TMPS6_MOUSE
ID TMPS6_MOUSE Reviewed; 811 AA.
AC Q9DBI0; A8W478; A8W479; Q3KN88; Q6PF94;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Transmembrane protease serine 6;
DE EC=3.4.21.-;
DE AltName: Full=Matriptase-2;
GN Name=Tmprss6;
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 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=12744720; DOI=10.1042/bj20030390;
RA Hooper J.D., Campagnolo L., Goodarzi G., Truong T.N., Stuhlmann H.,
RA Quigley J.P.;
RT "Mouse matriptase-2: identification, characterization and comparative mRNA
RT expression analysis with mouse hepsin in adult and embryonic tissues.";
RL Biochem. J. 373:689-702(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, DOMAIN,
RP MUTAGENESIS OF SER-762, AND DISRUPTION PHENOTYPE.
RC TISSUE=Liver;
RX PubMed=18451267; DOI=10.1126/science.1157121;
RA Du X., She E., Gelbart T., Truksa J., Lee P., Xia Y., Khovananth K.,
RA Mudd S., Mann N., Moresco E.M.Y., Beutler E., Beutler B.;
RT "The serine protease TMPRSS6 is required to sense iron deficiency.";
RL Science 320:1088-1092(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [6]
RP REVIEW.
RX PubMed=12784999; DOI=10.1023/a:1023003616848;
RA Netzel-Arnett S., Hooper J.D., Szabo R., Madison E.L., Quigley J.P.,
RA Bugge T.H., Antalis T.M.;
RT "Membrane anchored serine proteases: a rapidly expanding group of cell
RT surface proteolytic enzymes with potential roles in cancer.";
RL Cancer Metastasis Rev. 22:237-258(2003).
RN [7]
RP REVIEW.
RX PubMed=17981570; DOI=10.2741/2702;
RA Ramsay A.J., Reid J.C., Velasco G., Quigley J.P., Hooper J.D.;
RT "The type II transmembrane serine protease matriptase-2 -- identification,
RT structural features, enzymology, expression pattern and potential roles.";
RL Front. Biosci. 13:569-579(2008).
CC -!- FUNCTION: Membrane-bound serine protease (PubMed:18451267). Through the
CC cleavage of cell surface HJV, a regulator of the expression of the iron
CC absorption-regulating hormone hepicidin/HAMP, plays a role in iron
CC homeostasis (PubMed:18451267). {ECO:0000269|PubMed:18451267}.
CC -!- SUBUNIT: Interacts with HJV. {ECO:0000250|UniProtKB:Q8IU80}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12744720};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:12744720}.
CC Note=The processed, activated two-chains form is released in the
CC extracellular space. {ECO:0000250|UniProtKB:Q8IU80}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9DBI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBI0-2; Sequence=VSP_035564, VSP_035567;
CC Name=3;
CC IsoId=Q9DBI0-3; Sequence=VSP_035565, VSP_035566;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in adult mice liver,
CC kidney and uterus. Also strongly expressed within the nasal cavity by
CC olfactory epithelial cells. A weak, but detectable, signal in adult
CC mice tissues analyzed including brain, lung, heart, kidney, spleen,
CC muscle, intestine, thymus and pancreas. No signal in residual embryonic
CC yolk sac, developing kidney tubules or in embryonic tissues analyzed
CC including lung, heart, gastrointestinal tract and epithelium of the
CC oral cavity. {ECO:0000269|PubMed:12744720}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher levels from 12.5 dpc to 15.5
CC dpc with a peak at 13.5 dpc. Expressed in the developing liver and at
CC lower levels in developing pharyngo-tympanic tubes.
CC {ECO:0000269|PubMed:12744720}.
CC -!- DOMAIN: Cytoplasmic domain mediates HAMP suppression via proximal
CC promoter element(s). {ECO:0000269|PubMed:18451267}.
CC -!- PTM: The single-chain zymogen undergoes autoproteolytic processing.
CC This results in TMPRSS6 shedding from the cell surface and conversion
CC into an activated two-chains form which is released extracellularly.
