VLDLR_MOUSE
ID VLDLR_MOUSE Reviewed; 873 AA.
AC P98156; Q64022;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Very low-density lipoprotein receptor;
DE Short=VLDL receptor;
DE Short=VLDL-R;
DE Flags: Precursor;
GN Name=Vldlr;
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].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=7925422; DOI=10.1111/j.1432-1033.1994.00975.x;
RA Oka K., Ishimura-Oka K., Chu M.J., Sullivan M., Krushkal J., Li W.H.,
RA Chan L.;
RT "Mouse very-low-density-lipoprotein receptor (VLDLR) cDNA cloning, tissue-
RT specific expression and evolutionary relationship with the low-density-
RT lipoprotein receptor.";
RL Eur. J. Biochem. 224:975-982(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=8013374; DOI=10.1210/endo.135.1.8013374;
RA Gafvels M.E., Paavola L.G., Boyd C.O., Nolan P.M., Wittmaack F., Chawla A.,
RA Lazar M.A., Bucan M., Angelin B.O., Strauss J.F.;
RT "Cloning of a complementary deoxyribonucleic acid encoding the murine
RT homolog of the very low density lipoprotein/apolipoprotein-E receptor:
RT expression pattern and assignment of the gene to mouse chromosome 19.";
RL Endocrinology 135:387-394(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-262.
RX PubMed=7919660; DOI=10.1007/bf00357008;
RA Naggert J.K., Mu J.L.;
RT "The mouse very low density lipoprotein receptor (Vldlr) gene maps to
RT chromosome 19.";
RL Mamm. Genome 5:453-455(1994).
RN [4]
RP INTERACTION WITH RELN.
RX PubMed=10571241; DOI=10.1016/s0896-6273(00)80861-2;
RA Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C.,
RA Cooper J.A., Herz J.;
RT "Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces
RT tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation.";
RL Neuron 24:481-489(1999).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11108739;
RA Tacken P.J., Teusink B., Jong M.C., Harats D., Havekes L.M., van Dijk K.W.,
RA Hofker M.H.;
RT "LDL receptor deficiency unmasks altered VLDL triglyceride metabolism in
RT VLDL receptor transgenic and knockout mice.";
RL J. Lipid Res. 41:2055-2062(2000).
RN [6]
RP INTERACTION WITH SNX17.
RX PubMed=12169628; DOI=10.1093/emboj/cdf435;
RA Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D., Kahr L.,
RA Schneider W.J., Nimpf J.;
RT "The PX-domain protein SNX17 interacts with members of the LDL receptor
RT family and modulates endocytosis of the LDL receptor.";
RL EMBO J. 21:4259-4267(2002).
RN [7]
RP INTERACTION WITH LDLRAP1.
RX PubMed=12746448; DOI=10.1074/jbc.m304855200;
RA Jones C., Hammer R.E., Li W.-P., Cohen J.C., Hobbs H.H., Herz J.;
RT "Normal sorting but defective endocytosis of the low density lipoprotein
RT receptor in mice with autosomal recessive hypercholesterolemia.";
RL J. Biol. Chem. 278:29024-29030(2003).
RN [8]
RP FUNCTION.
RX PubMed=17913789; DOI=10.1242/dev.005447;
RA Hack I., Hellwig S., Junghans D., Brunne B., Bock H.H., Zhao S.,
RA Frotscher M.;
RT "Divergent roles of ApoER2 and Vldlr in the migration of cortical
RT neurons.";
RL Development 134:3883-3891(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Heart;
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).
RN [10]
RP UBIQUITINATION.
