LRP2_PIG
ID LRP2_PIG Reviewed; 4652 AA.
AC C0HL13;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Low-density lipoprotein receptor-related protein 2 {ECO:0000303|PubMed:9228033};
DE Short=LRP-2 {ECO:0000303|PubMed:9228033};
DE AltName: Full=Glycoprotein 330 {ECO:0000250|UniProtKB:P98158};
DE Short=gp330 {ECO:0000250|UniProtKB:P98158};
DE AltName: Full=Megalin {ECO:0000303|PubMed:9228033};
DE Flags: Precursor;
GN Name=LRP2 {ECO:0000250|UniProtKB:P98164};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH BETA-AMYLOID PEPTIDE 40 IN COMPLEX WITH CLU.
RX PubMed=9228033; DOI=10.1074/jbc.272.30.18644;
RA Hammad S.M., Ranganathan S., Loukinova E., Twal W.O., Argraves W.S.;
RT "Interaction of apolipoprotein J-amyloid beta-peptide complex with low
RT density lipoprotein receptor-related protein-2/megalin. A mechanism to
RT prevent pathological accumulation of amyloid beta-peptide.";
RL J. Biol. Chem. 272:18644-18649(1997).
RN [3] {ECO:0000305}
RP INTERACTION WITH SHH.
RX PubMed=11964399; DOI=10.1074/jbc.m201933200;
RA McCarthy R.A., Barth J.L., Chintalapudi M.R., Knaak C., Argraves W.S.;
RT "Megalin functions as an endocytic sonic hedgehog receptor.";
RL J. Biol. Chem. 277:25660-25667(2002).
CC -!- FUNCTION: Multiligand endocytic receptor (By similarity). Acts together
CC with CUBN to mediate endocytosis of high-density lipoproteins (By
CC similarity). Mediates receptor-mediated uptake of polybasic drugs such
CC as aprotinin, aminoglycosides and polymyxin B (By similarity). In the
CC kidney, mediates the tubular uptake and clearance of leptin (By
CC similarity). Also mediates transport of leptin across the blood-brain
CC barrier through endocytosis at the choroid plexus epithelium (By
CC similarity). Endocytosis of leptin in neuronal cells is required for
CC hypothalamic leptin signaling and leptin-mediated regulation of feeding
CC and body weight (By similarity). Mediates endocytosis and subsequent
CC lysosomal degradation of CST3 in kidney proximal tubule cells (By
CC similarity). Mediates renal uptake of 25-hydroxyvitamin D3 in complex
CC with the vitamin D3 transporter GC/DBP (By similarity). Mediates renal
CC uptake of metallothionein-bound heavy metals (By similarity). Together
CC with CUBN, mediates renal reabsorption of myoglobin (By similarity).
CC Mediates renal uptake and subsequent lysosomal degradation of APOM (By
CC similarity). Plays a role in kidney selenium homeostasis by mediating
CC renal endocytosis of selenoprotein SEPP1 (By similarity). Mediates
CC renal uptake of the antiapoptotic protein BIRC5/survivin which may be
CC important for functional integrity of the kidney (By similarity).
CC Mediates renal uptake of matrix metalloproteinase MMP2 in complex with
CC metalloproteinase inhibitor TIMP1 (By similarity). Mediates endocytosis
CC of Sonic hedgehog protein N-product (ShhN), the active product of SHH
CC (By similarity). Also mediates ShhN transcytosis (By similarity). In
CC the embryonic neuroepithelium, mediates endocytic uptake and
CC degradation of BMP4, is required for correct SHH localization in the
CC ventral neural tube and plays a role in patterning of the ventral
CC telencephalon (By similarity). Required at the onset of neurulation to
CC sequester SHH on the apical surface of neuroepithelial cells of the
CC rostral diencephalon ventral midline and to control PTCH1-dependent
CC uptake and intracellular trafficking of SHH (By similarity). During
CC neurulation, required in neuroepithelial cells for uptake of folate
CC bound to the folate receptor FOLR1 which is necessary for neural tube
CC closure (By similarity). In the adult brain, negatively regulates BMP
CC signaling in the subependymal zone which enables neurogenesis to
CC proceed (By similarity). In astrocytes, mediates endocytosis of ALB
CC which is required for the synthesis of the neurotrophic factor oleic
CC acid (By similarity). Involved in neurite branching (By similarity).
