UD18_RAT
ID UD18_RAT Reviewed; 530 AA.
AC Q64634;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=UDP-glucuronosyltransferase 1A8 {ECO:0000305};
DE Short=UGT1A8;
DE EC=2.4.1.17 {ECO:0000250|UniProtKB:Q9HAW9};
DE AltName: Full=A3;
DE AltName: Full=UDP-glucuronosyltransferase 1-8;
DE Short=UDPGT 1-8;
DE Short=UGT1*8;
DE Short=UGT1-08;
DE Short=UGT1.8;
DE Flags: Precursor;
GN Name=Ugt1a8 {ECO:0000312|RGD:708474}; Synonyms=Ugt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=7608130; DOI=10.1093/jb/117.2.392;
RA Emi Y., Ikushiro S., Iyanagi T.;
RT "Drug-responsive and tissue-specific alternative expression of multiple
RT first exons in rat UDP-glucuronosyltransferase family 1 (UGT1) gene
RT complex.";
RL J. Biochem. 117:392-399(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 286-530.
RC TISSUE=Liver;
RX PubMed=2112380; DOI=10.1016/0006-291x(90)91462-2;
RA Sato H., Koiwai O., Tanabe K., Kashiwamata S.;
RT "Isolation and sequencing of rat liver bilirubin UDP-
RT glucuronosyltransferase cDNA: possible alternate splicing of a common
RT primary transcript.";
RL Biochem. Biophys. Res. Commun. 169:260-264(1990).
CC -!- FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II
CC biotransformation reactions in which lipophilic substrates are
CC conjugated with glucuronic acid to increase the metabolite's water
CC solubility, thereby facilitating excretion into either the urine or
CC bile. Essential for the elimination and detoxification of drugs,
CC xenobiotics and endogenous compounds. Catalyzes the glucuronidation of
CC endogenous steroid hormones such as androgens and estrogens. Produces
CC dihydrotestosterone (DHT) diglucuronide from the DHT after two
CC subsequent glucoronidation steps. Also catalyzes of the glucuronidation
CC the isoflavones genistein, daidzein, glycitein, formononetin, biochanin
CC A and prunetin, which are phytoestrogens with anticancer and
CC cardiovascular properties. Involved in the glucuronidation of the AGTR1
CC angiotensin receptor antagonist caderastan, a drug which can inhibit
CC the effect of angiotensin II. {ECO:0000250|UniProtKB:Q9HAW9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol
CC 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52460,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:136641;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52461;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-
CC estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:52868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC ChEBI:CHEBI:57529, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone + UDP-alpha-D-glucuronate = estrone 3-O-(beta-D-
CC glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52476, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:136634; Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52477;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16alpha,17alpha-estriol + UDP-alpha-D-glucuronate =
CC 16alpha,17alpha-estriol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:52924, ChEBI:CHEBI:15378, ChEBI:CHEBI:42156,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136882;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52925;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 2-
CC hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:53004, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136931;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53005;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-
CC estradiol 2-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:53032, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136933;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53033;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyestrone + UDP-alpha-D-glucuronate = 2-hydroxyestrone
CC 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53048,
CC ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:136967;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53049;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 4-
CC hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:53036, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:62845, ChEBI:CHEBI:136936;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53037;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-
CC estradiol 4-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:53040, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:62845, ChEBI:CHEBI:136937;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53041;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxyestrone + UDP-alpha-D-glucuronate = 4-hydroxyestrone
CC 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53052,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:87602, ChEBI:CHEBI:136969;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53053;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxyestrone + UDP-alpha-D-glucuronate = estrone 4-O-
CC (beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53060,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:87602, ChEBI:CHEBI:136970;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53061;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methoxy-17beta-estradiol + UDP-alpha-D-glucuronate = 2-
CC methoxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:53072, ChEBI:CHEBI:15378, ChEBI:CHEBI:28955,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136974;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53073;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methoxyestrone + UDP-alpha-D-glucuronate = 2-methoxyestrone