RX PubMed=20427281; DOI=10.1074/jbc.m110.123729;
RA Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V.,
RA Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D., Nimpf J.,
RA van Berkel T.J., Tontonoz P., Zelcer N.;
RT "The E3 ubiquitin ligase IDOL induces the degradation of the low density
RT lipoprotein receptor family members VLDLR and ApoER2.";
RL J. Biol. Chem. 285:19720-19726(2010).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23506116; DOI=10.1111/gtc.12045;
RA Fuchigami T., Sato Y., Tomita Y., Takano T., Miyauchi S.Y., Tsuchiya Y.,
RA Saito T., Kubo K., Nakajima K., Fukuda M., Hattori M., Hisanaga S.;
RT "Dab1-mediated colocalization of multi-adaptor protein CIN85 with Reelin
RT receptors, ApoER2 and VLDLR, in neurons.";
RL Genes Cells 18:410-424(2013).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24293365; DOI=10.1074/jbc.m113.515320;
RA Nguyen A., Tao H., Metrione M., Hajri T.;
RT "Very low density lipoprotein receptor (VLDLR) expression is a determinant
RT factor in adipose tissue inflammation and adipocyte-macrophage
RT interaction.";
RL J. Biol. Chem. 289:1688-1703(2014).
CC -!- FUNCTION: Multifunctional cell surface receptor that binds VLDL and
CC transports it into cells by endocytosis and therefore plays an
CC important role in energy metabolism (PubMed:11108739, PubMed:24293365).
CC Binds also to a wide range of other molecules including Reelin/RELN or
CC apolipoprotein E/APOE-containing ligands as well as clusterin/CLU. In
CC the off-state of the pathway LRP8 and VLDLR form homo or
CC heterooligomers (By similarity). Upon binding to ligands, homooligomers
CC are rearranged to higher order receptor clusters that transmit the
CC extracellular RELN signal to intracellular signaling processes by
CC binding to DAB1 on its cytoplasmic tail (By similarity). This
CC interaction results in phosphorylation of DAB1 leading to the ultimate
CC cell responses required for the correct positioning of newly generated
CC neurons (PubMed:23506116). Later, mediates a stop signal for migrating
CC neurons, preventing them from entering the marginal zone
CC (PubMed:17913789). {ECO:0000250|UniProtKB:P98155,
CC ECO:0000269|PubMed:11108739, ECO:0000269|PubMed:17913789,
CC ECO:0000269|PubMed:23506116, ECO:0000269|PubMed:24293365}.
CC -!- SUBUNIT: Homooligomer (By similarity). Binds to the extracellular
CC matrix protein Reelin/RELN (PubMed:10571241). Interacts with LRP8 (By
CC similarity). Interacts with LDLRAP1 (PubMed:12746448). Interacts with
CC SNX17 (PubMed:12169628). Interacts with DAB1. Interacts with PCSK9 (By
CC similarity). Interacts with PAFAH1B3 and PAFAH1B2, the catalytic
CC complex of (PAF-AH (I)) heterotetrameric enzyme; these interactions may
CC modulate the Reelin pathway (By similarity). Interacts with STX5; this
CC interaction mediates VLDLR translocation from the endoplasmic reticulum
CC to the plasma membrane (By similarity). Interacts with CLU (By
CC similarity). {ECO:0000250|UniProtKB:P98155,
CC ECO:0000269|PubMed:10571241, ECO:0000269|PubMed:12169628,
CC ECO:0000269|PubMed:12746448}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Membrane, clathrin-coated pit; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Abundant in heart and muscle; less in kidney,
CC brain, ovary, testis, lung and adipose tissue. Strongly expressed in
CC neurons (PubMed:23506116).
CC -!- PTM: Ubiquitinated at Lys-839 by MYLIP leading to degradation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant mice show an increase in serum
CC triglycerides under a high fat diet, suggesting a role in extrahepatic
CC triglyceride uptake (PubMed:11108739). In addition, these mice show a
CC reduced high fat diet-induced inflammation and endoplasmic reticulum
CC (ER) stress in adipose tissue in conjunction with reduced macrophage
CC infiltration (PubMed:24293365). {ECO:0000269|PubMed:11108739,
CC ECO:0000269|PubMed:24293365}.
CC -!- MISCELLANEOUS: LRP8 and VLVLR together are required for correct
CC embryonic development in the brain. Targeted disruption of both genes
CC results in a phenotype virtually indistinguishable from that seen in
CC 'reeler' and 'scrambler' mice. Subtle effects of VLDLR deletion are
CC found mainly in the cerebellum, whereas lack of LRP8 predominantly
CC affects the positioning of the neurons in the neocortex.
