045-1]
DR CCDS; CCDS46435.1; -. [O95045-2]
DR RefSeq; NP_001128570.1; NM_001135098.1. [O95045-2]
DR RefSeq; NP_775491.1; NM_173355.3. [O95045-1]
DR PDB; 2XRF; X-ray; 2.30 A; A/B/C=23-317.
DR PDB; 3P0E; X-ray; 2.00 A; A/B/C/D/E/F=21-314.
DR PDB; 3P0F; X-ray; 1.54 A; A=21-314.
DR PDBsum; 2XRF; -.
DR PDBsum; 3P0E; -.
DR PDBsum; 3P0F; -.
DR AlphaFoldDB; O95045; -.
DR SMR; O95045; -.
DR BioGRID; 127387; 9.
DR IntAct; O95045; 5.
DR STRING; 9606.ENSP00000474090; -.
DR DrugBank; DB00544; Fluorouracil.
DR iPTMnet; O95045; -.
DR PhosphoSitePlus; O95045; -.
DR BioMuta; UPP2; -.
DR MassIVE; O95045; -.
DR PaxDb; O95045; -.
DR PeptideAtlas; O95045; -.
DR PRIDE; O95045; -.
DR ProteomicsDB; 50627; -. [O95045-1]
DR ProteomicsDB; 50628; -. [O95045-2]
DR Antibodypedia; 33709; 136 antibodies from 22 providers.
DR DNASU; 151531; -.
DR Ensembl; ENST00000005756.5; ENSP00000005756.5; ENSG00000007001.13. [O95045-1]
DR Ensembl; ENST00000605860.5; ENSP00000474090.1; ENSG00000007001.13. [O95045-2]
DR GeneID; 151531; -.
DR KEGG; hsa:151531; -.
DR MANE-Select; ENST00000005756.5; ENSP00000005756.5; NM_173355.4; NP_775491.1.
DR UCSC; uc002tzp.4; human. [O95045-1]
DR CTD; 151531; -.
DR DisGeNET; 151531; -.
DR GeneCards; UPP2; -.
DR HGNC; HGNC:23061; UPP2.
DR HPA; ENSG00000007001; Group enriched (kidney, liver).
DR MIM; 617340; gene.
DR neXtProt; NX_O95045; -.
DR OpenTargets; ENSG00000007001; -.
DR PharmGKB; PA134866434; -.
DR VEuPathDB; HostDB:ENSG00000007001; -.
DR eggNOG; KOG3728; Eukaryota.
DR GeneTree; ENSGT00940000161094; -.
DR HOGENOM; CLU_054104_0_0_1; -.
DR InParanoid; O95045; -.
DR OrthoDB; 1423938at2759; -.
DR PhylomeDB; O95045; -.
DR TreeFam; TF314310; -.
DR BRENDA; 2.4.2.3; 2681.
DR PathwayCommons; O95045; -.
DR Reactome; R-HSA-73614; Pyrimidine salvage.
DR Reactome; R-HSA-73621; Pyrimidine catabolism.
DR SABIO-RK; O95045; -.
DR SignaLink; O95045; -.
DR UniPathway; UPA00574; UER00633.
DR BioGRID-ORCS; 151531; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; UPP2; human.
DR EvolutionaryTrace; O95045; -.
DR GenomeRNAi; 151531; -.
DR Pharos; O95045; Tbio.
DR PRO; PR:O95045; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95045; protein.
DR Bgee; ENSG00000007001; Expressed in kidney epithelium and 59 other tissues.
DR ExpressionAtlas; O95045; baseline and differential.
DR Genevisible; O95045; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045098; C:type III intermediate filament; IDA:UniProtKB.
DR GO; GO:0047847; F:deoxyuridine phosphorylase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004850; F:uridine phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0006249; P:dCMP catabolic process; IDA:MGI.
DR GO; GO:0009116; P:nucleoside metabolic process; NAS:UniProtKB.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006218; P:uridine catabolic process; IDA:UniProtKB.
DR GO; GO:0046108; P:uridine metabolic process; NAS:UniProtKB.
DR CDD; cd17763; UP_hUPP-like; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR010059; Uridine_phosphorylase_euk.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01719; euk_UDPppase; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycosyltransferase;
KW Redox-active center; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="Uridine phosphorylase 2"
FT /id="PRO_0000063193"
FT BINDING 66
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:21855639,
FT ECO:0007744|PDB:3P0E"
FT BINDING 100
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:21855639,
FT ECO:0007744|PDB:3P0E"
FT BINDING 144..147
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:21855639,
FT ECO:0007744|PDB:3P0E"
FT BINDING 148..149
FT /ligand="uridine"
FT /ligand_id="ChEBI:CHEBI:16704"
FT /evidence="ECO:0000305|PubMed:21855639,
FT ECO:0007744|PDB:2XRF, ECO:0007744|PDB:3P0E,
FT ECO:0007744|PDB:3P0F"
FT BINDING 223..225
FT /ligand="uridine"
FT /ligand_id="ChEBI:CHEBI:16704"
FT /evidence="ECO:0000305|PubMed:21855639,
FT ECO:0007744|PDB:2XRF, ECO:0007744|PDB:3P0E,
FT ECO:0007744|PDB:3P0F"
FT DISULFID 95..102
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:21855639,
FT ECO:0007744|PDB:3P0F"
FT VAR_SEQ 1
FT /note="M -> MLAPGCELDPDQEVVRTRPEDVPASPSTSTMIVSVLRPPSHASCTAC
FT GTVTFHIVERM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043756"
FT VARIANT 10
FT /note="R -> S (in dbSNP:rs6710480)"
FT /id="VAR_024431"
FT VARIANT 78
FT /note="M -> L (in dbSNP:rs7561584)"
FT /id="VAR_034580"
FT CONFLICT 153
FT /note="I -> M (in Ref. 1; AAO61681)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="T -> R (in Ref. 1; AAO61681)"
FT /evidence="ECO:0000305"
FT CONFLICT 256..262
FT /note="ESTVFAA -> GIYSVCS (in Ref. 1; AAO61681)"
FT /evidence="ECO:0000305"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3P0F"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3P0E"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:3P0E"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 141..153
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:3P0F"
FT STRAND 270..280
FT /evidence="ECO:0007829|PDB:3P0F"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:3P0F"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:3P0F"
SQ SEQUENCE 317 AA; 35527 MW; 69F6BA1DC44977A3 CRC64;
MASVIPASNR SMRSDRNTYV GKRFVHVKNP YLDLMDEDIL YHLDLGTKTH NLPAMFGDVK
FVCVGGSPNR MKAFALFMHK ELGFEEAEED IKDICAGTDR YCMYKTGPVL AISHGMGIPS
ISIMLHELIK LLHHARCCDV TIIRIGTSGG IGIAPGTVVI TDIAVDSFFK PRFEQVILDN
IVTRSTELDK ELSEELFNCS KEIPNFPTLV GHTMCTYDFY EGQGRLDGAL CSFSREKKLD
YLKRAFKAGV RNIEMESTVF AAMCGLCGLK AAVVCVTLLD RLDCDQINLP HDVLVEYQQR
PQLLISNFIR RRLGLCD
