CP2W1_HUMAN
ID CP2W1_HUMAN Reviewed; 490 AA.
AC Q8TAV3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytochrome P450 2W1 {ECO:0000303|PubMed:22591743};
DE EC=1.14.14.- {ECO:0000269|PubMed:22591743, ECO:0000269|PubMed:26936974};
DE AltName: Full=CYPIIW1;
DE Flags: Precursor;
GN Name=CYP2W1 {ECO:0000303|PubMed:26936974, ECO:0000312|HGNC:HGNC:20243};
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 [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=16426568; DOI=10.1016/j.bbrc.2005.12.200;
RA Karlgren M., Gomez A., Stark K., Svard J., Rodriguez-Antona C., Oliw E.,
RA Bernal M.L., Ramon y Cajal S., Johansson I., Ingelman-Sundberg M.;
RT "Tumor-specific expression of the novel cytochrome P450 enzyme, CYP2W1.";
RL Biochem. Biophys. Res. Commun. 341:451-458(2006).
RN [4]
RP FUNCTION.
RX PubMed=16551781; DOI=10.1124/mol.106.023648;
RA Wu Z.L., Sohl C.D., Shimada T., Guengerich F.P.;
RT "Recombinant enzymes overexpressed in bacteria show broad catalytic
RT specificity of human cytochrome P450 2W1 and limited activity of human
RT cytochrome P450 2S1.";
RL Mol. Pharmacol. 69:2007-2014(2006).
RN [5]
RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-177, MUTAGENESIS OF ASN-177,
RP FUNCTION, AND IDENTIFICATION OF SUBSTRATE.
RX PubMed=20805301; DOI=10.1124/mol.110.067652;
RA Gomez A., Nekvindova J., Travica S., Lee M.Y., Johansson I., Edler D.,
RA Mkrtchian S., Ingelman-Sundberg M.;
RT "Colorectal cancer-specific cytochrome P450 2W1: intracellular
RT localization, glycosylation, and catalytic activity.";
RL Mol. Pharmacol. 78:1004-1011(2010).
RN [6]
RP FUNCTION, AND IDENTIFICATION OF SUBSTRATE.
RX PubMed=24278521; DOI=10.5487/tr.2010.26.3.171;
RA Eun C.Y., Han S., Lim Y.R., Park H.G., Han J.S., Cho K.S., Chun Y.J.,
RA Kim D.;
RT "Bioactivation of aromatic amines by human CYP2W1, an orphan cytochrome
RT P450 enzyme.";
RL Toxicol. Res. 26:171-175(2010).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22591743; DOI=10.1194/jlr.m027185;
RA Xiao Y., Guengerich F.P.;
RT "Metabolomic analysis and identification of a role for the orphan human
RT cytochrome P450 2W1 in selective oxidation of lysophospholipids.";
RL J. Lipid Res. 53:1610-1617(2012).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26936974; DOI=10.1124/dmd.116.069633;
RA Zhao Y., Wan D., Yang J., Hammock B.D., Ortiz de Montellano P.R.;
RT "Catalytic Activities of Tumor-Specific Human Cytochrome P450 CYP2W1 Toward
RT Endogenous Substrates.";
RL Drug Metab. Dispos. 44:771-780(2016).
RN [9]
RP VARIANTS ALA-58; THR-181; ILE-432; HIS-482 AND LEU-488.
RX PubMed=20602611; DOI=10.2217/pgs.10.66;
RA Gervasini G., de Murillo S.G., Ladero J.M., Agundez J.A.;
RT "CYP2W1 variant alleles in Caucasians and association of the CYP2W1 G541A
RT (Ala181Thr) polymorphism with increased colorectal cancer risk.";
RL Pharmacogenomics 11:919-925(2010).
