LSR_MOUSE
ID LSR_MOUSE Reviewed; 594 AA.
AC Q99KG5; Q3TJE7; Q3UIQ9; Q61148; Q61149; Q6U816;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Lipolysis-stimulated lipoprotein receptor {ECO:0000305};
DE AltName: Full=Angulin-3 {ECO:0000303|PubMed:23239027};
DE AltName: Full=Lipolysis-stimulated receptor;
DE AltName: Full=Liver-specific bHLH-Zip transcription factor;
DE AltName: Full=Liver-specific gene on mouse chromosome 7 protein;
DE Flags: Precursor;
GN Name=Lsr {ECO:0000312|MGI:MGI:1927471}; Synonyms=Ildr3, Lisch7;
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), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 256-594.
RC STRAIN=C57BL/6 X CBA;
RA Lin Q., Ooi K.S., Sawadogo M.;
RT "Lisch7, a liver-specific gene immediately upstream of the USF2 gene on
RT mouse chromosome 7.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-576, FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/Ola;
RX PubMed=15265030; DOI=10.1111/j.1432-1033.2004.04223.x;
RA Mesli S., Javorschi S., Berard A.M., Landry M., Priddle H., Kivlichan D.,
RA Smith A.J.H., Yen F.T., Bihain B.E., Darmon M.;
RT "Distribution of the lipolysis stimulated receptor in adult and embryonic
RT murine tissues and lethality of LSR-/- embryos at 12.5 to 14.5 days of
RT gestation.";
RL Eur. J. Biochem. 271:3103-3114(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-588, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND SER-379, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, 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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, AND
RP INTERACTION WITH MARVELD2.
RX PubMed=21245199; DOI=10.1242/jcs.072058;
RA Masuda S., Oda Y., Sasaki H., Ikenouchi J., Higashi T., Akashi M.,
RA Nishi E., Furuse M.;
RT "LSR defines cell corners for tricellular tight junction formation in
RT epithelial cells.";
RL J. Cell Sci. 124:548-555(2011).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH MARVELD2 AND OCLN.
RX PubMed=23239027; DOI=10.1242/jcs.116442;
RA Higashi T., Tokuda S., Kitajiri S., Masuda S., Nakamura H., Oda Y.,
RA Furuse M.;
RT "Analysis of the 'angulin' proteins LSR, ILDR1 and ILDR2--tricellulin
RT recruitment, epithelial barrier function and implication in deafness
RT pathogenesis.";
RL J. Cell Sci. 126:966-977(2013).
RN [9]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-308, AND MUTAGENESIS OF
RP SER-308.
RX PubMed=24889144; DOI=10.1111/gtc.12158;
RA Nakatsu D., Kano F., Taguchi Y., Sugawara T., Nishizono T., Nishikawa K.,
RA Oda Y., Furuse M., Murata M.;
RT "JNK1/2-dependent phosphorylation of angulin-1/LSR is required for the
RT exclusive localization of angulin-1/LSR and tricellulin at tricellular
RT contacts in EpH4 epithelial sheet.";
RL Genes Cells 19:565-581(2014).
CC -!- FUNCTION: Probable role in the clearance of triglyceride-rich
CC lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of
CC free fatty acids and allows their subsequent uptake in the cells
CC (PubMed:15265030). Maintains epithelial barrier function by recruiting
CC MARVELD2/tricellulin to tricellular tight junctions (PubMed:21245199,
CC PubMed:23239027). {ECO:0000269|PubMed:15265030,
CC ECO:0000269|PubMed:21245199, ECO:0000269|PubMed:23239027}.
CC -!- SUBUNIT: Homotrimer or homotetramer (By similarity). Assembles into
CC cell-cell contacts (PubMed:21245199). Interacts (via the cytoplasmic
CC domain) with MARVELD2 (via C-terminal cytoplasmic domain); the
CC interaction is required to recruit MARVELD2 to tricellular contacts
CC (PubMed:21245199, PubMed:23239027). Interacts with OCLN
CC (PubMed:23239027). {ECO:0000250, ECO:0000250|UniProtKB:Q9WU74,
CC ECO:0000269|PubMed:21245199, ECO:0000269|PubMed:23239027}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21245199};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight
CC junction {ECO:0000269|PubMed:21245199, ECO:0000269|PubMed:23239027,
CC ECO:0000269|PubMed:24889144}. Note=Located at tricellular contacts.
CC {ECO:0000269|PubMed:21245199, ECO:0000269|PubMed:23239027,
CC ECO:0000269|PubMed:24889144}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99KG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KG5-2; Sequence=VSP_019696;
CC Name=3;
CC IsoId=Q99KG5-3; Sequence=VSP_019695;
CC -!- TISSUE SPECIFICITY: Expressed in eptihelial tissues (at protein level)
CC (PubMed:21245199). Specifically expressed in liver and to a lower
CC extent in kidney (at protein level). Also detected in brain, testis,
CC ovaries, adrenal gland, intestine, muscle, and lung. In colon, only
CC expressed in the lower portion of crypts (PubMed:23239027).
CC {ECO:0000269|PubMed:15265030, ECO:0000269|PubMed:21245199,
CC ECO:0000269|PubMed:23239027}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in liver, stomach, small
CC intestine and colon. Also detected in other epithelial tissues.
CC {ECO:0000269|PubMed:23239027}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (at protein level).
CC Detected from 7.5 dpc to 17 dpc. {ECO:0000269|PubMed:15265030}.
CC -!- PTM: Phosphorylation at Ser-308 by MAPK8/JNK1 and MAPK9/JNK2 may be
CC required for exclusive localization at tricellular tight junstions.
CC {ECO:0000269|PubMed:24889144}.
CC -!- DISRUPTION PHENOTYPE: Death between 12.5 dpc and 15.5 dpc probably due
CC to impaired liver and embryonic development.
CC {ECO:0000269|PubMed:15265030}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. LISCH7 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92719.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U49507; AAA92719.1; ALT_FRAME; mRNA.
DR EMBL; U49508; AAA92720.1; -; Genomic_DNA.
DR EMBL; AK146807; BAE27447.1; -; mRNA.
DR EMBL; AK167463; BAE39548.1; -; mRNA.
DR EMBL; BC004672; AAH04672.1; -; mRNA.
DR EMBL; AY376636; AAQ83379.1; -; Genomic_DNA.
DR CCDS; CCDS21119.1; -. [Q99KG5-1]
DR CCDS; CCDS52185.1; -. [Q99KG5-3]
DR CCDS; CCDS52186.1; -. [Q99KG5-2]
DR RefSeq; NP_001157656.1; NM_001164184.1. [Q99KG5-2]
DR RefSeq; NP_001157657.1; NM_001164185.1. [Q99KG5-3]
DR RefSeq; NP_059101.1; NM_017405.2. [Q99KG5-1]
DR AlphaFoldDB; Q99KG5; -.
DR BioGRID; 207572; 1.
DR IntAct; Q99KG5; 2.
DR MINT; Q99KG5; -.
DR STRING; 10090.ENSMUSP00000001279; -.
DR iPTMnet; Q99KG5; -.
DR PhosphoSitePlus; Q99KG5; -.
DR SwissPalm; Q99KG5; -.
DR jPOST; Q99KG5; -.
DR MaxQB; Q99KG5; -.
DR PaxDb; Q99KG5; -.
DR PeptideAtlas; Q99KG5; -.
DR PRIDE; Q99KG5; -.
DR ProteomicsDB; 293406; -. [Q99KG5-1]
DR ProteomicsDB; 293407; -. [Q99KG5-2]
DR ProteomicsDB; 293408; -. [Q99KG5-3]
DR Antibodypedia; 1523; 192 antibodies from 29 providers.
DR DNASU; 54135; -.
DR Ensembl; ENSMUST00000001279; ENSMUSP00000001279; ENSMUSG00000001247. [Q99KG5-1]
DR Ensembl; ENSMUST00000098553; ENSMUSP00000096153; ENSMUSG00000001247. [Q99KG5-3]
DR Ensembl; ENSMUST00000108116; ENSMUSP00000103751; ENSMUSG00000001247. [Q99KG5-2]
DR Ensembl; ENSMUST00000205961; ENSMUSP00000146120; ENSMUSG00000001247. [Q99KG5-1]
DR GeneID; 54135; -.
DR KEGG; mmu:54135; -.
DR UCSC; uc009ghj.2; mouse. [Q99KG5-1]
DR UCSC; uc009ghk.2; mouse. [Q99KG5-2]
DR UCSC; uc009ghl.2; mouse. [Q99KG5-3]
DR CTD; 51599; -.
DR MGI; MGI:1927471; Lsr.
DR VEuPathDB; HostDB:ENSMUSG00000001247; -.