CC During optic nerve development, required for SHH-mediated migration and
CC proliferation of oligodendrocyte precursor cells (By similarity).
CC Mediates endocytic uptake and clearance of SHH in the retinal margin
CC which protects retinal progenitor cells from mitogenic stimuli and
CC keeps them quiescent (By similarity). Plays a role in reproductive
CC organ development by mediating uptake in reproductive tissues of
CC androgen and estrogen bound to the sex hormone binding protein SHBG (By
CC similarity). Mediates endocytosis of angiotensin-2 (By similarity).
CC Also mediates endocytosis of angiotensis 1-7 (By similarity). Binds to
CC the complex composed of beta-amyloid protein 40 and CLU/APOJ and
CC mediates its endocytosis and lysosomal degradation (PubMed:9228033).
CC Required for embryonic heart development (By similarity). Required for
CC normal hearing, possibly through interaction with estrogen in the inner
CC ear (By similarity). {ECO:0000250|UniProtKB:A2ARV4,
CC ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164,
CC ECO:0000269|PubMed:9228033}.
CC -!- SUBUNIT: Binds plasminogen, extracellular matrix components,
CC plasminogen activator-plasminogen activator inhibitor type I complex,
CC apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin,
CC CLU/clusterin and calcium (By similarity). Forms a multimeric complex
CC together with LRPAP1 (By similarity). Interacts (via PxLPxI/L motif)
CC with ANKRA2 (via ankyrin repeats) (By similarity). Interacts with
CC LRP2BP (By similarity). Interacts (via NPXY motif) with DAB2; the
CC interaction is not affected by tyrosine phosphorylation of the NPXY
CC motif (By similarity). Interacts with MB (By similarity). Interacts
CC with BMP4 (By similarity). Interacts with the Sonic hedgehog protein N-
CC product which is the active product of SHH (PubMed:11964399). Interacts
CC with CST3 in a calcium-dependent manner (By similarity). Interacts with
CC the vitamin-D binding protein GC/DBP (By similarity). Interacts with
CC sex hormone-binding protein SHBG (By similarity). Interacts with
CC angiotensin-2 (By similarity). Also interacts with angiotensin 1-7 (By
CC similarity). Interacts with APOM (By similarity). Interacts with
CC selenoprotein SEPP1 (By similarity). Interacts with LEP (By
CC similarity). Interacts with ALB (By similarity). Interacts with the
CC antiapoptotic protein BIRC5/survivin (By similarity). Interacts with
CC matrix metalloproteinase MMP2 in complex with metalloproteinase
CC inhibitor TIMP1 (By similarity). In neurons, forms a trimeric complex
CC with APP and APPB1/FE65 (By similarity). Interacts with LDLRAP1/ARH;
CC mediates trafficking of LRP2 to the endocytic recycling compartment (By
CC similarity). Does not interact with beta-amyloid protein 40 alone but
CC interacts with the complex composed of beta-amyloid protein 40 and
CC CLU/APOJ (PubMed:9228033). Interacts with MDK (By similarity).
CC {ECO:0000250|UniProtKB:A2ARV4, ECO:0000250|UniProtKB:P98158,
CC ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:11964399,
CC ECO:0000269|PubMed:9228033}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P98158}; Single-pass type I membrane protein
CC {ECO:0000255}. Endosome lumen {ECO:0000250|UniProtKB:P98158}. Membrane,
CC clathrin-coated pit {ECO:0000250|UniProtKB:A2ARV4}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, axon
CC {ECO:0000250|UniProtKB:A2ARV4}. Note=Localizes to brush border
CC membranes in the kidney. In the endolymphatic sac of the inner ear,
CC located in the lumen of endosomes as a soluble form.
CC {ECO:0000250|UniProtKB:P98158}.
CC -!- DOMAIN: Two overlapping PxLPxI/L motifs mediate interaction with
CC ankyrin repeats of ANKRA2. {ECO:0000250|UniProtKB:P98158}.
