CP2S1_HUMAN
ID CP2S1_HUMAN Reviewed; 504 AA.
AC Q96SQ9; Q9BZ66;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cytochrome P450 2S1 {ECO:0000303|PubMed:11181079};
DE EC=1.14.14.- {ECO:0000269|PubMed:12711469};
DE AltName: Full=CYPIIS1;
DE AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE EC=4.2.1.152 {ECO:0000269|PubMed:21068195};
DE AltName: Full=Thromboxane-A synthase;
DE EC=5.3.99.5 {ECO:0000269|PubMed:21068195};
GN Name=CYP2S1 {ECO:0000303|PubMed:11181079, ECO:0000312|HGNC:HGNC:15654};
GN ORFNames=UNQ891/PRO1906;
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11181079; DOI=10.1006/bbrc.2001.4390;
RA Rylander T., Neve E., Ingelman-Sundberg M., Oscarson M.;
RT "Identification and tissue distribution of the novel human cytochrome P450
RT 2S1 (CYP2S1).";
RL Biochem. Biophys. Res. Commun. 281:529-535(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
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]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION BY
RP ULTRAVIOLET RADIATION.
RX PubMed=12711469; DOI=10.1016/s0140-6736(03)13081-4;
RA Smith G., Wolf C.R., Deeni Y.Y., Dawe R.S., Evans A.T., Comrie M.M.,
RA Ferguson J., Ibbotson S.H.;
RT "Cutaneous expression of cytochrome P450 CYP2S1: individuality in
RT regulation by therapeutic agents for psoriasis and other skin diseases.";
RL Lancet 361:1336-1343(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=21068195; DOI=10.1124/dmd.110.035121;
RA Bui P., Imaizumi S., Beedanagari S.R., Reddy S.T., Hankinson O.;
RT "Human CYP2S1 metabolizes cyclooxygenase- and lipoxygenase-derived
RT eicosanoids.";
RL Drug Metab. Dispos. 39:180-190(2011).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC retinoids and eicosanoids (PubMed:12711469, PubMed:21068195). In
CC epidermis, may contribute to the oxidative metabolism of all-trans-
CC retinoic acid. For this activity, 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 (NADPH--hemoprotein reductase) (PubMed:12711469).
CC Additionally, displays peroxidase and isomerase activities toward
CC various oxygenated eicosanoids such as prostaglandin H2 (PGH2) and
CC hydroperoxyeicosatetraenoates (HPETEs) (PubMed:21068195). Independently
CC of cytochrome P450 reductase, NADPH, and O2, catalyzes the breakdown of
CC PGH2 to hydroxyheptadecatrienoic acid (HHT) and malondialdehyde (MDA),
CC which is known to act as a mediator of DNA damage (PubMed:21068195).
CC {ECO:0000269|PubMed:12711469, ECO:0000269|PubMed:21068195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-5,6-epoxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55860, 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:139183;
CC Evidence={ECO:0000269|PubMed:12711469};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55861;
CC Evidence={ECO:0000305|PubMed:12711469};
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:12711469};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC Evidence={ECO:0000305|PubMed:12711469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-
CC (6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342;
CC Evidence={ECO:0000269|PubMed:21068195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633;
CC Evidence={ECO:0000305|PubMed:21068195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-
CC (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231;
CC EC=4.2.1.152; Evidence={ECO:0000269|PubMed:21068195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
CC Evidence={ECO:0000305|PubMed:21068195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-
CC (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446;
CC Evidence={ECO:0000269|PubMed:21068195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC Evidence={ECO:0000305|PubMed:21068195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = thromboxane A2; Xref=Rhea:RHEA:17137,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57445; EC=5.3.99.5;
CC Evidence={ECO:0000269|PubMed:21068195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17138;
CC Evidence={ECO:0000305|PubMed:21068195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)-
CC heptadecatrienoate + malonaldehyde; Xref=Rhea:RHEA:48644,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:90694, ChEBI:CHEBI:566274;
CC Evidence={ECO:0000269|PubMed:21068195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48645;
CC Evidence={ECO:0000305|PubMed:21068195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-
CC octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57466, ChEBI:CHEBI:90781;
CC Evidence={ECO:0000269|PubMed:21068195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
CC Evidence={ECO:0000305|PubMed:21068195};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:21068195}.
CC -!- INTERACTION:
CC Q96SQ9; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-8633740, EBI-10173507;
CC Q96SQ9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-8633740, EBI-10171774;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11181079}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11181079}. Microsome membrane
CC {ECO:0000269|PubMed:11181079}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11181079}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96SQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96SQ9-2; Sequence=VSP_010531;
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in extrahepatic tissues
CC including trachea, lung, stomach, small intestine, colon, kidney,
CC breast, placenta and spleen (PubMed:11181079, PubMed:12711469).
CC Expressed in peripheral blood leukocytes (PubMed:11181079).
CC Constitutively expressed in skin (at protein level) (PubMed:12711469).
CC {ECO:0000269|PubMed:11181079, ECO:0000269|PubMed:12711469}.
CC -!- INDUCTION: Up-regulated in skin upon exposure to ultraviolet radiation
CC or treatment with all-trans retinoic acid (substrate-inducible).
CC {ECO:0000269|PubMed:12711469}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF335278; AAK13498.1; -; mRNA.
DR EMBL; AY358603; AAQ88966.1; -; mRNA.
DR EMBL; AK027605; BAB55227.1; -; mRNA.
DR EMBL; BC033691; AAH33691.1; -; mRNA.
