LDLR_MOUSE
ID LDLR_MOUSE Reviewed; 862 AA.
AC P35951; Q6GTJ9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Low-density lipoprotein receptor;
DE Short=LDL receptor;
DE Flags: Precursor;
GN Name=Ldlr;
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=Liver;
RX PubMed=8466528; DOI=10.1006/bbrc.1993.1299;
RA Hoffer M.J.V., van Eck M.M., Petrij F., van der Zee A., de Wit E.,
RA Meijer D., Grosveld G., Havekes L.M., Hofker M.H., Frants R.R.;
RT "The mouse low density lipoprotein receptor gene: cDNA sequence and exon-
RT intron structure.";
RL Biochem. Biophys. Res. Commun. 191:880-886(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1475710; DOI=10.1007/bf01233084;
RA Polvino W.J., Dichek D.A., Mason J., Anderson W.F.;
RT "Molecular cloning and nucleotide sequence of cDNA encoding a functional
RT murine low-density-lipoprotein receptor.";
RL Somat. Cell Mol. Genet. 18:443-450(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH DAB2, DOMAIN, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
RA Morris S.M., Cooper J.A.;
RT "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts
RT with AP-2.";
RL Traffic 2:111-123(2001).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, Lung, Pancreas, Spleen, and
RC 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: Binds LDL, the major cholesterol-carrying lipoprotein of
CC plasma, and transports it into cells by endocytosis. In order to be
CC internalized, the receptor-ligand complexes must first cluster into
CC clathrin-coated pits. {ECO:0000250|UniProtKB:P01130}.
CC -!- SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain); the
CC interaction is impaired by tyrosine phosphorylation of the NPXY motif
CC (PubMed:11247302). Interacts (via NPXY motif) with LDLRAP1 (via PID
CC domain) (By similarity). Interacts with ARRB1 (By similarity).
CC Interacts with SNX17 (PubMed:12169628). Interacts with the full-length
CC immature form of PCSK9 (via C-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:P01130, ECO:0000269|PubMed:11247302,
CC ECO:0000269|PubMed:12169628}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01130};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}.
CC Membrane, clathrin-coated pit {ECO:0000269|PubMed:11247302}. Golgi
CC apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome
CC {ECO:0000250|UniProtKB:P01130}. Late endosome
CC {ECO:0000250|UniProtKB:P01130}. Lysosome
CC {ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon ligand
CC binding. {ECO:0000269|PubMed:12169628}.
CC -!- DOMAIN: The NPXY motif mediates the interaction with the clathrin
CC adapter DAB2 and with LDLRAP1 which are involved in receptor
CC internalization. A few residues outside the motif also play a role in
CC the interaction. {ECO:0000269|PubMed:11247302}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P01130}.
CC -!- PTM: Ubiquitinated by MYLIP leading to degradation.
CC {ECO:0000250|UniProtKB:P01130}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z19521; CAA79581.1; -; mRNA.
DR EMBL; X64414; CAA45759.1; -; mRNA.
DR EMBL; AC161371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466522; EDL25212.1; -; Genomic_DNA.
DR EMBL; BC053041; AAH53041.1; -; mRNA.
DR CCDS; CCDS22910.1; -.
DR PIR; I48623; QRMSLD.
DR RefSeq; NP_001239587.1; NM_001252658.1.
DR RefSeq; NP_001239588.1; NM_001252659.1.
DR RefSeq; NP_034830.2; NM_010700.3.
DR AlphaFoldDB; P35951; -.
DR SMR; P35951; -.
DR BioGRID; 201133; 8.
DR ComplexPortal; CPX-129; LDLR-PCSK9 complex.
DR IntAct; P35951; 2.
DR MINT; P35951; -.
DR STRING; 10090.ENSMUSP00000034713; -.
DR GlyGen; P35951; 3 sites.
DR iPTMnet; P35951; -.
DR PhosphoSitePlus; P35951; -.
DR SwissPalm; P35951; -.
DR EPD; P35951; -.
DR jPOST; P35951; -.
DR PaxDb; P35951; -.
DR PeptideAtlas; P35951; -.
DR PRIDE; P35951; -.
DR ProteomicsDB; 265056; -.
DR Antibodypedia; 2424; 965 antibodies from 43 providers.
DR DNASU; 16835; -.
DR Ensembl; ENSMUST00000034713; ENSMUSP00000034713; ENSMUSG00000032193.
DR GeneID; 16835; -.
DR KEGG; mmu:16835; -.
DR UCSC; uc009omh.2; mouse.
