UD2A2_HUMAN
ID UD2A2_HUMAN Reviewed; 536 AA.
AC P0DTE5; B4E2F4; D3GER1; D3GER2; E9PDM7; J3KNA3; Q9Y4X1;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=UDP-glucuronosyltransferase 2A2 {ECO:0000303|PubMed:19858781};
DE Short=UDPGT 2A2;
DE EC=2.4.1.17 {ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:19858781, ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:23756265};
GN Name=UGT2A2 {ECO:0000312|HGNC:HGNC:28183};
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] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Nasal mucosa;
RX PubMed=19858781; DOI=10.1097/fpc.0b013e3283330767;
RA Sneitz N., Court M.H., Zhang X., Laajanen K., Yee K.K., Dalton P., Ding X.,
RA Finel M.;
RT "Human UDP-glucuronosyltransferase UGT2A2: cDNA construction, expression,
RT and functional characterization in comparison with UGT2A1 and UGT2A3.";
RL Pharmacogenet. Genomics 19:923-934(2009).
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18719240; DOI=10.1124/dmd.108.022731;
RA Itaeaho K., Mackenzie P.I., Ikushiro S., Miners J.O., Finel M.;
RT "The configuration of the 17-hydroxy group variably influences the
RT glucuronidation of beta-estradiol and epiestradiol by human UDP-
RT glucuronosyltransferases.";
RL Drug Metab. Dispos. 36:2307-2315(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23756265; DOI=10.1124/dmd.113.052613;
RA Perreault M., Gauthier-Landry L., Trottier J., Verreault M., Caron P.,
RA Finel M., Barbier O.;
RT "The Human UDP-glucuronosyltransferase UGT2A1 and UGT2A2 enzymes are highly
RT active in bile acid glucuronidation.";
RL Drug Metab. Dispos. 41:1616-1620(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23288867; DOI=10.1124/dmd.112.049072;
RA Sneitz N., Vahermo M., Mosorin J., Laakkonen L., Poirier D., Finel M.;
RT "Regiospecificity and stereospecificity of human UDP-
RT glucuronosyltransferases in the glucuronidation of estriol, 16-epiestriol,
RT 17-epiestriol, and 13-epiestradiol.";
RL Drug Metab. Dispos. 41:582-591(2013).
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 (PubMed:19858781, PubMed:18719240, PubMed:23756265,
CC PubMed:23288867). Essential for the elimination and detoxification of
CC drugs, xenobiotics and endogenous compounds (PubMed:19858781,
CC PubMed:23756265). Catalyzes the glucuronidation of endogenous estrogen
CC hormone estradiol (PubMed:18719240, PubMed:23288867). Contributes to
CC bile acid (BA) detoxification by catalyzing the glucuronidation of BA
CC substrates, which are natural detergents for dietary lipids absorption
CC (PubMed:23756265). Shows a potential role in detoxification of toxic
CC waste compounds in the amniotic fluid before birth, and air-born
CC chemical after birth (PubMed:19858781). {ECO:0000269|PubMed:18719240,
CC ECO:0000269|PubMed:19858781, ECO:0000269|PubMed:23288867,
CC ECO:0000269|PubMed:23756265}.
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:0000269|PubMed:18719240, ECO:0000269|PubMed:19858781,
CC ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:23756265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000305|PubMed:18719240, ECO:0000305|PubMed:19858781,
CC ECO:0000305|PubMed:23288867, ECO:0000305|PubMed:23756265};
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:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869;
CC Evidence={ECO:0000269|PubMed:23288867, ECO:0000305|PubMed:18719240};
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:0000269|PubMed:18719240};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52461;
CC Evidence={ECO:0000305|PubMed:18719240};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholate + UDP-alpha-D-glucuronate =
CC chenodeoxycholoyl-24-O-(beta-D-glucuronate) + UDP;
CC Xref=Rhea:RHEA:52940, ChEBI:CHEBI:36234, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:136899;
CC Evidence={ECO:0000269|PubMed:23756265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52941;
CC Evidence={ECO:0000305|PubMed:23756265};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lithocholate + UDP-alpha-D-glucuronate = lithocholoyl-24-O-
CC (beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52952, ChEBI:CHEBI:29744,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136902;
CC Evidence={ECO:0000269|PubMed:23756265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52953;
CC Evidence={ECO:0000305|PubMed:23756265};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=deoxycholate + UDP-alpha-D-glucuronate = deoxycholoyl-24-O-
CC (beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52948, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136901;
CC Evidence={ECO:0000269|PubMed:23756265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52949;
CC Evidence={ECO:0000305|PubMed:23756265};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hyocholate + UDP-alpha-D-glucuronate = hyocholoyl-24-O-(beta-