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DR EMBL; L33417; AAC37668.1; -; mRNA.
DR EMBL; U06670; AAA59384.1; -; mRNA.
DR EMBL; S73732; AAB32228.2; -; Genomic_DNA.
DR CCDS; CCDS29721.1; -.
DR PIR; I48952; I48952.
DR RefSeq; NP_001154892.1; NM_001161420.1.
DR RefSeq; NP_038731.2; NM_013703.2.
DR RefSeq; XP_006526980.1; XM_006526917.1.
DR RefSeq; XP_006526981.1; XM_006526918.2.
DR AlphaFoldDB; P98156; -.
DR SMR; P98156; -.
DR BioGRID; 204529; 9.
DR DIP; DIP-33283N; -.
DR IntAct; P98156; 2.
DR STRING; 10090.ENSMUSP00000127329; -.
DR GlyGen; P98156; 3 sites.
DR iPTMnet; P98156; -.
DR PhosphoSitePlus; P98156; -.
DR MaxQB; P98156; -.
DR PaxDb; P98156; -.
DR PeptideAtlas; P98156; -.
DR PRIDE; P98156; -.
DR ProteomicsDB; 297961; -.
DR Antibodypedia; 9217; 489 antibodies from 36 providers.
DR DNASU; 22359; -.
DR Ensembl; ENSMUST00000167487; ENSMUSP00000127329; ENSMUSG00000024924.
DR GeneID; 22359; -.
DR KEGG; mmu:22359; -.
DR UCSC; uc008hbt.2; mouse.
DR CTD; 7436; -.
DR MGI; MGI:98935; Vldlr.
DR VEuPathDB; HostDB:ENSMUSG00000024924; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000155460; -.
DR InParanoid; P98156; -.
DR OMA; DEYACKN; -.
DR OrthoDB; 359795at2759; -.
DR PhylomeDB; P98156; -.
DR TreeFam; TF351700; -.
DR Reactome; R-MMU-8866376; Reelin signalling pathway.
DR Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
DR Reactome; R-MMU-8964046; VLDL clearance.
DR BioGRID-ORCS; 22359; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Vldlr; mouse.
DR PRO; PR:P98156; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P98156; protein.
DR Bgee; ENSMUSG00000024924; Expressed in decidua and 270 other tissues.
DR ExpressionAtlas; P98156; baseline and differential.
DR Genevisible; P98156; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0038024; F:cargo receptor activity; ISO:MGI.
DR GO; GO:0038025; F:reelin receptor activity; IMP:CACAO.
DR GO; GO:0034189; F:very-low-density lipoprotein particle binding; ISO:MGI.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; ISS:BHF-UCL.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:CACAO.
DR GO; GO:0034436; P:glycoprotein transport; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:1900006; P:positive regulation of dendrite development; IGI:BHF-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IGI:BHF-UCL.
DR GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; ISS:BHF-UCL.
DR CDD; cd00112; LDLa; 8.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 4.10.400.10; -; 8.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR032931; VLDLR.