DR CTD; 3949; -.
DR MGI; MGI:96765; Ldlr.
DR VEuPathDB; HostDB:ENSMUSG00000032193; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000161046; -.
DR HOGENOM; CLU_008163_2_0_1; -.
DR InParanoid; P35951; -.
DR OMA; IMNEAIF; -.
DR OrthoDB; 359795at2759; -.
DR PhylomeDB; P35951; -.
DR TreeFam; TF351700; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8964026; Chylomicron clearance.
DR Reactome; R-MMU-8964038; LDL clearance.
DR BioGRID-ORCS; 16835; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Ldlr; mouse.
DR PRO; PR:P35951; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P35951; protein.
DR Bgee; ENSMUSG00000032193; Expressed in cumulus cell and 264 other tissues.
DR ExpressionAtlas; P35951; baseline and differential.
DR Genevisible; P35951; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:1990666; C:PCSK9-LDLR complex; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR GO; GO:0097443; C:sorting endosome; IDA:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0071813; F:lipoprotein particle binding; IBA:GO_Central.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:MGI.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IDA:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:MGI.
DR GO; GO:0097242; P:amyloid-beta clearance; IGI:ARUK-UCL.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IDA:ARUK-UCL.
DR GO; GO:0048844; P:artery morphogenesis; IMP:BHF-UCL.
DR GO; GO:0071398; P:cellular response to fatty acid; IGI:BHF-UCL.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0070508; P:cholesterol import; IMP:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
DR GO; GO:0030301; P:cholesterol transport; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IGI:BHF-UCL.
DR GO; GO:0030299; P:intestinal cholesterol absorption; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IGI:MGI.
DR GO; GO:0042159; P:lipoprotein catabolic process; IDA:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IGI:MGI.
DR GO; GO:0007616; P:long-term memory; IGI:ARUK-UCL.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IDA:MGI.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IGI:ARUK-UCL.
DR GO; GO:0061889; P:negative regulation of astrocyte activation; IGI:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:1903979; P:negative regulation of microglial cell activation; IGI:ARUK-UCL.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; IDA:ARUK-UCL.
DR GO; GO:0001920; P:negative regulation of receptor recycling; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; IDA:ARUK-UCL.
DR GO; GO:0015914; P:phospholipid transport; IMP:BHF-UCL.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; IDA:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:BHF-UCL.
DR GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IDA:ARUK-UCL.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:ARUK-UCL.
DR GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; ISO:MGI.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IGI:ARUK-UCL.
DR GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; IMP:BHF-UCL.
DR GO; GO:0051246; P:regulation of protein metabolic process; IGI:ARUK-UCL.
DR GO; GO:0061771; P:response to caloric restriction; IGI:ARUK-UCL.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 4.10.400.10; -; 6.
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 Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57424; SSF57424; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 7.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Cholesterol metabolism; Coated pit; Disulfide bond;
KW EGF-like domain; Endocytosis; Endosome; Glycoprotein; Golgi apparatus; LDL;
KW Lipid metabolism; Lipid transport; Lysosome; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Steroid metabolism;
KW Sterol metabolism; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P01131"
FT CHAIN 22..862
FT /note="Low-density lipoprotein receptor"
FT /id="PRO_0000017313"
FT TOPO_DOM 22..790
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P01131"
FT TRANSMEM 791..812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 813..862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11247302"
FT DOMAIN 25..65
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 66..106
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 107..145
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 146..186
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 196..234
