STEA4_MOUSE
ID STEA4_MOUSE Reviewed; 470 AA.
AC Q923B6; Q91W31; Q91ZE8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Metalloreductase STEAP4;
DE EC=1.16.1.9 {ECO:0000250|UniProtKB:Q687X5};
DE AltName: Full=Dudulin-4;
DE AltName: Full=Six-transmembrane epithelial antigen of prostate 4;
DE AltName: Full=Tumor necrosis factor-alpha-induced adipose-related protein;
GN Name=Steap4; Synonyms=Tiarp {ECO:0000303|PubMed:11443137};
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], SUBCELLULAR LOCATION, AND INDUCTION BY TNFA.
RC STRAIN=SWR/J; TISSUE=Adipose tissue;
RX PubMed=11443137; DOI=10.1074/jbc.m105726200;
RA Moldes M., Lasnier F., Gauthereau X., Klein C., Pairault J., Feve B.,
RA Chambaut-Guerin A.-M.;
RT "Tumor necrosis factor-alpha-induced adipose-related protein (TIARP), a
RT cell-surface protein that is highly induced by tumor necrosis factor-alpha
RT and adipose conversion.";
RL J. Biol. Chem. 276:33938-33946(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Serru V., Lamblin D., Manivet P., Pernet P., Vaubourdolle M.,
RA Kellermann O., Loric S.;
RT "Molecular cloning and expression of two new members of the dudulin
RT family.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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].
RC STRAIN=FVB/N; 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 INDUCTION BY IL6, AND TISSUE SPECIFICITY.
RX PubMed=14988015; DOI=10.1016/s0014-5793(04)00096-1;
RA Fasshauer M., Kralisch S., Klier M., Lossner U., Bluher M.,
RA Chambaut-Guerin A.-M., Klein J., Paschke R.;
RT "Interleukin-6 is a positive regulator of tumor necrosis factor alpha-
RT induced adipose-related protein in 3T3-L1 adipocytes.";
RL FEBS Lett. 560:153-157(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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 FUNCTION, INDUCTION BY TNFA, AND DISRUPTION PHENOTYPE.
RX PubMed=17482547; DOI=10.1016/j.cell.2007.02.049;
RA Wellen K.E., Fucho R., Gregor M.F., Furuhashi M., Morgan C., Lindstad T.,
RA Vaillancourt E., Gorgun C.Z., Saatcioglu F., Hotamisligil G.S.;
RT "Coordinated regulation of nutrient and inflammatory responses by STAMP2 is
RT essential for metabolic homeostasis.";
RL Cell 129:537-548(2007).
RN [8]
RP FUNCTION, INDUCTION BY TNFA, AND TISSUE SPECIFICITY.
RX PubMed=19660107; DOI=10.1186/ar2779;
RA Inoue A., Matsumoto I., Tanaka Y., Iwanami K., Kanamori A., Ochiai N.,
RA Goto D., Ito S., Sumida T.;
RT "Tumor necrosis factor alpha-induced adipose-related protein expression in
RT experimental arthritis and in rheumatoid arthritis.";
RL Arthritis Res. Ther. 11:R118-R118(2009).
RN [9]
RP INDUCTION BY IL1B.
RX PubMed=19289123; DOI=10.1016/j.febslet.2009.03.015;
RA Kralisch S., Sommer G., Weise S., Lipfert J., Lossner U., Kamprad M.,
RA Schrock K., Bluher M., Stumvoll M., Fasshauer M.;
RT "Interleukin-1beta is a positive regulator of TIARP/STAMP2 gene and protein
RT expression in adipocytes in vitro.";
RL FEBS Lett. 583:1196-1200(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Liver;
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: Integral membrane protein that functions as NADPH-dependent
CC ferric-chelate reductase, using NADPH from one side of the membrane to
CC reduce a Fe(3+) chelate that is bound on the other side of the membrane
CC (PubMed:16609065). Mediates sequential transmembrane electron transfer
CC from NADPH to FAD and onto heme, and finally to the Fe(3+) chelate (By
CC similarity). Can also reduce Cu(2+) to Cu(1+) (PubMed:16609065). Plays
CC a role in systemic metabolic homeostasis, integrating inflammatory and
CC metabolic responses (PubMed:17482547). Associated with obesity and
CC insulin-resistance (By similarity). Involved in inflammatory arthritis,
CC through the regulation of inflammatory cytokines (PubMed:19660107).
CC Inhibits anchorage-independent cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q687X5, ECO:0000269|PubMed:16609065,
CC ECO:0000269|PubMed:17482547, ECO:0000269|PubMed:19660107}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q4V8K1};
CC Note=Can also utilize the flavins FMN and riboflavin.
CC {ECO:0000250|UniProtKB:Q4V8K1};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- SUBUNIT: Homotrimer. Interacts with PTK2/FAK1; the interaction may
CC regulate PTK2 phosphorylation. {ECO:0000250|UniProtKB:Q687X5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11443137,
CC ECO:0000269|PubMed:16609065}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q687X5}. Golgi apparatus membrane
CC {ECO:0000305|PubMed:11443137}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q687X5}. Early endosome membrane
CC {ECO:0000269|PubMed:16609065}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q687X5}.
CC -!- TISSUE SPECIFICITY: Expressed in white and brown adipose tissues cells,
CC as well as in muscle and liver cells. Detected in joints and spleens of
CC arthritic mice. {ECO:0000269|PubMed:14988015,
CC ECO:0000269|PubMed:19660107}.
CC -!- INDUCTION: By Tnfa (TNF-alpha), by Il6 in white and brown adipose
CC tissue, and IL1B in white adipose tissue. Tnfa, Il6 and Il1b shows
CC sinergistic stimulatory effects. {ECO:0000269|PubMed:11443137,
CC ECO:0000269|PubMed:14988015, ECO:0000269|PubMed:17482547,
CC ECO:0000269|PubMed:19289123, ECO:0000269|PubMed:19660107}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but exhibit overt
CC inflammation with increased expression of Il6, Tnfa, Ccl2, haptoglobin
CC and Socs3 in visceral adipose tissue as well as macrophage
CC infiltration. They develop metabolic disease on regular diet with
CC insulin resistance, glucose intolerance, mild hyperglycemia,
CC dyslipidemia, and fatty liver disease. Adipocytes isolated from
CC visceral fat exhibit severily defective glucose transport, with
CC decreased expression of Slc2a4, Adipoq, Fas and Pparg. Glucose disposal
CC is lower in response to insulin stimulation and hepatic glucose
CC production is higher, confirming systemic and hepatic insulin-
CC resistance. {ECO:0000269|PubMed:17482547}.
CC -!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40270.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ319746; CAC41351.1; -; mRNA.
DR EMBL; AY029778; AAK40270.1; ALT_FRAME; mRNA.
DR EMBL; AK040760; BAC30696.1; -; mRNA.
DR EMBL; BC006651; AAH06651.1; -; mRNA.
DR CCDS; CCDS39008.1; -.
DR RefSeq; NP_473439.2; NM_054098.3.
DR AlphaFoldDB; Q923B6; -.
DR SMR; Q923B6; -.
DR STRING; 10090.ENSMUSP00000111081; -.
DR iPTMnet; Q923B6; -.
DR PhosphoSitePlus; Q923B6; -.
DR SwissPalm; Q923B6; -.
DR jPOST; Q923B6; -.
DR MaxQB; Q923B6; -.
DR PaxDb; Q923B6; -.
DR PRIDE; Q923B6; -.
DR ProteomicsDB; 254587; -.
DR Antibodypedia; 29814; 296 antibodies from 36 providers.
DR Ensembl; ENSMUST00000115421; ENSMUSP00000111081; ENSMUSG00000012428.
DR GeneID; 117167; -.
DR KEGG; mmu:117167; -.
DR UCSC; uc008wjg.1; mouse.
DR CTD; 79689; -.
DR MGI; MGI:1923560; Steap4.
DR VEuPathDB; HostDB:ENSMUSG00000012428; -.
DR eggNOG; ENOG502R746; Eukaryota.
DR GeneTree; ENSGT00390000008042; -.
DR HOGENOM; CLU_034618_1_1_1; -.
DR InParanoid; Q923B6; -.
DR OMA; GWERNPK; -.
DR OrthoDB; 638341at2759; -.
DR PhylomeDB; Q923B6; -.
DR TreeFam; TF332031; -.
DR BioGRID-ORCS; 117167; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Steap4; mouse.
DR PRO; PR:Q923B6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q923B6; protein.
DR Bgee; ENSMUSG00000012428; Expressed in epididymal fat pad and 128 other tissues.
DR Genevisible; Q923B6; MM.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008823; F:cupric reductase activity; IDA:MGI.
DR GO; GO:0009055; F:electron transfer activity; ISO:MGI.
DR GO; GO:0071949; F:FAD binding; ISO:MGI.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015677; P:copper ion import; IDA:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IEP:UniProtKB.
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:0070207; P:protein homotrimerization; ISO:MGI.
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 Cell membrane; Copper; Endosome; FAD; Flavoprotein; Golgi apparatus; Heme;
KW Ion transport; Iron; Iron transport; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..470
FT /note="Metalloreductase STEAP4"
FT /id="PRO_0000285175"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT DOMAIN 247..395
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000255"
FT BINDING 27..30
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q4V8K1"
FT BINDING 49..50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q4V8K1"
FT BINDING 67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q4V8K1"
FT BINDING 81..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q4V8K1"
FT BINDING 106
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q4V8K1"
FT BINDING 139
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q4V8K1"
FT BINDING 140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q4V8K1"
FT BINDING 269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 304
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:P32791"
FT BINDING 366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 397
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:P32791"
FT CONFLICT 36
FT /note="L -> M (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="Y -> C (in Ref. 1; CAC41351)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="R -> H (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="G -> E (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="F -> L (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Q -> H (in Ref. 1; CAC41351)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="V -> I (in Ref. 1; CAC41351 and 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="V -> L (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="V -> M (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="V -> A (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="N -> K (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="N -> S (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="L -> V (in Ref. 2; AAK40270)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="V -> I (in Ref. 1; CAC41351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 52994 MW; 6823E7682AC78B19 CRC64;
MEKAHADEFP LTTDSSEKQG VVCIFGTGDF GKSLGLKMLQ CGYSIVFGSR NPQVSSLLPR
GAEVLSYSEA ASKSDIIILA MHREHYDSLT ELVDYLKGKV LVDVSNNRKI NQYPESNAEY
LAQLEPGAHV VKAFNTISAW ALQSGTLDAS RQVFVCGNDS KAKQRVMDIA RTLGLTPLDQ
GSLMAASEIE NYPLQLFPMW RFPFYLSSVL CVFFFVYCAI REVIYPYVNG KTDATYRLAI
SIPNRVFPIT ALILLALVYL PGILAAILQL YRGTKYRRFP NWLDHWMLCR KQLGLVALGF
AFLHVIYTLV IPIRYYVRWR LRNATITQAL TNKDSPFITS YAWINDSYLA LGILGFFLFL
LLGITSLPSV SNMVNWREFR FVQSKLGYLT LVLCTAHTLV YGGKRFLSPS ILRWSLPSAY
ILALVIPCAV LVLKCILIMP CIDKTLTRIR QGWERNSKYT QSALNGKSDI
