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Low-density lipoprotein receptor-related protein 5 (LRP-5) (Low-density lipoprotein receptor-related protein 7) (LRP-7) (Lr3)

 LRP5_MOUSE              Reviewed;        1614 AA.
Q91VN0; E9QQ75; O88883; Q9R208;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
07-NOV-2018, entry version 151.
RecName: Full=Low-density lipoprotein receptor-related protein 5 {ECO:0000303|PubMed:11956231};
Short=LRP-5;
AltName: Full=Low-density lipoprotein receptor-related protein 7 {ECO:0000303|PubMed:10049586};
Short=LRP-7;
Flags: Precursor;
Name=Lrp5 {ECO:0000303|PubMed:11956231, ECO:0000312|MGI:MGI:1278315};
Synonyms=Lr3 {ECO:0000303|PubMed:10049586},
Lrp7 {ECO:0000303|PubMed:10049586};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=9714764; DOI=10.1016/S0378-1119(98)00311-4;
Hey P.J., Twells R.C.J., Phillips M.S., Nakagawa Y., Brown S.D.,
Kawaguchi Y., Cox R., Xie G., Dugan V., Hammond H., Metzker M.L.,
Todd J.A., Hess J.F.;
"Cloning of a novel member of the low-density lipoprotein receptor
family.";
Gene 216:103-111(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND
TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10049586; DOI=10.1006/geno.1998.5688;
Chen D., Lathrop W., Dong Y.;
"Molecular cloning of mouse Lrp7(Lr3) cDNA and chromosomal mapping of
orthologous genes in mouse and human.";
Genomics 55:314-321(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DEVELOPMENTAL STAGE.
PubMed=11719191; DOI=10.1016/S0092-8674(01)00571-2;
Gong Y., Slee R.B., Fukai N., Rawadi G., Roman-Roman S.,
Reginato A.M., Wang H., Cundy T., Glorieux F.H., Lev D., Zacharin M.,
Oexle K., Marcelino J., Suwairi W., Heeger S., Sabatakos G., Apte S.,
Adkins W.N., Allgrove J., Arslan-Kirchner M., Batch J.A., Beighton P.,
Black G.C., Boles R.G., Boon L.M., Borrone C., Brunner H.G.,
Carle G.F., Dallapiccola B., De Paepe A., Floege B., Halfhide M.L.,
Hall B., Hennekam R.C.M., Hirose T., Jans A., Jueppner H., Kim C.A.,
Keppler-Noreuil K., Kohlschuetter A., LaCombe D., Lambert M.,
Lemyre E., Letteboer T., Peltonen L., Ramesar R.S., Romanengo M.,
Somer H., Steichen-Gersdorf E., Steinmann B., Sullivan B.,
Superti-Furga A., Swoboda W., van den Boogaard M.-J., Van Hul W.,
Vikkula M., Votruba M., Zabel B., Garcia T., Baron R., Olsen B.R.,
Warman M.L.;
"LDL receptor-related protein 5 (LRP5) affects bone accrual and eye
development.";
Cell 107:513-523(2001).
[6]
INTERACTION WITH MESD, OLIGOMERIZATION, AND SUBCELLULAR LOCATION.
PubMed=12581525; DOI=10.1016/S0092-8674(03)00045-X;
Hsieh J.-C., Lee L., Zhang L., Wefer S., Brown K., DeRossi C.,
Wines M.E., Rosenquist T., Holdener B.C.;
"Mesd encodes an LRP5/6 chaperone essential for specification of mouse
embryonic polarity.";
Cell 112:355-367(2003).
[7]
DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=15142971; DOI=10.1242/dev.01137;
Kelly O.G., Pinson K.I., Skarnes W.C.;
"The Wnt co-receptors Lrp5 and Lrp6 are essential for gastrulation in
mice.";
Development 131:2803-2815(2004).
[8]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11956231; DOI=10.1083/jcb.200201089;
Kato M., Patel M.S., Levasseur R., Lobov I., Chang B.H.,
Glass D.A. II, Hartmann C., Li L., Hwang T.H., Brayton C.F.,
Lang R.A., Karsenty G., Chan L.;
"Cbfa1-independent decrease in osteoblast proliferation, osteopenia,
and persistent embryonic eye vascularization in mice deficient in
Lrp5, a Wnt coreceptor.";
J. Cell Biol. 157:303-314(2002).
-!- FUNCTION: Acts as a coreceptor with members of the frizzled family
of seven-transmembrane spanning receptors to transduce signal by
Wnt proteins. Activates the canonical Wnt signaling pathway that
controls cell fate determination and self-renewal during embryonic
development and adult tissue regeneration (PubMed:11956231). In
particular, may play an important role in the development of the
posterior patterning of the epiblast during gastrulation
(PubMed:15142971). During bone development, regulates osteoblast
proliferation and differentiation thus determining bone mass
(PubMed:11956231). Mechanistically, the formation of the signaling
complex between Wnt ligand, frizzled receptor and LRP5 coreceptor
promotes the recruitment of AXIN1 to LRP5, stabilizing beta-
catenin/CTNNB1 and activating TCF/LEF-mediated transcriptional
programs (By similarity). Acts as a coreceptor for non-Wnt
proteins, such as norrin/NDP. Binding of norrin/NDP to frizzled
4/FZD4-LRP5 receptor complex triggers beta-catenin/CTNNB1-
dependent signaling known to be required for retinal vascular
development (By similarity). Plays a role in controlling postnatal
vascular regression in retina via macrophage-induced endothelial
cell apoptosis (PubMed:11956231). {ECO:0000250|UniProtKB:O75197,
ECO:0000269|PubMed:11956231, ECO:0000269|PubMed:15142971}.
-!- SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated
oligomer aggregates on Wnt-signaling (PubMed:12581525). Component
of a WNT-signaling complex that contains a WNT protein, a FZD
protein and LRP5 or LRP6. Interacts with FZD8; the interaction is
formed on WNT-binding and signaling. Interacts (via the
phosphorylated PPPSP motif domains) with AXIN1; the interaction
prevents inhibition of beta-catenin phosphorylation and signaling
and is enhanced in the presence of GSK3B and WNT1 or WNT3A.
Interacts (via beta-propeller regions 3 and 4) with DKK1; the
interaction, enhanced by MESD and/or KREMEN, inhibits beta-catenin
signaling by preventing GSK3-mediated phosphorylation of the PPPSP
motifs and subsequent, AXIN1 binding. Interacts with CSNK1E.
Interacts with SOST; the interaction antagonizes canonical Wnt
signaling. Interacts with APCDD1 (By similarity). Interacts with
MESD; the interaction prevents the formation of LRP5 aggregates,
targets LRP5 to the plasma membrane and, when complexed with
KREMEN2, increases DKK1 binding (PubMed:12581525). Interacts with
CAPRIN2 (By similarity). {ECO:0000250|UniProtKB:O75197,
ECO:0000269|PubMed:12581525}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12581525};
Single-pass type I membrane protein {ECO:0000269|PubMed:12581525}.
Endoplasmic reticulum {ECO:0000269|PubMed:12581525}.
Note=Chaperoned to the plasma membrane by MESD. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced.;
Name=1;
IsoId=Q91VN0-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Widely expressed, with the highest expression
levels in liver, heart, and lung and the lowest levels in brain
and spleen. {ECO:0000269|PubMed:10049586,
ECO:0000269|PubMed:11956231}.
-!- DEVELOPMENTAL STAGE: Expressed in early embryo throughout the
ectoderm at 6.5 dpc and in visceral endoderm overlying the
extraembryonic ectoderm at 7.5 dpc. Not present in the mesoderm
nor in endoderm emerging from the primitive streak
(PubMed:15142971). Expressed in differentiating osteoblasts that
contribute to the lateral membranous part of clavicle at embryonic
day 13.5. Expressed in osteoblasts lining the bony trabeculae of
the humerus at embryonic day 16.5. Expressed in osteoblasts on
both surfaces of the temporal bone at embryonic day 17.5
(PubMed:11719191). {ECO:0000269|PubMed:11719191,
ECO:0000269|PubMed:15142971}.
-!- PTM: Phosphorylation of cytoplasmic PPPSP motifs regulates the
signal transduction of the Wnt signaling pathway through acting as
a docking site for AXIN1. {ECO:0000250|UniProtKB:O75197}.
-!- DISRUPTION PHENOTYPE: Mice exhibit decreased osteoblast
proliferation, developing low bone mass postnatally. Also display
persistent embryonic eye vascularization due to a failure of
macrophage-induced endothelial cell apoptosis. Mutant animals
exhibit a loss of middle phalanx ossification at 18.5 dpc. LRP5
and LRP6 double null mutants are more severely affected. Embryos
arrest prior to mid-gestation. {ECO:0000269|PubMed:11956231,
ECO:0000269|PubMed:15142971}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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EMBL; AF064984; AAC36468.1; -; mRNA.
EMBL; AF077847; AAC70183.1; -; mRNA.
EMBL; AC112990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC117797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011374; AAH11374.1; -; mRNA.
CCDS; CCDS37881.1; -. [Q91VN0-1]
RefSeq; NP_032539.2; NM_008513.3. [Q91VN0-1]
UniGene; Mm.274581; -.
ProteinModelPortal; Q91VN0; -.
BioGrid; 201202; 8.
IntAct; Q91VN0; 2.
MINT; Q91VN0; -.
STRING; 10090.ENSMUSP00000025856; -.
iPTMnet; Q91VN0; -.
PhosphoSitePlus; Q91VN0; -.
EPD; Q91VN0; -.
MaxQB; Q91VN0; -.
PaxDb; Q91VN0; -.
PRIDE; Q91VN0; -.
Ensembl; ENSMUST00000025856; ENSMUSP00000025856; ENSMUSG00000024913. [Q91VN0-1]
GeneID; 16973; -.
KEGG; mmu:16973; -.
UCSC; uc008fwq.2; mouse. [Q91VN0-1]
CTD; 4041; -.
MGI; MGI:1278315; Lrp5.
eggNOG; ENOG410KD0T; Eukaryota.
eggNOG; ENOG4111JJ7; LUCA.
GeneTree; ENSGT00760000118968; -.
HOVERGEN; HBG049167; -.
InParanoid; Q91VN0; -.
KO; K03068; -.
OMA; PFTGISC; -.
OrthoDB; EOG091G0178; -.
TreeFam; TF315253; -.
Reactome; R-MMU-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination.
PRO; PR:Q91VN0; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024913; Expressed in 191 organ(s), highest expression level in retina.
ExpressionAtlas; Q91VN0; baseline and differential.
Genevisible; Q91VN0; MM.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0071936; F:coreceptor activity involved in Wnt signaling pathway; ISO:MGI.
GO; GO:0042813; F:Wnt-activated receptor activity; IDA:MGI.
GO; GO:0017147; F:Wnt-protein binding; IPI:MGI.
GO; GO:0060612; P:adipose tissue development; ISO:MGI.
GO; GO:0060033; P:anatomical structure regression; IMP:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IMP:MGI.
GO; GO:0060348; P:bone development; IMP:BHF-UCL.
GO; GO:0048539; P:bone marrow development; ISO:MGI.
GO; GO:0060349; P:bone morphogenesis; ISO:MGI.
GO; GO:0046849; P:bone remodeling; IMP:MGI.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0042074; P:cell migration involved in gastrulation; IGI:MGI.
GO; GO:0060764; P:cell-cell signaling involved in mammary gland development; IMP:MGI.
GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0035426; P:extracellular matrix-cell signaling; IDA:BHF-UCL.
GO; GO:0001702; P:gastrulation with mouth forming second; IGI:MGI.
GO; GO:0006007; P:glucose catabolic process; ISO:MGI.
GO; GO:0035108; P:limb morphogenesis; IGI:MGI.
GO; GO:0060603; P:mammary gland duct morphogenesis; IGI:MGI.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0002076; P:osteoblast development; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:MGI.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
GO; GO:0046850; P:regulation of bone remodeling; IMP:MGI.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISO:MGI.
GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0061304; P:retinal blood vessel morphogenesis; ISO:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
GO; GO:0001944; P:vasculature development; IMP:MGI.
GO; GO:0016055; P:Wnt signaling pathway; ISO:MGI.
CDD; cd00112; LDLa; 3.
Gene3D; 2.120.10.30; -; 4.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR017049; LRP5/6.
Pfam; PF00057; Ldl_recept_a; 3.
Pfam; PF00058; Ldl_recept_b; 14.
PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 1.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 4.
SMART; SM00192; LDLa; 3.
SMART; SM00135; LY; 20.
SUPFAM; SSF57424; SSF57424; 3.
PROSITE; PS01209; LDLRA_1; 3.
PROSITE; PS50068; LDLRA_2; 3.
PROSITE; PS51120; LDLRB; 20.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Developmental protein;
Disulfide bond; EGF-like domain; Endocytosis; Endoplasmic reticulum;
Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix;
Wnt signaling pathway.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1614 Low-density lipoprotein receptor-related
protein 5.
/FTId=PRO_0000017329.
TOPO_DOM 31 1383 Extracellular. {ECO:0000255}.
TRANSMEM 1384 1406 Helical. {ECO:0000255}.
TOPO_DOM 1407 1614 Cytoplasmic. {ECO:0000255}.
REPEAT 74 118 LDL-receptor class B 1.
REPEAT 119 161 LDL-receptor class B 2.
REPEAT 162 205 LDL-receptor class B 3.
REPEAT 206 246 LDL-receptor class B 4.
REPEAT 247 289 LDL-receptor class B 5.
DOMAIN 294 336 EGF-like 1.
REPEAT 384 426 LDL-receptor class B 6.
REPEAT 427 469 LDL-receptor class B 7.
REPEAT 470 513 LDL-receptor class B 8.
REPEAT 514 556 LDL-receptor class B 9.
REPEAT 557 599 LDL-receptor class B 10.
DOMAIN 600 640 EGF-like 2.
REPEAT 686 728 LDL-receptor class B 11.
REPEAT 729 771 LDL-receptor class B 12.
REPEAT 772 814 LDL-receptor class B 13.
REPEAT 815 854 LDL-receptor class B 14.
REPEAT 855 897 LDL-receptor class B 15.
DOMAIN 901 941 EGF-like 3.
REPEAT 988 1034 LDL-receptor class B 16.
REPEAT 1035 1077 LDL-receptor class B 17.
REPEAT 1078 1122 LDL-receptor class B 18.
REPEAT 1123 1164 LDL-receptor class B 19.
REPEAT 1165 1206 LDL-receptor class B 20.
DOMAIN 1212 1253 EGF-like 4.
DOMAIN 1257 1295 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1296 1332 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1334 1370 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
REGION 31 287 Beta-propeller 1.
REGION 340 601 Beta-propeller 2.
REGION 643 902 Beta-propeller 3.
REGION 944 1211 Beta-propeller 4.
MOTIF 1499 1505 PPPSP motif A.
MOTIF 1537 1544 PPPSP motif B.
MOTIF 1573 1580 PPPSP motif C.
MOTIF 1590 1595 PPPSP motif D.
MOTIF 1604 1611 PPPSP motif E.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 704 704 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 877 877 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 298 309 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 305 320 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 322 335 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 604 615 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 611 624 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 626 639 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 905 916 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 912 925 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 927 940 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1216 1227 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1223 1237 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1239 1252 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1258 1272 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1265 1285 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1279 1294 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1297 1309 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1304 1322 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1316 1331 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1335 1347 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1342 1360 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1354 1369 {ECO:0000255|PROSITE-ProRule:PRU00124}.
CONFLICT 220 220 R -> H (in Ref. 2; AAC70183).
{ECO:0000305}.
CONFLICT 1520 1520 I -> S (in Ref. 4; AAH11374).
{ECO:0000305}.
CONFLICT 1553 1553 T -> I (in Ref. 1; AAC36468 and 2;
AAC70183). {ECO:0000305}.
SEQUENCE 1614 AA; 178885 MW; 80FF4288470A4FC5 CRC64;
METAPTRAPP PPPPPLLLLV LYCSLVPAAA SPLLLFANRR DVRLVDAGGV KLESTIVASG
LEDAAAVDFQ FSKGAVYWTD VSEEAIKQTY LNQTGAAAQN IVISGLVSPD GLACDWVGKK
LYWTDSETNR IEVANLNGTS RKVLFWQDLD QPRAIALDPA HGYMYWTDWG EAPRIERAGM
DGSTRKIIVD SDIYWPNGLT IDLEEQKLYW ADAKLSFIHR ANLDGSFRQK VVEGSLTHPF
ALTLSGDTLY WTDWQTRSIH ACNKWTGEQR KEILSALYSP MDIQVLSQER QPPFHTPCEE
DNGGCSHLCL LSPREPFYSC ACPTGVQLQD NGKTCKTGAE EVLLLARRTD LRRISLDTPD
FTDIVLQVGD IRHAIAIDYD PLEGYVYWTD DEVRAIRRAY LDGSGAQTLV NTEINDPDGI
AVDWVARNLY WTDTGTDRIE VTRLNGTSRK ILVSEDLDEP RAIVLHPVMG LMYWTDWGEN
PKIECANLDG RDRHVLVNTS LGWPNGLALD LQEGKLYWGD AKTDKIEVIN IDGTKRKTLL
EDKLPHIFGF TLLGDFIYWT DWQRRSIERV HKVKASRDVI IDQLPDLMGL KAVNVAKVVG
TNPCADGNGG CSHLCFFTPR ATKCGCPIGL ELLSDMKTCI IPEAFLVFTS RATIHRISLE
TNNNDVAIPL TGVKEASALD FDVSNNHIYW TDVSLKTISR AFMNGSSVEH VIEFGLDYPE
GMAVDWMGKN LYWADTGTNR IEVARLDGQF RQVLVWRDLD NPRSLALDPT KGYIYWTEWG
GKPRIVRAFM DGTNCMTLVD KVGRANDLTI DYADQRLYWT DLDTNMIESS NMLGQERMVI
ADDLPYPFGL TQYSDYIYWT DWNLHSIERA DKTSGRNRTL IQGHLDFVMD ILVFHSSRQD
GLNDCVHSNG QCGQLCLAIP GGHRCGCASH YTLDPSSRNC SPPSTFLLFS QKFAISRMIP
DDQLSPDLVL PLHGLRNVKA INYDPLDKFI YWVDGRQNIK RAKDDGTQPS MLTSPSQSLS
PDRQPHDLSI DIYSRTLFWT CEATNTINVH RLDGDAMGVV LRGDRDKPRA IAVNAERGYM
YFTNMQDHAA KIERASLDGT EREVLFTTGL IRPVALVVDN ALGKLFWVDA DLKRIESCDL
SGANRLTLED ANIVQPVGLT VLGRHLYWID RQQQMIERVE KTTGDKRTRV QGRVTHLTGI
HAVEEVSLEE FSAHPCARDN GGCSHICIAK GDGTPRCSCP VHLVLLQNLL TCGEPPTCSP
DQFACTTGEI DCIPGAWRCD GFPECADQSD EEGCPVCSAS QFPCARGQCV DLRLRCDGEA
DCQDRSDEAN CDAVCLPNQF RCTSGQCVLI KQQCDSFPDC ADGSDELMCE INKPPSDDIP
AHSSAIGPVI GIILSLFVMG GVYFVCQRVM CQRYTGASGP FPHEYVGGAP HVPLNFIAPG
GSQHGPFPGI PCSKSVMSSM SLVGGRGSVP LYDRNHVTGA SSSSSSSTKA TLYPPILNPP
PSPATDPSLY NVDVFYSSGI PATARPYRPY VIRGMAPPTT PCSTDVCDSD YSTSRWKSSK
YYLDLNSDSD PYPPPPTPHS QYLSAEDSCP PSPGTERSYC HLFPPPPSPC TDSS


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