DR CCDS; CCDS12573.1; -. [Q96SQ9-1]
DR PIR; JC7613; JC7613.
DR RefSeq; NP_085125.1; NM_030622.7. [Q96SQ9-1]
DR AlphaFoldDB; Q96SQ9; -.
DR SMR; Q96SQ9; -.
DR BioGRID; 118915; 139.
DR IntAct; Q96SQ9; 39.
DR MINT; Q96SQ9; -.
DR STRING; 9606.ENSP00000308032; -.
DR BindingDB; Q96SQ9; -.
DR ChEMBL; CHEMBL4523986; -.
DR SwissLipids; SLP:000001465; -.
DR iPTMnet; Q96SQ9; -.
DR PhosphoSitePlus; Q96SQ9; -.
DR BioMuta; CYP2S1; -.
DR DMDM; 48428134; -.
DR EPD; Q96SQ9; -.
DR jPOST; Q96SQ9; -.
DR MassIVE; Q96SQ9; -.
DR MaxQB; Q96SQ9; -.
DR PaxDb; Q96SQ9; -.
DR PeptideAtlas; Q96SQ9; -.
DR PRIDE; Q96SQ9; -.
DR ProteomicsDB; 78138; -. [Q96SQ9-1]
DR ProteomicsDB; 78139; -. [Q96SQ9-2]
DR Antibodypedia; 45241; 218 antibodies from 29 providers.
DR DNASU; 29785; -.
DR Ensembl; ENST00000310054.9; ENSP00000308032.3; ENSG00000167600.14. [Q96SQ9-1]
DR GeneID; 29785; -.
DR KEGG; hsa:29785; -.
DR MANE-Select; ENST00000310054.9; ENSP00000308032.3; NM_030622.8; NP_085125.1.
DR UCSC; uc002opw.4; human. [Q96SQ9-1]
DR CTD; 29785; -.
DR DisGeNET; 29785; -.
DR GeneCards; CYP2S1; -.
DR HGNC; HGNC:15654; CYP2S1.
DR HPA; ENSG00000167600; Group enriched (intestine, stomach).
DR MIM; 611529; gene.
DR neXtProt; NX_Q96SQ9; -.
DR OpenTargets; ENSG00000167600; -.
DR PharmGKB; PA27113; -.
DR VEuPathDB; HostDB:ENSG00000167600; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000162131; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; Q96SQ9; -.
DR OMA; YEMFSRL; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q96SQ9; -.
DR TreeFam; TF352043; -.
DR PathwayCommons; Q96SQ9; -.
DR Reactome; R-HSA-211958; Miscellaneous substrates.
DR Reactome; R-HSA-211981; Xenobiotics.
DR Reactome; R-HSA-211999; CYP2E1 reactions.
DR SignaLink; Q96SQ9; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 29785; 18 hits in 1074 CRISPR screens.
DR ChiTaRS; CYP2S1; human.
DR GeneWiki; CYP2S1; -.
DR GenomeRNAi; 29785; -.
DR Pharos; Q96SQ9; Tbio.
DR PRO; PR:Q96SQ9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96SQ9; protein.
DR Bgee; ENSG00000167600; Expressed in ileal mucosa and 119 other tissues.
DR ExpressionAtlas; Q96SQ9; baseline and differential.
DR Genevisible; Q96SQ9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
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:0036134; F:12-hydroxyheptadecatrienoic acid synthase activity; IEA:RHEA.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
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; TAS:Reactome.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0004796; F:thromboxane-A synthase activity; IDA:UniProtKB.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0006690; P:icosanoid metabolic process; IDA:UniProtKB.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01684; EP450ICYP2A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Fatty acid metabolism; Heme;
KW Iron; Isomerase; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Microsome; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..504
FT /note="Cytochrome P450 2S1"
FT /id="PRO_0000051780"
FT BINDING 440
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"
FT VAR_SEQ 488..504
FT /note="FQLQVRPTDLHSTTQTR -> STVGMDRVNVSRVYTAGSHIYTPAVVFRSLS
FT HGPHAHLTHAAKMHNRTPIHNYKGHKATAGLAFHRHKYSPSAITST (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010531"
FT VARIANT 466
FT /note="P -> L (in dbSNP:rs34971233)"
FT /id="VAR_033820"
SQ SEQUENCE 504 AA; 55817 MW; 853513370F65E25A CRC64;
MEATGTWALL LALALLLLLT LALSGTRARG HLPPGPTPLP LLGNLLQLRP GALYSGLMRL
SKKYGPVFTI YLGPWRPVVV LVGQEAVREA LGGQAEEFSG RGTVAMLEGT FDGHGVFFSN
GERWRQLRKF TMLALRDLGM GKREGEELIQ AEARCLVETF QGTEGRPFDP SLLLAQATSN
VVCSLLFGLR FSYEDKEFQA VVRAAGGTLL GVSSQGGQTY EMFSWFLRPL PGPHKQLLHH
VSTLAAFTVR QVQQHQGNLD ASGPARDLVD AFLLKMAQEE QNPGTEFTNK NMLMTVIYLL
FAGTMTVSTT VGYTLLLLMK YPHVQKWVRE ELNRELGAGQ APSLGDRTRL PYTDAVLHEA
QRLLALVPMG IPRTLMRTTR FRGYTLPQGT EVFPLLGSIL HDPNIFKHPE EFNPDRFLDA
DGRFRKHEAF LPFSLGKRVC LGEGLAKAEL FLFFTTILQA FSLESPCPPD TLSLKPTVSG
LFNIPPAFQL QVRPTDLHST TQTR
