STEA3_MOUSE
ID STEA3_MOUSE Reviewed; 488 AA.
AC Q8CI59; Q3TKE4; Q80ZF3; Q8C5F0; Q924Z1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Metalloreductase STEAP3;
DE EC=1.16.1.-;
DE AltName: Full=Dudulin-2;
DE AltName: Full=Protein nm1054;
DE AltName: Full=Six-transmembrane epithelial antigen of prostate 3;
DE AltName: Full=Tumor suppressor-activated pathway protein 6;
GN Name=Steap3; Synonyms=Tsap6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=12606722; DOI=10.1073/pnas.0530298100;
RA Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C.,
RA Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L.,
RA Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R.,
RA Telerman A.;
RT "The p53-inducible TSAP6 gene product regulates apoptosis and the cell
RT cycle and interacts with Nix and the Myt1 kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Serru V., Lamblin D., Lenoir C., Manivet P., Vaubourdolle M.,
RA Kellermann O., Loric S.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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, ENZYME ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP HEME-BINDING, COFACTOR, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-316 AND
RP HIS-409.
RX PubMed=16227996; DOI=10.1038/ng1658;
RA Ohgami R.S., Campagna D.R., Greer E.L., Antiochos B., McDonald A., Chen J.,
RA Sharp J.J., Fujiwara Y., Barker J.E., Fleming M.D.;
RT "Identification of a ferrireductase required for efficient transferrin-
RT dependent iron uptake in erythroid cells.";
RL Nat. Genet. 37:1264-1269(2005).
RN [6]
RP FUNCTION.
RX PubMed=16609065; DOI=10.1182/blood-2006-02-003681;
RA Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.;
RT "The Steap proteins are metalloreductases.";
RL Blood 108:1388-1394(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-20, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-20, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Endosomal ferrireductase required for efficient transferrin-
CC dependent iron uptake in erythroid cells. Participates in erythroid
CC iron homeostasis by reducing Fe(3+) to Fe(2+). Also mediates reduction
CC of Cu(2+) to Cu(1+), suggesting that it participates in copper
CC homeostasis. Uses NADP(+) as acceptor. May play a role downstream of
CC p53/TP53 to interface apoptosis and cell cycle progression. Indirectly
CC involved in exosome secretion by facilitating the secretion of proteins
CC such as TCTP. {ECO:0000269|PubMed:16227996,
CC ECO:0000269|PubMed:16609065}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- SUBUNIT: Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and TCTP
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:16227996};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16227996}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CI59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CI59-2; Sequence=VSP_024832;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal liver (the site of
CC midgestational hematopoiesis). {ECO:0000269|PubMed:12606722,
CC ECO:0000269|PubMed:16227996}.
CC -!- PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced
CC cleavage occurs at multiple sites in a glycosylation-independent manner
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice display iron deficiency anemia, due to a
CC defect in iron release through the transferrin cycle.
CC {ECO:0000269|PubMed:16227996}.
CC -!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK50539.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY214462; AAO38239.1; -; mRNA.
DR EMBL; AY029586; AAK50539.1; ALT_FRAME; mRNA.
DR EMBL; AK078769; BAC37383.1; -; mRNA.
DR EMBL; AK167028; BAE39201.1; -; mRNA.
DR EMBL; AK171237; BAE42333.1; -; mRNA.
DR EMBL; BC037435; AAH37435.1; -; mRNA.
DR CCDS; CCDS48343.1; -. [Q8CI59-1]
DR RefSeq; NP_001078878.1; NM_001085409.1.
DR RefSeq; NP_573449.2; NM_133186.3.
DR AlphaFoldDB; Q8CI59; -.
DR SMR; Q8CI59; -.
DR BioGRID; 212849; 3.
DR IntAct; Q8CI59; 4.
DR STRING; 10090.ENSMUSP00000108260; -.
DR GlyGen; Q8CI59; 1 site.
DR iPTMnet; Q8CI59; -.
DR PhosphoSitePlus; Q8CI59; -.
DR SwissPalm; Q8CI59; -.
DR jPOST; Q8CI59; -.
DR MaxQB; Q8CI59; -.
DR PaxDb; Q8CI59; -.
DR PeptideAtlas; Q8CI59; -.
DR PRIDE; Q8CI59; -.
DR ProteomicsDB; 257489; -. [Q8CI59-1]
DR ProteomicsDB; 257490; -. [Q8CI59-2]
DR GeneID; 68428; -.
DR KEGG; mmu:68428; -.
DR CTD; 55240; -.
DR MGI; MGI:1915678; Steap3.
DR eggNOG; ENOG502QRP3; Eukaryota.
DR InParanoid; Q8CI59; -.
DR PhylomeDB; Q8CI59; -.
DR TreeFam; TF332031; -.
DR Reactome; R-MMU-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR BioGRID-ORCS; 68428; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Steap3; mouse.
DR PRO; PR:Q8CI59; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CI59; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0008823; F:cupric reductase activity; IDA:MGI.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:MGI.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0015677; P:copper ion import; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:1990182; P:exosomal secretion; IMP:MGI.
DR GO; GO:0033212; P:iron import into cell; IDA:MGI.
DR GO; GO:0098706; P:iron ion import across cell outer membrane; IDA:MGI.
DR GO; GO:0006826; P:iron ion transport; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1902167; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell cycle; Copper; Endosome; FAD;
KW Flavoprotein; Glycoprotein; Heme; Ion transport; Iron; Iron transport;
KW Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..488
FT /note="Metalloreductase STEAP3"
FT /id="PRO_0000285172"
FT TOPO_DOM 1..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..258
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..358
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..433
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 259..407
FT /note="Ferric oxidoreductase"
FT BINDING 36..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 58..59
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 91..98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 116
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 281
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 316
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:Q687X5"
FT BINDING 378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 395
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 409
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:Q687X5"
FT SITE 325..326
FT /note="Cleavage; by RHBDL4/RHBDD1"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MAAEAHRQQGSCPTIPSEGCGKSPEKKGSAADSRPGTAM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12606722"
FT /id="VSP_024832"
FT MUTAGEN 316
FT /note="H->L: Loss of function."
FT /evidence="ECO:0000269|PubMed:16227996"
FT MUTAGEN 409
FT /note="H->L: Loss of function."
FT /evidence="ECO:0000269|PubMed:16227996"
FT CONFLICT 81
FT /note="V -> M (in Ref. 3; BAC37383)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="G -> V (in Ref. 2; AAK50539)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..172
FT /note="SDQP -> GNQQ (in Ref. 2; AAK50539)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..179
FT /note="RTIS -> QRVM (in Ref. 2; AAK50539)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="W -> G (in Ref. 2; AAK50539)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="V -> A (in Ref. 3; BAC37383/BAE39201)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="S -> N (in Ref. 3; BAC37383/BAE39201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 54749 MW; 9A08D99C90CF83F4 CRC64;
MSGEMDKPLI SRRLVDSDGS LAEVPKEAPK VGILGSGDFA RSLATRLVGS GFSVVVGSRN
PKRTAGLFPS LAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLADQLAGKI LVDVSNPTEK
EHLQHRQSNA EYLASLFPAC TVVKAFNVIS AWALQAGPRD GNRQVLICSD QPEAKRTISE
MARAMGFTPL DMGSLASARE VEAIPLRLLP SWKVPTLLAL GLFVCFYTYN FIRDVLQPYI
RKDENKFYKM PLSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ
HRKQIGLLSF FFAMLHALYS FCLPLRRSHR YDLVNLAVKQ VLANKSRLWV EEEVWRMEIY
LSLGVLALGM LSLLAVTSLP SIANSLNWKE FSFVQSTLGF VALILSTMHT LTYGWTRAFE
ENHYKFYLPP TFTLTLLLPC VIILAKGLFL LPCLSRRLTK IRRGWEKDGA VKFMLPGDHT
QGEKTSHV