CC -!- DOMAIN: The cytoplasmic domain is required for sorting to the apical
CC cell membrane. {ECO:0000250|UniProtKB:P98158}.
CC -!- PTM: A fraction undergoes proteolytic cleavage of the extracellular
CC domain at the cell membrane to generate a cytoplasmic tail fragment.
CC This is internalized into the early endosome from where it trafficks in
CC an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment
CC (ERC). In the ERC, it is further cleaved by gamma-secretase to release
CC a fragment which translocates to the nucleus and mediates
CC transcriptional repression. {ECO:0000250|UniProtKB:P98158}.
CC -!- PTM: N-glycosylation is required for ligand binding.
CC {ECO:0000250|UniProtKB:A2ARV4}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; GL881906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9823.ENSSSCP00000016881; -.
DR eggNOG; KOG1215; Eukaryota.
DR OrthoDB; 1606at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0060982; P:coronary artery morphogenesis; ISS:UniProtKB.
DR GO; GO:1904447; P:folate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0030001; P:metal ion transport; ISS:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0140058; P:neuron projection arborization; ISS:UniProtKB.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:UniProtKB.
DR GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IDA:ARUK-UCL.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IGI:ARUK-UCL.
DR GO; GO:0003139; P:secondary heart field specification; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0060068; P:vagina development; ISS:UniProtKB.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:UniProtKB.
DR CDD; cd00112; LDLa; 35.
DR Gene3D; 2.120.10.30; -; 8.
DR Gene3D; 4.10.400.10; -; 35.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
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; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00057; Ldl_recept_a; 35.
DR Pfam; PF00058; Ldl_recept_b; 15.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 27.
DR SMART; SM00179; EGF_CA; 10.
DR SMART; SM00192; LDLa; 36.
DR SMART; SM00135; LY; 38.
DR SUPFAM; SSF57184; SSF57184; 2.
DR SUPFAM; SSF57424; SSF57424; 36.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS01209; LDLRA_1; 29.
DR PROSITE; PS50068; LDLRA_2; 36.
DR PROSITE; PS51120; LDLRB; 35.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cell projection; Coated pit; Disulfide bond;
KW EGF-like domain; Endocytosis; Endosome; Glycoprotein; Hearing; Membrane;
KW Metal-binding; Neurogenesis; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; SH3-binding; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..4652
FT /note="Low-density lipoprotein receptor-related protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441957"
FT TOPO_DOM 26..4422
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 4423..4443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4444..4652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 27..63
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 66..104
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 108..144
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 142..181
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 183..219
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 223..259
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 267..308
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 348..386
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 436..478
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 479..521
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 522..568
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 569..613
FT /note="LDL-receptor class B 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 753..795
FT /note="LDL-receptor class B 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 796..837
FT /note="LDL-receptor class B 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 838..881
FT /note="LDL-receptor class B 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 882..925
FT /note="LDL-receptor class B 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 1025..1061
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1066..1104
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1110..1146
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1150..1186
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1188..1225
FT /note="LDL-receptor class A 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1231..1269
FT /note="LDL-receptor class A 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1272..1308
FT /note="LDL-receptor class A 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1313..1351
FT /note="LDL-receptor class A 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REPEAT 1480..1522
FT /note="LDL-receptor class B 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1523..1565
FT /note="LDL-receptor class B 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1568..1611
FT /note="LDL-receptor class B 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1612..1654
FT /note="LDL-receptor class B 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1655..1696
FT /note="LDL-receptor class B 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1789..1831
FT /note="LDL-receptor class B 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1832..1881
FT /note="LDL-receptor class B 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1882..1929
FT /note="LDL-receptor class B 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1930..1971
FT /note="LDL-receptor class B 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1972..2012
FT /note="LDL-receptor class B 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2105..2154
FT /note="LDL-receptor class B 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2155..2199
FT /note="LDL-receptor class B 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2200..2243
FT /note="LDL-receptor class B 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2244..2287
FT /note="LDL-receptor class B 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2429..2475
FT /note="LDL-receptor class B 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2476..2516
FT /note="LDL-receptor class B 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2517..2560
FT /note="LDL-receptor class B 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2561..2602
FT /note="LDL-receptor class B 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2603..2644
FT /note="LDL-receptor class B 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 2696..2734
FT /note="LDL-receptor class A 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2737..2773
FT /note="LDL-receptor class A 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2776..2815
FT /note="LDL-receptor class A 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2818..2857
FT /note="LDL-receptor class A 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2860..2897
FT /note="LDL-receptor class A 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2902..2941
FT /note="LDL-receptor class A 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2944..2986
FT /note="LDL-receptor class A 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2989..3025
FT /note="LDL-receptor class A 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3028..3066
FT /note="LDL-receptor class A 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3071..3107
FT /note="LDL-receptor class A 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3149..3189
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 3236..3278
FT /note="LDL-receptor class B 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3279..3321
FT /note="LDL-receptor class B 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3330..3373
FT /note="LDL-receptor class B 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3374..3417
FT /note="LDL-receptor class B 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3418..3458
FT /note="LDL-receptor class B 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 3509..3547
FT /note="LDL-receptor class A 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3550..3588
FT /note="LDL-receptor class A 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3591..3629
FT /note="LDL-receptor class A 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3632..3670
FT /note="LDL-receptor class A 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3675..3713
FT /note="LDL-receptor class A 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3716..3753
FT /note="LDL-receptor class A 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3756..3792
FT /note="LDL-receptor class A 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3795..3831
FT /note="LDL-receptor class A 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3839..3877
FT /note="LDL-receptor class A 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3880..3919
FT /note="LDL-receptor class A 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3925..3961
FT /note="LDL-receptor class A 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3964..4004
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4005..4046
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 4152..4194
FT /note="LDL-receptor class B 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 4195..4238
FT /note="LDL-receptor class B 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 4240..4281
FT /note="LDL-receptor class B 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 4375..4409
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4534..4652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4588..4601
FT /note="Interaction with DAB2"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT MOTIF 4450..4459
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 4453..4458
FT /note="PxLPxI/L motif 1; mediates interaction with ANKRA2"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT MOTIF 4456..4461
FT /note="PxLPxI/L motif 2; mediates interaction with ANKRA2"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT MOTIF 4518..4523
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT MOTIF 4594..4597
FT /note="NPXY motif"
FT /evidence="ECO:0000255"
FT MOTIF 4597..4600
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 4610..4621
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 4534..4552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4568..4597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4621..4640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT BINDING 1210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT BINDING 1212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT BINDING 1214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT BINDING 1220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT BINDING 1221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT MOD_RES 4460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ARV4"
FT MOD_RES 4568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ARV4"
FT MOD_RES 4615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98158"
FT MOD_RES 4629
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2ARV4"
FT MOD_RES 4650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ARV4"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2984