DR PANTHER; PTHR24270:SF16; PTHR24270:SF16; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57424; SSF57424; 8.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 8.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 5.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Coated pit; Disulfide bond; EGF-like domain;
KW Endocytosis; Glycoprotein; Isopeptide bond; Lipid metabolism;
KW Lipid transport; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation; VLDL.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..873
FT /note="Very low-density lipoprotein receptor"
FT /id="PRO_0000017344"
FT TOPO_DOM 28..797
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 798..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..69
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 70..110
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 111..151
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 152..190
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 191..231
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 237..275
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 276..314
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 316..355
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 356..391
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 396..431
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 439..480
FT /note="LDL-receptor class B 1"
FT REPEAT 481..524
FT /note="LDL-receptor class B 2"
FT REPEAT 525..567
FT /note="LDL-receptor class B 3"
FT REPEAT 568..611
FT /note="LDL-receptor class B 4"
FT REPEAT 612..654
FT /note="LDL-receptor class B 5"
FT REPEAT 655..697
FT /note="LDL-receptor class B 6"
FT DOMAIN 702..750
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 751..790
FT /note="Clustered O-linked oligosaccharides"
FT MOTIF 832..837
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 781
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..45
FT /evidence="ECO:0000250"
FT DISULFID 40..58
FT /evidence="ECO:0000250"
FT DISULFID 52..67
FT /evidence="ECO:0000250"
FT DISULFID 72..84
FT /evidence="ECO:0000250"
FT DISULFID 79..97
FT /evidence="ECO:0000250"
FT DISULFID 91..108
FT /evidence="ECO:0000250"
FT DISULFID 113..127
FT /evidence="ECO:0000250"
FT DISULFID 120..140
FT /evidence="ECO:0000250"
FT DISULFID 134..149
FT /evidence="ECO:0000250"
FT DISULFID 154..166
FT /evidence="ECO:0000250"
FT DISULFID 161..179
FT /evidence="ECO:0000250"
FT DISULFID 173..188
FT /evidence="ECO:0000250"
FT DISULFID 193..205
FT /evidence="ECO:0000250"
FT DISULFID 200..218
FT /evidence="ECO:0000250"
FT DISULFID 212..229
FT /evidence="ECO:0000250"
FT DISULFID 239..251
FT /evidence="ECO:0000250"
FT DISULFID 246..264
FT /evidence="ECO:0000250"
FT DISULFID 258..273
FT /evidence="ECO:0000250"
FT DISULFID 278..290
FT /evidence="ECO:0000250"
FT DISULFID 285..303
FT /evidence="ECO:0000250"
FT DISULFID 297..312
FT /evidence="ECO:0000250"
FT DISULFID 318..331
FT /evidence="ECO:0000250"
FT DISULFID 326..344
FT /evidence="ECO:0000250"
FT DISULFID 338..355
FT /evidence="ECO:0000250"
FT DISULFID 360..371
FT /evidence="ECO:0000250"
FT DISULFID 367..380
FT /evidence="ECO:0000250"
FT DISULFID 382..394
FT /evidence="ECO:0000250"
FT DISULFID 400..410
FT /evidence="ECO:0000250"
FT DISULFID 406..419
FT /evidence="ECO:0000250"
FT DISULFID 421..434
FT /evidence="ECO:0000250"
FT DISULFID 706..719
FT /evidence="ECO:0000250"
FT DISULFID 715..734
FT /evidence="ECO:0000250"
FT DISULFID 736..749
FT /evidence="ECO:0000250"
FT CROSSLNK 839
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P98155"
FT CONFLICT 161
FT /note="C -> G (in Ref. 1; AAC37668)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="P -> L (in Ref. 3; AAB32228)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="C -> S (in Ref. 2; AAA59384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 96373 MW; 08F09F93825195CB CRC64;
MGTSARWALW LLLALCWAPR DSGATASGKK AKCDSSQFQC TNGRCITLLW KCDGDEDCAD
GSDEKNCVKK TCAESDFVCK NGQCVPNRWQ CDGDPDCEDG SDESPEQCHM RTCRINEISC
GARSTQCIPV SWRCDGENDC DNGEDEENCG NITCSADEFT CSSGRCVSRN FVCNGQDDCD
DGSDELDCAP PTCGAHEFQC STSSCIPLSW VCDDDADCSD QSDESLEQCG RQPVIHTKCP
TSEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI
RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDMSKVCDQ EQDCRDWSDE PLKECHINEC
LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE
CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA
QKLFWADLSQ KAIFSASIDD KVGRHFKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA
TLDGAKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTEDIQ
WPNGITLDLV KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI
DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEDDM ENGGCEYLCL
PAPQINDHSP KYTCSCPNGY NLEENGRECQ STSTPVTYSE TKDINTTDIL RTSGLVPGGI
NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT
TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA