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 235..273
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 275..314
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 315..354
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 355..394
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 398..439
FT /note="LDL-receptor class B 1"
FT REPEAT 440..485
FT /note="LDL-receptor class B 2"
FT REPEAT 486..528
FT /note="LDL-receptor class B 3"
FT REPEAT 529..572
FT /note="LDL-receptor class B 4"
FT REPEAT 573..615
FT /note="LDL-receptor class B 5"
FT REPEAT 616..658
FT /note="LDL-receptor class B 6"
FT DOMAIN 663..713
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 722..770
FT /note="Clustered O-linked oligosaccharides"
FT REGION 730..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..862
FT /note="Required for MYLIP-triggered down-regulation of
FT LDLR"
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT MOTIF 825..830
FT /note="NPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT COMPBIAS 747..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 725
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35952"
FT MOD_RES 733
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35952"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35952"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..52
FT /evidence="ECO:0000250"
FT DISULFID 46..63
FT /evidence="ECO:0000250"
FT DISULFID 68..82
FT /evidence="ECO:0000250"
FT DISULFID 75..95
FT /evidence="ECO:0000250"
FT DISULFID 89..104
FT /evidence="ECO:0000250"
FT DISULFID 109..121
FT /evidence="ECO:0000250"
FT DISULFID 116..134
FT /evidence="ECO:0000250"
FT DISULFID 128..143
FT /evidence="ECO:0000250"
FT DISULFID 148..160
FT /evidence="ECO:0000250"
FT DISULFID 155..173
FT /evidence="ECO:0000250"
FT DISULFID 167..184
FT /evidence="ECO:0000250"
FT DISULFID 198..210
FT /evidence="ECO:0000250"
FT DISULFID 205..223
FT /evidence="ECO:0000250"
FT DISULFID 217..232
FT /evidence="ECO:0000250"
FT DISULFID 237..249
FT /evidence="ECO:0000250"
FT DISULFID 244..262
FT /evidence="ECO:0000250"
FT DISULFID 256..271
FT /evidence="ECO:0000250"
FT DISULFID 277..290
FT /evidence="ECO:0000250"
FT DISULFID 285..303
FT /evidence="ECO:0000250"
FT DISULFID 297..314
FT /evidence="ECO:0000250"
FT DISULFID 319..330
FT /evidence="ECO:0000250"
FT DISULFID 326..339
FT /evidence="ECO:0000250"
FT DISULFID 341..353
FT /evidence="ECO:0000250"
FT DISULFID 359..369
FT /evidence="ECO:0000250"
FT DISULFID 365..378
FT /evidence="ECO:0000250"
FT DISULFID 380..393
FT /evidence="ECO:0000250"
FT DISULFID 667..682
FT /evidence="ECO:0000250"
FT DISULFID 678..697
FT /evidence="ECO:0000250"
FT DISULFID 699..712
FT /evidence="ECO:0000250"
FT CONFLICT 23
FT /note="A -> V (in Ref. 1; CAA79581)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="C -> G (in Ref. 1; CAA79581)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="E -> K (in Ref. 1; CAA79581)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="Q -> P (in Ref. 1; CAA79581)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="N -> K (in Ref. 1; CAA79581)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="D -> H (in Ref. 1; CAA79581)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..187
FT /note="GR -> AE (in Ref. 1; CAA79581)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="N -> NIT (in Ref. 1; CAA79581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 862 AA; 94947 MW; 43E7D6A293BE609C CRC64;
MSTADLMRRW VIALLLAAAG VAAEDSCSRN EFQCRDGKCI ASKWVCDGSP ECPDGSDESP
ETCMSVTCQS NQFSCGGRVS RCIPDSWRCD GQVDCENDSD EQGCPPKTCS QDDFRCQDGK
CISPQFVCDG DRDCLDGSDE AHCQATTCGP AHFRCNSSIC IPSLWACDGD VDCVDGSDEW
PQNCQGRDTA SKGVSSPCSS LEFHCGSSEC IHRSWVCDGE ADCKDKSDEE HCAVATCRPD
EFQCADGSCI HGSRQCDREH DCKDMSDELG CVNVTQCDGP NKFKCHSGEC ISLDKVCDSA
RDCQDWSDEP IKECKTNECL DNNGGCSHIC KDLKIGSECL CPSGFRLVDL HRCEDIDECQ
EPDTCSQLCV NLEGSYKCEC QAGFHMDPHT RVCKAVGSIG YLLFTNRHEV RKMTLDRSEY
TSLLPNLKNV VALDTEVTNN RIYWSDLSQK KIYSALMDQA PNLSYDTIIS EDLHAPDGLA
VDWIHRNIYW TDSVPGSVSV ADTKGVKRRT LFQEAGSRPR AIVVDPVHGF MYWTDWGTPA
KIKKGGLNGV DIHSLVTENI QWPNGITLDL SSGRLYWVDS KLHSISSIDV NGGNRKTILE
DENRLAHPFS LAIYEDKVYW TDVINEAIFS ANRLTGSDVN LVAENLLSPE DIVLFHKVTQ
PRGVNWCETT ALLPNGGCQY LCLPAPQIGP HSPKFTCACP DGMLLAKDMR SCLTEVDTVL
TTQGTSAVRP VVTASATRPP KHSEDLSAPS TPRQPVDTPG LSTVASVTVS HQVQGDMAGR
GNEEQPHGMR FLSIFFPIAL VALLVLGAVL LWRNWRLKNI NSINFDNPVY QKTTEDELHI
CRSQDGYTYP SRQMVSLEDD VA