DR eggNOG; ENOG502QWP5; Eukaryota.
DR GeneTree; ENSGT00950000183058; -.
DR HOGENOM; CLU_028969_2_0_1; -.
DR InParanoid; Q99KG5; -.
DR OMA; GPLMNQP; -.
DR OrthoDB; 457764at2759; -.
DR PhylomeDB; Q99KG5; -.
DR TreeFam; TF330877; -.
DR BioGRID-ORCS; 54135; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Lsr; mouse.
DR PRO; PR:Q99KG5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99KG5; protein.
DR Bgee; ENSMUSG00000001247; Expressed in mucosa of stomach and 203 other tissues.
DR ExpressionAtlas; Q99KG5; baseline and differential.
DR Genevisible; Q99KG5; MM.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0070160; C:tight junction; IDA:UniProtKB.
DR GO; GO:0061689; C:tricellular tight junction; IDA:UniProtKB.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0030228; F:lipoprotein particle receptor activity; TAS:HGNC-UCL.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; TAS:HGNC-UCL.
DR GO; GO:0010669; P:epithelial structure maintenance; IDA:UniProtKB.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IMP:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IDA:ARUK-UCL.
DR GO; GO:0042953; P:lipoprotein transport; TAS:HGNC-UCL.
DR GO; GO:0001889; P:liver development; IMP:HGNC-UCL.
DR GO; GO:0061833; P:protein localization to tricellular tight junction; IMP:ARUK-UCL.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI.
DR GO; GO:1904274; P:tricellular tight junction assembly; IDA:ARUK-UCL.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR008664; LISCH7.
DR Pfam; PF05624; LSR; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Chylomicron;
KW Disulfide bond; Immunoglobulin domain; LDL; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Tight junction; Transmembrane;
KW Transmembrane helix; VLDL.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..594
FT /note="Lipolysis-stimulated lipoprotein receptor"
FT /id="PRO_0000245309"
FT TOPO_DOM 36..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 89..181
FT /note="Ig-like V-type"
FT REGION 375..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU74"
FT MOD_RES 308
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000269|PubMed:24889144,
FT ECO:0007744|PubMed:17242355"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 478
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X29"
FT DISULFID 113..165
FT /evidence="ECO:0000250"
FT VAR_SEQ 187..255
FT /note="GRTSEAPELLPGFRAGPLEDWLFVVVVCLASLLFFLLLGICWCQCCPHTCCC
FT YVRCPCCPDKCCCPEAL -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019695"
FT VAR_SEQ 187..205
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019696"
FT MUTAGEN 308
FT /note="S->A: Decreased phosphorylation levels."
FT /evidence="ECO:0000269|PubMed:24889144"
FT CONFLICT 423
FT /note="P -> T (in Ref. 1; AAA92720)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="P -> H (in Ref. 2; BAE39548)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="R -> L (in Ref. 1; AAA92720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 66108 MW; 2ADE28BB870A001D CRC64;
MAPAASACAG APGSHPATTI FVCLFLIIYC PDRASAIQVT VPDPYHVVIL FQPVTLHCTY
QMSNTLTAPI VIWKYKSFCR DRVADAFSPA SVDNQLNAQL AAGNPGYNPY VECQDSVRTV
RVVATKQGNA VTLGDYYQGR RITITGNADL TFEQTAWGDS GVYYCSVVSA QDLDGNNEAY
AELIVLGRTS EAPELLPGFR AGPLEDWLFV VVVCLASLLF FLLLGICWCQ CCPHTCCCYV
RCPCCPDKCC CPEALYAAGK AATSGVPSIY APSIYTHLSP AKTPPPPPAM IPMRPPYGYP
GDFDRTSSVG GHSSQVPLLR EVDGSVSSEV RSGYRIQANQ QDDSMRVLYY MEKELANFDP
SRPGPPNGRV ERAMSEVTSL HEDDWRSRPS RAPALTPIRD EEWNRHSPRS PRTWEQEPLQ
EQPRGGWGSG RPRARSVDAL DDINRPGSTE SGRSSPPSSG RRGRAYAPPR SRSRDDLYDP
DDPRDLPHSR DPHYYDDLRS RDPRADPRSR QRSHDPRDAG FRSRDPQYDG RLLEEALKKK
GAGERRRVYR EEEEEEEEGH YPPAPPPYSE TDSQASRERR MKKNLALSRE SLVV