CC -!- FUNCTION: A cytochrome P450 monooxygenase that may play a role in
CC retinoid and phospholipid metabolism (PubMed:22591743,
CC PubMed:26936974). Catalyzes the hydroxylation of saturated carbon
CC hydrogen bonds. Hydroxylates all trans-retinoic acid (atRA) to 4-
CC hydroxyretinoate and may regulate atRA clearance. Other retinoids such
CC as all-trans retinol and all-trans retinal are potential endogenous
CC substrates (PubMed:26936974). Catalyzes both epoxidation of double
CC bonds and hydroxylation of carbon hydrogen bonds of the fatty acyl
CC chain of 1-acylphospholipids/2-lysophospholipids. Can metabolize
CC various lysophospholipids classes including lysophosphatidylcholines
CC (LPCs), lysophosphatidylinositols (LPIs), lysophosphatidylserines
CC (LPSs), lysophosphatidylglycerols (LPGs), lysophosphatidylethanolamines
CC (LPEs) and lysophosphatidic acids (LPAs) (PubMed:22591743). Has low or
CC no activity toward 2-acylphospholipids/1-lysophospholipids,
CC diacylphospholipids and free fatty acids (PubMed:26936974,
CC PubMed:22591743). May play a role in tumorigenesis by activating
CC procarcinogens such as aflatoxin B1, polycyclic aromatic hydrocarbon
CC dihydrodiols and aromatic amines (PubMed:20805301, PubMed:16551781,
CC PubMed:24278521). Mechanistically, uses molecular oxygen inserting one
CC oxygen atom into a substrate, and reducing the second into a water
CC molecule, with two electrons provided by NADPH via cytochrome P450
CC reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:22591743,
CC PubMed:26936974). {ECO:0000269|PubMed:16551781,
CC ECO:0000269|PubMed:20805301, ECO:0000269|PubMed:22591743,
CC ECO:0000269|PubMed:24278521, ECO:0000269|PubMed:26936974}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178;
CC Evidence={ECO:0000269|PubMed:26936974};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC Evidence={ECO:0000305|PubMed:26936974};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + O2 + reduced
CC [NADPH--hemoprotein reductase] = 1-[8-hydroxy-(9Z)-octadecenoyl]-sn-
CC glycero-3-phosphocholine + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:50328, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:132285; Evidence={ECO:0000269|PubMed:22591743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50329;
CC Evidence={ECO:0000305|PubMed:22591743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + O2 + reduced
CC [NADPH--hemoprotein reductase] = 1-[11-hydroxy-(9Z)-octadecenoyl]-sn-
CC glycero-3-phosphocholine + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:50332, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:132286; Evidence={ECO:0000269|PubMed:22591743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50333;
CC Evidence={ECO:0000305|PubMed:22591743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + O2 + reduced
CC [NADPH--hemoprotein reductase] = 1-[(9S,10R)-epoxy-octadecanoyl]-sn-
CC glycero-3-phosphocholine + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:50324, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:132278; Evidence={ECO:0000269|PubMed:22591743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50325;
CC Evidence={ECO:0000305|PubMed:22591743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + O2 + reduced
CC [NADPH--hemoprotein reductase] = 1-[(9R,10S)-epoxy-octadecanoyl]-sn-
CC glycero-3-phosphocholine + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:50320, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:132280; Evidence={ECO:0000269|PubMed:22591743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50321;
CC Evidence={ECO:0000305|PubMed:22591743};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q6VVX0};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.6 uM for all-trans-retinoate {ECO:0000269|PubMed:26936974};
CC KM=38 uM for 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine (18:1
CC LPC) (hydroxylation) {ECO:0000269|PubMed:22591743};
CC KM=34 uM for 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine (18:1
CC LPC) (epoxidation) {ECO:0000269|PubMed:22591743};
CC KM=14 uM for 16:0 LPC (hydroxylation) {ECO:0000269|PubMed:22591743};
CC KM=83 uM for hexadecanoate (16:0) (hydroxylation)
CC {ECO:0000269|PubMed:22591743};
CC KM=101 uM for (9Z)-octadecenoate (18:1) (hydroxylation)
CC {ECO:0000269|PubMed:22591743};
CC KM=95 uM for (9Z)-octadecenoate (18:1) (epoxidation)
CC {ECO:0000269|PubMed:22591743};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:20805301}. Cell membrane
CC {ECO:0000269|PubMed:20805301}. Microsome membrane
CC {ECO:0000269|PubMed:20805301}. Note=About 8% are expressed on the cell
CC surface. {ECO:0000269|PubMed:20805301}.
CC -!- TISSUE SPECIFICITY: Very low levels are detected in fetal and adult
CC tissues. Highly expressed in several tumor samples, in particular colon
CC and adrenal tumors. {ECO:0000269|PubMed:16426568}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CYP2W1ID44337ch7p22.html";
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DR EMBL; AC073957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025761; AAH25761.2; -; mRNA.
DR CCDS; CCDS5319.2; -.
DR RefSeq; NP_060251.2; NM_017781.2.
DR AlphaFoldDB; Q8TAV3; -.
DR SMR; Q8TAV3; -.
DR BioGRID; 120251; 14.
DR IntAct; Q8TAV3; 3.
DR STRING; 9606.ENSP00000310149; -.
DR BindingDB; Q8TAV3; -.
DR ChEMBL; CHEMBL2406897; -.
DR SwissLipids; SLP:000001619; -.
DR GlyGen; Q8TAV3; 1 site.
DR iPTMnet; Q8TAV3; -.
DR PhosphoSitePlus; Q8TAV3; -.
DR BioMuta; CYP2W1; -.
DR DMDM; 114152790; -.
DR jPOST; Q8TAV3; -.
DR MassIVE; Q8TAV3; -.
DR MaxQB; Q8TAV3; -.
DR PaxDb; Q8TAV3; -.
DR PeptideAtlas; Q8TAV3; -.
DR PRIDE; Q8TAV3; -.
DR ProteomicsDB; 73927; -.
DR Antibodypedia; 1974; 222 antibodies from 29 providers.
DR DNASU; 54905; -.
DR Ensembl; ENST00000308919.12; ENSP00000310149.7; ENSG00000073067.14.
DR GeneID; 54905; -.
DR KEGG; hsa:54905; -.
DR MANE-Select; ENST00000308919.12; ENSP00000310149.7; NM_017781.3; NP_060251.2.
DR UCSC; uc003sjq.1; human.
DR CTD; 54905; -.
DR DisGeNET; 54905; -.
DR GeneCards; CYP2W1; -.
DR HGNC; HGNC:20243; CYP2W1.
DR HPA; ENSG00000073067; Group enriched (adrenal gland, intestine, skin).
DR MIM; 615967; gene.
DR neXtProt; NX_Q8TAV3; -.
DR OpenTargets; ENSG00000073067; -.
DR PharmGKB; PA134992665; -.
DR VEuPathDB; HostDB:ENSG00000073067; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000161956; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; Q8TAV3; -.
DR OMA; VPRCTAV; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q8TAV3; -.
DR TreeFam; TF352043; -.
DR PathwayCommons; Q8TAV3; -.
DR Reactome; R-HSA-211958; Miscellaneous substrates.
DR Reactome; R-HSA-211981; Xenobiotics.
DR SignaLink; Q8TAV3; -.
DR BioGRID-ORCS; 54905; 8 hits in 1063 CRISPR screens.
DR GeneWiki; CYP2W1; -.
DR GenomeRNAi; 54905; -.
DR Pharos; Q8TAV3; Tbio.
DR PRO; PR:Q8TAV3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8TAV3; protein.
DR Bgee; ENSG00000073067; Expressed in buccal mucosa cell and 120 other tissues.
DR ExpressionAtlas; Q8TAV3; baseline and differential.
DR Genevisible; Q8TAV3; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005503; F:all-trans retinal binding; IDA:UniProtKB.
DR GO; GO:1904768; F:all-trans-retinol binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0001972; F:retinoic acid binding; IDA:UniProtKB.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0046222; P:aflatoxin metabolic process; IDA:UniProtKB.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:0034653; P:retinoic acid catabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Glycoprotein; Heme; Iron;
KW Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..490
FT /note="Cytochrome P450 2W1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000051782"
FT BINDING 433
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q6VVX0"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20805301"
FT VARIANT 58
FT /note="E -> A (in dbSNP:rs1316523256)"
FT /evidence="ECO:0000269|PubMed:20602611"
FT /id="VAR_071912"
FT VARIANT 181
FT /note="A -> T (associated with increased colorectal cancer
FT risk; dbSNP:rs3735684)"
FT /evidence="ECO:0000269|PubMed:20602611"
FT /id="VAR_027413"
FT VARIANT 432
FT /note="V -> I (in dbSNP:rs78873069)"
FT /evidence="ECO:0000269|PubMed:20602611"
FT /id="VAR_071913"
FT VARIANT 482
FT /note="Q -> H (in dbSNP:rs773499447)"
FT /evidence="ECO:0000269|PubMed:20602611"
FT /id="VAR_071914"
FT VARIANT 488
FT /note="P -> L (in dbSNP:rs3808348)"
FT /evidence="ECO:0000269|PubMed:20602611"
FT /id="VAR_071915"
FT MUTAGEN 177
FT /note="N->A: Loss of glycosylation."
FT /evidence="ECO:0000269|PubMed:20805301"
SQ SEQUENCE 490 AA; 53844 MW; BB84B2F1FEFEF5BC CRC64;
MALLLLLFLG LLGLWGLLCA CAQDPSPAAR WPPGPRPLPL VGNLHLLRLS QQDRSLMELS
ERYGPVFTVH LGRQKTVVLT GFEAVKEALA GPGQELADRP PIAIFQLIQR GGGIFFSSGA
RWRAARQFTV RALHSLGVGR EPVADKILQE LKCLSGQLDG YRGRPFPLAL LGWAPSNITF
ALLFGRRFDY RDPVFVSLLG LIDEVMVLLG SPGLQLFNVY PWLGALLQLH RPVLRKIEEV
RAILRTLLEA RRPHVCPGDP VCSYVDALIQ QGQGDDPEGL FAEANAVACT LDMVMAGTET
TSATLQWAAL LMGRHPDVQG RVQEELDRVL GPGRTPRLED QQALPYTSAV LHEVQRFITL
LPHVPRCTAA DTQLGGFLLP KGTPVIPLLT SVLLDETQWQ TPGQFNPGHF LDANGHFVKR
EAFLPFSAGR RVCVGERLAR TELFLLFAGL LQRYRLLPPP GVSPASLDTT PARAFTMRPR
AQALCAVPRP