CC D-glucuronate) + UDP; Xref=Rhea:RHEA:52960, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:133661, ChEBI:CHEBI:136904;
CC Evidence={ECO:0000269|PubMed:23756265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52961;
CC Evidence={ECO:0000305|PubMed:23756265};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hyodeoxycholate + UDP-alpha-D-glucuronate = H(+) +
CC hyodeoxycholate 6-O-(beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58875, ChEBI:CHEBI:136905;
CC Evidence={ECO:0000269|PubMed:23756265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52965;
CC Evidence={ECO:0000305|PubMed:23756265};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45.4 uM for 17beta-estradiol/estradiol (when assaying
CC glucuronidation at position 3) {ECO:0000269|PubMed:18719240};
CC KM=55.1 uM for UDP-glucuronate (with 4-methyl-umbelliferone as
CC substrate) {ECO:0000269|PubMed:19858781};
CC KM=4469 uM for 4-nitrophenol {ECO:0000269|PubMed:19858781};
CC KM=2998 uM for 4-methyl-umbelliferone {ECO:0000269|PubMed:19858781};
CC KM=245 uM for 4-phenylphenol {ECO:0000269|PubMed:19858781};
CC KM=3442.9 uM for cholate (when assaying glucuronidation at position
CC 24) {ECO:0000269|PubMed:23756265};
CC KM=143.6 uM for chenodeoxycholate (when assaying glucuronidation at
CC position 24) {ECO:0000269|PubMed:23756265};
CC KM=107.1 uM for lithocholate (when assaying glucuronidation at
CC position 3) {ECO:0000269|PubMed:23756265};
CC KM=113.7 uM for lithocholate (when assaying glucuronidation at
CC position 24) {ECO:0000269|PubMed:23756265};
CC KM=178.3 uM for deoxycholate (when assaying glucuronidation at
CC position 3) {ECO:0000269|PubMed:23756265};
CC KM=189 uM for deoxycholate (when assaying glucuronidation at position
CC 24) {ECO:0000269|PubMed:23756265};
CC KM=150.4 uM for hyodeoxycholate (when assaying glucuronidation at
CC position 6) {ECO:0000269|PubMed:23756265};
CC KM=226.1 uM for hyodeoxycholate (when assaying glucuronidation at
CC position 24) {ECO:0000269|PubMed:23756265};
CC KM=222.4 uM for hyocholate (when assaying glucuronidation at position
CC 6) {ECO:0000269|PubMed:23756265};
CC KM=465.8 uM for hyocholate (when assaying glucuronidation at position
CC 24) {ECO:0000269|PubMed:23756265};
CC Vmax=29.7 pmol/min/mg enzyme for the formation of 17alpha-estradiol
CC 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=4 pmol/min/mg enzyme for the formation of 17beta-estradiol 3-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=1.8 pmol/min/mg enzyme for the formation of 17alpha-estradiol
CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=1.4 pmol/min/mg enzyme for the formation of 16alpha,17alpha-
CC estriol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=70 pmol/min/mg enzyme for the formation of 17alpha-estradiol 3-
CC O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240};
CC Vmax=62.8 pmol/min/mg enzyme for the formation of 17beta-estradiol 3-
CC O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240};
CC Vmax=69 pmol/min/mg enzyme with 4-nitrophenol as substrate
CC {ECO:0000269|PubMed:19858781};
CC Vmax=39 pmol/min/mg enzyme with 4-methyl-umbelliferone as substrate
CC {ECO:0000269|PubMed:19858781};
CC Vmax=124 pmol/min/mg enzyme with 4-phenylphenol as substrate
CC {ECO:0000269|PubMed:19858781};
CC Vmax=2621.7 pmol/min/mg enzyme for the formation of choloyl-24-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=805 pmol/min/mg enzyme for the formation of chenodeoxycholoyl-
CC 24-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=61.7 pmol/min/mg enzyme for the formation of lithocholoyl-3-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=265.1 pmol/min/mg enzyme for the formation of lithocholoyl-24-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=8.3 pmol/min/mg enzyme for the formation of deoxycholoyl-3-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=196.7 pmol/min/mg enzyme for the formation of deoxycholoyl-24-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=1373.3 pmol/min/mg enzyme for the formation of hyodeoxycholate
CC 6-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=28.3 pmol/min/mg enzyme for the formation of hyocholoyl-24-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=65.1 pmol/min/mg enzyme for the formation of hyocholate 6-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC Vmax=911.7 pmol/min/mg enzyme for the formation of hyocholoyl-24-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:23756265};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:19858781}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DTE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DTE5-2; Sequence=VSP_060686;
CC -!- TISSUE SPECIFICITY: Mainly expressed in the nasal mucosa.
CC {ECO:0000269|PubMed:19858781}.
CC -!- MISCELLANEOUS: UGT2A2 isoform is part of the UGT2A complex locus which
CC displays alternative use of promoters and exons. The locus is defined
CC by 2 alternative promoters resulting in 2 fonctionally active
CC polypeptides UGT2A1 and UGT2A2. Alternative splicing of exons results
CC in additional isoforms for each protein class.
CC {ECO:0000303|PubMed:19858781}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; FJ664272; ACV70034.1; -; mRNA.
DR EMBL; FJ664273; ACV70035.1; -; mRNA.
DR EMBL; AC093829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS56331.1; -. [P0DTE5-1]
DR CCDS; CCDS77924.1; -. [P0DTE5-2]
DR RefSeq; NP_001099147.2; NM_001105677.2. [P0DTE5-1]
DR RefSeq; NP_001288162.1; NM_001301233.1. [P0DTE5-2]
DR AlphaFoldDB; P0DTE5; -.
DR SMR; P0DTE5; -.
DR IntAct; P0DTE5; 1.
DR ChEMBL; CHEMBL4523985; -.
DR SwissLipids; SLP:000001984; -.
DR GlyGen; P0DTE5; 3 sites.
DR PhosphoSitePlus; P0DTE5; -.
DR MassIVE; P0DTE5; -.
DR PeptideAtlas; P0DTE5; -.
DR Antibodypedia; 72053; 7 antibodies from 4 providers.
DR DNASU; 574537; -.
DR Ensembl; ENST00000604021.1; ENSP00000474383.2; ENSG00000271271.6. [P0DTE5-2]
DR Ensembl; ENST00000604629.6; ENSP00000475028.2; ENSG00000271271.6. [P0DTE5-1]
DR GeneID; 574537; -.
DR KEGG; hsa:574537; -.
DR MANE-Select; ENST00000604629.6; ENSP00000475028.2; NM_001105677.2; NP_001099147.2.
DR CTD; 574537; -.
DR GeneCards; UGT2A2; -.
DR HGNC; HGNC:28183; UGT2A2.
DR HPA; ENSG00000271271; Group enriched (kidney, liver).
DR MIM; 619809; gene.
DR neXtProt; NX_P0DTE5; -.
DR GeneTree; ENSGT00940000161344; -.
DR OMA; VLIMPSS; -.
DR Reactome; R-HSA-156588; Glucuronidation.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR PRO; PR:P0DTE5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR Bgee; ENSG00000271271; Expressed in olfactory segment of nasal mucosa and 12 other tissues.
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:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008206; P:bile acid metabolic process; IDA:UniProtKB.
DR GO; GO:0052695; P:cellular glucuronidation; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..536
FT /note="UDP-glucuronosyltransferase 2A2"
FT /id="PRO_0000450721"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..500
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 298..341
FT /note="Missing (in isoform 2)"
FT /id="VSP_060686"
SQ SEQUENCE 536 AA; 60772 MW; 2234435E46224749 CRC64;
MVSIRDFTMP KKFVQMLVFN LTLTEVVLSG NVLIWPTDGS HWLNIKIILE ELIQRNHNVT
VLASSATLFI NSNPDSPVNF EVIPVSYKKS NIDSLIEHMI MLWIDHRPTP LTIWAFYKEL
GKLLDTFFQI NIQLCDGVLK NPKLMARLQK GGFDVLVADP VTICGDLVAL KLGIPFMYTL
RFSPASTVER HCGKIPAPVS YVPAALSELT DQMTFGERIK NTISYSLQDY IFQSYWGEWN
SYYSKILGRP TTLCETMGKA EIWLIRTYWD FEFPRPYLPN FEFVGGLHCK PAKPLPKEME
EFIQSSGKNG VVVFSLGSMV KNLTEEKANL IASALAQIPQ KVLWRYKGKK PATLGNNTQL
FDWIPQNDLL GHPKTKAFIT HGGTNGIYEA IYHGVPMVGV PMFADQPDNI AHMKAKGAAV
EVNLNTMTSV DLLSALRTVI NEPSYKENAM RLSRIHHDQP VKPLDRAVFW IEFVMRHKGA
KHLRVAAHDL TWFQYHSLDV IGFLLVCVTT AIFLVIQCCL FSCQKFGKIG KKKKRE