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 4066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 4325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 28..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 35..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 47..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 67..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 74..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 87..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 109..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 116..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 128..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 143..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 153..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 165..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 184..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 191..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 203..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 224..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 231..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 243..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 268..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 275..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 288..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 352..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 358..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 373..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1026..1038
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1033..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1045..1060
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1067..1081
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1074..1094
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1088..1103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1111..1123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1118..1136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1130..1145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1151..1163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1158..1176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1170..1185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1189..1202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1196..1215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1209..1224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1232..1245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1239..1258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1252..1268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1273..1285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1280..1298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1292..1307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1314..1327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1321..1340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1334..1350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2697..2709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2704..2722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2716..2733
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2738..2750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2745..2763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2757..2772
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2777..2790
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2785..2803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2797..2814
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2819..2832
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2826..2845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2839..2856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2861..2873
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2868..2886
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2880..2896
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2903..2915
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2910..2928
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2922..2940
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2945..2962
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2952..2975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2969..2985
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2990..3002
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2997..3015
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3009..3024
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3029..3041
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3036..3054
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3048..3065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3072..3084
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3079..3097
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3091..3106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3153..3164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3160..3173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3175..3188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3510..3523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3517..3536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3530..3546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3551..3563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3558..3576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3570..3587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3592..3604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3599..3617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3611..3628