CC The process involves a trans-activation mechanism that requires TMPRSS6
CC oligomerization. {ECO:0000250|UniProtKB:Q8IU80}.
CC -!- DISRUPTION PHENOTYPE: Mice display the phenotype named mask,
CC characterized by progressive loss of body (but not facial) hair,
CC microcytic anemia and female infertility, all reversible by dietary
CC iron supplementation. The mask phenotype results from reduced
CC absorption of dietary iron caused by high levels of hepcidin.
CC {ECO:0000269|PubMed:18451267}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY240929; AAP69827.1; -; mRNA.
DR EMBL; EU190436; ABW38782.1; -; mRNA.
DR EMBL; EU190437; ABW38783.1; -; mRNA.
DR EMBL; AK004939; BAB23684.2; -; mRNA.
DR EMBL; AL590144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029645; AAH29645.2; -; mRNA.
DR EMBL; BC057674; AAH57674.1; ALT_INIT; mRNA.
DR EMBL; BK000520; DAA00246.1; -; Genomic_DNA.
DR CCDS; CCDS37133.1; -. [Q9DBI0-1]
DR RefSeq; NP_082178.2; NM_027902.2. [Q9DBI0-1]
DR RefSeq; XP_006521479.1; XM_006521416.2.
DR AlphaFoldDB; Q9DBI0; -.
DR SMR; Q9DBI0; -.
DR BioGRID; 214901; 11.
DR IntAct; Q9DBI0; 1.
DR STRING; 10090.ENSMUSP00000017086; -.
DR MEROPS; S01.308; -.
DR GlyGen; Q9DBI0; 7 sites.
DR PhosphoSitePlus; Q9DBI0; -.
DR MaxQB; Q9DBI0; -.
DR PaxDb; Q9DBI0; -.
DR PeptideAtlas; Q9DBI0; -.
DR PRIDE; Q9DBI0; -.
DR ProteomicsDB; 260709; -. [Q9DBI0-1]
DR ProteomicsDB; 260710; -. [Q9DBI0-2]
DR ProteomicsDB; 260711; -. [Q9DBI0-3]
DR Antibodypedia; 25860; 160 antibodies from 21 providers.
DR DNASU; 71753; -.
DR Ensembl; ENSMUST00000017086; ENSMUSP00000017086; ENSMUSG00000016942. [Q9DBI0-1]
DR Ensembl; ENSMUST00000229516; ENSMUSP00000155355; ENSMUSG00000016942. [Q9DBI0-2]
DR Ensembl; ENSMUST00000230159; ENSMUSP00000155549; ENSMUSG00000016942. [Q9DBI0-3]
DR GeneID; 71753; -.
DR KEGG; mmu:71753; -.
DR UCSC; uc007wpi.1; mouse. [Q9DBI0-1]
DR UCSC; uc011zvt.1; mouse. [Q9DBI0-2]
DR CTD; 164656; -.
DR MGI; MGI:1919003; Tmprss6.
DR VEuPathDB; HostDB:ENSMUSG00000016942; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000160104; -.
DR HOGENOM; CLU_006842_19_3_1; -.
DR InParanoid; Q9DBI0; -.
DR OMA; QVHYSIF; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9DBI0; -.
DR TreeFam; TF330647; -.
DR BRENDA; 3.4.21.109; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 71753; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Tmprss6; mouse.
DR PRO; PR:Q9DBI0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DBI0; protein.
DR Bgee; ENSMUSG00000016942; Expressed in left lobe of liver and 84 other tissues.
DR ExpressionAtlas; Q9DBI0; baseline and differential.
DR Genevisible; Q9DBI0; MM.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IGI:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:BHF-UCL.
DR GO; GO:0042730; P:fibrinolysis; ISS:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
DR GO; GO:0033619; P:membrane protein proteolysis; ISS:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; ISS:UniProtKB.
DR CDD; cd00112; LDLa; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.30.70.960; -; 1.
DR Gene3D; 4.10.400.10; -; 3.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR017118; Pept_S1A_matriptase-2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF037135; Matriptase-2; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57424; SSF57424; 3.
DR SUPFAM; SSF82671; SSF82671; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Repeat; Serine protease;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..811
FT /note="Transmembrane protease serine 6"
FT /id="PRO_0000088697"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..811
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 86..209
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 213..336
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 323..440
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 445..477
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 478..514
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 518..555
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 577..811
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 617
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 668
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 762
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 335..366
FT /evidence="ECO:0000250"
FT DISULFID 458..470
FT /evidence="ECO:0000250"
FT DISULFID 464..480
FT /evidence="ECO:0000250"
FT DISULFID 474..489
FT /evidence="ECO:0000250"
FT DISULFID 491..503
FT /evidence="ECO:0000250"
FT DISULFID 497..516
FT /evidence="ECO:0000250"
FT DISULFID 510..525
FT /evidence="ECO:0000250"
FT DISULFID 531..543
FT /evidence="ECO:0000250"
FT DISULFID 538..557
FT /evidence="ECO:0000250"
FT DISULFID 551..566
FT /evidence="ECO:0000250"
FT DISULFID 602..618
FT /evidence="ECO:0000250"
FT DISULFID 702..768
FT /evidence="ECO:0000250"
FT DISULFID 733..747
FT /evidence="ECO:0000250"
FT DISULFID 758..787
FT /evidence="ECO:0000250"
FT VAR_SEQ 567..594
FT /note="DCGLQGLSSRIVGGTVSSEGEWPWQASL -> AWPPRSCGPCSWERCGRTRA
FT GQARCPSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18451267"
FT /id="VSP_035564"
FT VAR_SEQ 567..581
FT /note="DCGLQGLSSRIVGGT -> GPLQPYCGRDRVLRG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18451267"
FT /id="VSP_035565"
FT VAR_SEQ 582..811
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18451267"
FT /id="VSP_035566"
FT VAR_SEQ 595..811
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18451267"
FT /id="VSP_035567"
FT MUTAGEN 762
FT /note="S->A: Protease-dead."
FT /evidence="ECO:0000269|PubMed:18451267"
FT CONFLICT 690
FT /note="P -> PP (in Ref. 3; BAB23684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 811 AA; 90978 MW; 32EB3E7C3127801B CRC64;
MPRCFQLPCS TRMPTTEVPQ AADGQGDAGD GEEAAEPEGK FKPPKNTKRK NRDYVRFTPL
LLVLAALVSA GVMLWYFLGY KAEVTVSQVY SGSLRVLNRH FSQDLGRRES IAFRSESAKA
QKMLQELVAS TRLGTYYNSS SVYSFGEGPL TCFFWFILDI PEYQRLTLSP EVVRELLVDE
LLSNSSTLAS YKTEYEVDPE GLVILEASVN DIVVLNSTLG CYRYSYVNPG QVLPLKGPDQ
QTTSCLWHLQ GPEDLMIKVR LEWTRVDCRD RVAMYDAAGP LEKRLITSVY GCSRQEPVME
VLASGSVMAV VWKKGMHSYY DPFLLSVKSV AFQDCQVNLT LEGRLDTQGF LRTPYYPSYY
SPSTHCSWHL TVPSLDYGLA LWFDAYALRR QKYNRLCTQG QWMIQNRRLC GFRTLQPYAE
RIPMVASDGV TINFTSQISL TGPGVQVYYS LYNQSDPCPG EFLCSVNGLC VPACDGIKDC
PNGLDERNCV CRAMFQCQED STCISLPRVC DRQPDCLNGS DEEQCQEGVP CGTFTFQCED
RSCVKKPNPE CDGQSDCRDG SDEQHCDCGL QGLSSRIVGG TVSSEGEWPW QASLQIRGRH
ICGGALIADR WVITAAHCFQ EDSMASPKLW TVFLGKMRQN SRWPGEVSFK VSRLFLHPYH
EEDSHDYDVA LLQLDHPVVY SATVRPVCLP ARSHFFEPGQ HCWITGWGAQ REGGPVSNTL
QKVDVQLVPQ DLCSEAYRYQ VSPRMLCAGY RKGKKDACQG DSGGPLVCRE PSGRWFLAGL
VSWGLGCGRP NFFGVYTRVT RVINWIQQVL T