CC 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53064,
CC ChEBI:CHEBI:1189, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:136971;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53065;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methoxy-17beta-estradiol + UDP-alpha-D-glucuronate = 4-
CC methoxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:53080, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:136975, ChEBI:CHEBI:136976;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53081;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methoxyestrone + UDP-alpha-D-glucuronate = 4-methoxyestrone
CC 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53068,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:136972, ChEBI:CHEBI:136973;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53069;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + UDP-alpha-D-
CC glucuronate = 5alpha-dihydrotestosterone 17-O-(beta-D-glucuronate) +
CC H(+) + UDP; Xref=Rhea:RHEA:53000, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16330, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:136914; Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53001;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-dihydrotestosterone 17-O-(beta-D-glucuronate) + UDP-
CC alpha-D-glucuronate = 5alpha-dihydrotestosterone 17-O-[beta-D-
CC glucuronosyl-(1->2)-glucuronate] + H(+) + UDP; Xref=Rhea:RHEA:53388,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:136914, ChEBI:CHEBI:136916;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53389;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prunetin + UDP-alpha-D-glucuronate = prunetin-4'-O-beta-D-
CC glucuronide + UDP; Xref=Rhea:RHEA:63588, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:147403, ChEBI:CHEBI:147404;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63589;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prunetin + UDP-alpha-D-glucuronate = prunetin-5-O-beta-D-
CC glucuronide + UDP; Xref=Rhea:RHEA:63612, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:147403, ChEBI:CHEBI:147405;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63613;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=candesartan + UDP-alpha-D-glucuronate = candesartan O-beta-D-
CC glucuronoside + UDP; Xref=Rhea:RHEA:63724, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:149509, ChEBI:CHEBI:149522;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63725;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=mycophenolate + UDP-alpha-D-glucuronate = H(+) + mycophenolate
CC 7-O-beta-D-glucuronide + UDP; Xref=Rhea:RHEA:63704,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:62932, ChEBI:CHEBI:149486;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63705;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW9};
CC -!- SUBUNIT: Homodimers. Homooligomer. Interacts with UGT1A1, UGT1A3,
CC UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9 and UGT1A10 to form
CC heterodimers. {ECO:0000250|UniProtKB:Q9HAW9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9HAW9}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=UGT1A8 is one of the isoforms produced at the UGT1A complex
CC locus. The UGT1A complex locus produces different isoforms based on
CC alternative use of promoters, first exons and terminal exons.
CC {ECO:0000250|UniProtKB:Q9HAW9};
CC Name=1;
CC IsoId=Q64634-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D38063; BAA07259.1; -; Genomic_DNA.
DR EMBL; M34007; AAA42312.1; ALT_TERM; mRNA.
DR AlphaFoldDB; Q64634; -.
DR SMR; Q64634; -.
DR STRING; 10116.ENSRNOP00000065158; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q64634; 3 sites.
DR PaxDb; Q64634; -.
DR PRIDE; Q64634; -.
DR UCSC; RGD:708474; rat. [Q64634-1]
DR RGD; 708474; Ugt1a8.
DR eggNOG; KOG1192; Eukaryota.
DR InParanoid; Q64634; -.
DR PhylomeDB; Q64634; -.
DR BRENDA; 2.4.1.17; 5301.
DR Reactome; R-RNO-156588; Glucuronidation.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR PRO; PR:Q64634; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:RGD.
DR GO; GO:0005504; F:fatty acid binding; ISO:RGD.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0005496; F:steroid binding; ISO:RGD.
DR GO; GO:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0046226; P:coumarin catabolic process; IDA:RGD.
DR GO; GO:0051552; P:flavone metabolic process; ISO:RGD.
DR GO; GO:0052696; P:flavonoid glucuronidation; ISO:RGD.
DR GO; GO:0001889; P:liver development; IBA:GO_Central.
DR GO; GO:0018411; P:protein glucuronidation; TAS:RGD.
DR GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
DR GO; GO:0052697; P:xenobiotic glucuronidation; ISO:RGD.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..530
FT /note="UDP-glucuronosyltransferase 1A8"
FT /id="PRO_0000036022"
FT TRANSMEM 488..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 530 AA; 60060 MW; 507098AE81D4AC5C CRC64;
MAPSGCPPSL PLCVCLFLAS GFAQAGRLLV VPMDGSHWFT MQMIVEKLSH RGHEVVVVIP
EVSWHMGKSL NFTVKLLLVL NTLEDLNYHF KFFAHNQWKT QEVGMFSLLK HSGKGFFELL
FSHCRSLFKD KKLVEYLKQS SFDAVFLDPF DVCGLILAKY FSLPSVVFSG GIFCHYLDEG
AQCPSPPSYV PRILSKFTDT MTFKERVWNH LSYMKERAFC PYFFKTAVEI ASEVLQTPVT
MRDLFSPVSI WMFRTDFVLE FPRPMMPNMV YIGGINCHQG KPLSKEFEAY VNASGEHGIV
VFSLGSMVSE IPEKKAMEIA EALGRIPQTL LWRYTGTRPS NLAKNTILVK WLPQNDLLGH
PKARAFITHS GSHGIYEGIC NGVPMVMMPL FGDQMDNAKR METRGAGVTL NVLEMTADDL
ENALKTVINN KSYKENIMRL SSLHKDRPIE PLDLAVFWVE YVMRHKGAPH LRPAAHDLTW
YQYHSLDVIG FLLAIVLTVV FIVYKSCAYG CRKCFGGKGR VKKSHKSKTH