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3633..3645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3640..3658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3652..3669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3676..3690
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3684..3703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3697..3712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3717..3730
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3725..3743
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3737..3752
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3757..3769
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3764..3782
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3776..3791
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3796..3808
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3803..3821
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3815..3830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3840..3852
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3847..3865
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3859..3876
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3881..3894
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3889..3907
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3901..3918
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3926..3938
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3933..3951
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3945..3960
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3968..3977
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3973..3987
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3989..4003
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4009..4019
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4015..4028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4030..4045
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4379..4387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4381..4397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4399..4408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 4652 AA; 521302 MW; A512AC3DEDFC535C CRC64;
MERWAAAAAC TLLLAFAACL APASGRECLG NEFRCSNGHC ITESWRCDGT RDCLDGSDEI
GCPPSTCGST QFHCENEDVC IPLYWVCDGE EDCSNGADEH QRCPPGRTCS SHHFTCTNGE
CIPVEYRCDH STDCLDGTDE INCRYPVCQQ QTCHNGACYN TSQRCDGEID CRDASDELNC
TQRCLRNEFQ CGSGECIPRD YVCDHDPDCS DSSDEHSCSV YQPCKGNEFA CSNGFCINQN
WVCDGMADCL DNSDEDGCES SIIRTHECYP NEWACPEDGK CIPLSRVCDG IADCPRGGDE
NKQGRVCDVN MCPSLGCEYQ CHKSPSGGTC NCPPGFIVNK NNTRSCVDFN DCQIWGICDH
FCEDRIGHHQ CFCAEGYVLE HEQHCRANSS SGQAFVIFSN GRNLLLGDIQ GQSFEYLVRS
QNRGSPVGVD FHYRLSKVFW TDTMQNKVFS LDIDGLVIRE VLSVSIEDPE NLAVDWINNK
LYIVETNVNR IDLANLDGSH RITLITENLG RPRGIALDPT VGYLFFSDWQ SISGQPKIER
AYMDGSNRKD LVKIKLGWPG GITLDLVAKR VYWVDARFDY IETVTYDGTQ RKTVLQGGSN
IPHPFGITLF EDNLFFTDWT KFSVMKANKF TETNPRVYFR SSTRPFGVTV YHAIRQPSVR
NPCGNNNGGC EHICVLSHRT DNGGLGYRCK CKLGYIPGLD DYSCVATKQF LFFSTDVAVR
GIPLTPSNQK DVILPVTGSP SVFVGIDFDA KENAIFFSDT SKDMIFRQKI NGTGREIITA
NRVPSVESLS FDWISRNLYW TDASYRSVTV MRLADKSRRT IVQNLNNPRS IVVHPIAGYI
FFTDWFRPAK ILRAWSDGSH MLPIVNTTLG WPNGLAIDWG SSRLYWVDAF LDKIEHTTFD
GLDRRALNHL QQMTHPFGLT VFGEYVYFTD WRQRSIVRVR KTDGGEMTIL RNGVGNVMRV
KIFETSIQVG SNACNRPTNP NGDCSHFCFP VPNLQRVCGC PYGMRLASNR LNCVNDSSRE
PPMEQCGALS FPCNNGRCVP LHYRCDGVDD CHDNSDEVQC GAFNTSCAPS AFACGHGGGE
CIPSYWRCDN HNDCVDGSDE QNCSSQAQTS CRADYFTCDN HMCIPKNWLC DTDNDCGDGS
DEKRCDLGET CSPTQFHCPN HRCIDLAFVC DGDKDCADGS DESACVINCT DSQFKCVGSN
KCISNTYRCD GVSDCSDHSD EIDCPTRPPG MCRQDEFQCR EDGICIPDSW ECDGHPDCLT
GSDEHSGCPP RTCPXSRFLC ANGNCIFRDW LCDGDNDCRD MSDEKDCPTQ PFLCPSWQWQ
CPGHSICVNL SSVCDGISDC PHGTDESPLC NQESCLHSNG GCTHLCIQGP FGAQCECPLG
YRLANDSKTC EDIDECRIPG FCSQHCYNMR GSFRCWCDIE YSLEADQRTC KATASESLLL
VVANQNQLIA DNITKSMDHM RALIQDGSHI VAVDFDSVRG RIFWSDKTLG KIFSAFQNGT
DRKPVFNSGN IMTESIAVDW VGRNLYWADF ALETIEVSKL DGTLRTVLLS ENVTSPRGIV
LDPRVNDRVI FWTNWGSYPR IERASMDGEM RTVIVQQKIF WPNGLAIDYP TRLLYFADGN
LDHIHFCKYD GSNRKQVISS GEGSGHLFAI TIFEDSIYWT DRNSQDVRKA NKWHGGNESV
VLSASQPLGI VAVHPARQPT ARNPCTIARC SHLCLLSSER LYSCACPSGW SLSQDSMTCV
RDDDAFLIVV RRTTIFGISL NPEVNTDNAM VPISGMESGY DVEVDYSEQF LYYADYPGEI
YKVKTDGTNR TLFDPLTKVG STTTLALDWL SRNLYYTDSE ARSIKVLTLR GNVRYRKTLI
TNDGTTLGIG VPVSITVDPA KGKLYWSDLG IEGRVPAKIA CANMDGTSRK NLFTGHLENV
GFITLDIQEQ KLYWTVRSYI SIERGNVDGT DRMSLVNSLP RPRGIAVYGP YLYYADEQNQ
VIERVDKATG ANKVVVREGL PNLRALRIYR RRGSESSNGC SNNINACQQI CLPVPGGLFT
CACAVGFKLN PDNRTCSSHD SFIVVSMLTA IRGYSLDVSD HSEAMVPVEL EGQNTLHVDV
DVSSGFVYWA DFNRNVQTDN AIRRIKIDGS GFADIITDGI GKDGIRGIAV DWVAGNLYFI
NAFVSETLIE VLRINTTHRR VLLKTTEDVP RDIVVDPKNR YLFWSDIGQT PKIERSFLDC
TNRTVLVSEM VASPRGLALD HNSGYIYWVD DSLDLIARVS IHGGNSETIR FGSSYPTPYA
IAVFGNSIIW VDRDLKTIFQ ASKEPFKTDP PTVIRNNINW LRDVTVFDKQ AQPRSPAEVN
YNPCLQNNGG CTHFCFALPQ LRTPKCGCAF GVLQGDGRSC AISREDFLIY ALDNSVRSLH
FDPEDYNVPF TAISVEETAV AVDYDSIDNR IYFTQVLASG KGQISYISLN SRSHSPTVVI
SNLGSPDGIA FDWIGRRIYY SDYTNQTIQS MNMDGSRRTV VARVTKPRAI VLDPCQGYMY
WTDWSTNAQI ERATMAGNFR NSIVNRDLVW PNGLTLDYKE NLLYWADASL QKIERSSVTG
TGREVIVSRA NAPFGLTVYG QYIYWTDWLT QKIYRANKYD GSGQTAMTTA LPFLPNGIRA
VVNNQELCHN PCGRFNGGCS HVCAPGPNGP ECKCPHEGRW YLANNNKYCI VDDGKRCNST
QFTCLSGYCI LESLKCNDID ECGDSSDELE TLCAYHTCPP TSFTCANGRC IQRHFRCDHY
NDCGDNSDES GCRFRSCNIT TEFSCNNGKC LPLQLVCDGI DHCNDNNTSD EKNCAQHTCL
PDYIKCANSN VCIPRLFLCD GDNDCGDMSD ENPIYCVSPT CKNNEFQCTS GSCIPELWHC
DGERDCDDGS DEPATCVYSP STCSSDEFKC DNNRCIQMEW ICDGDNDCGD MSDEDGRHHC
ENHNCSSYAF HCVNSAPPSR RCIPLSWVCD GDADCSDAYD EHQNCTRRNC SGTEFRCSNG
LCIPNWFRCD RRNDCGDYSD ERNCKYPACD ENLFTCQNGI CTYKSYICDG ENDCGDNSDE
LEHLCHKEET TCPPHQFRCN NGNCIEMVKV CNHQADCSDN SDEERCGVNE CNDPLLSGCD
QNCTDTLTSF YCSCKPGYRL LPDKRTCVDI DECKETPSVC SQKCENLLGS YICKCAPGYT
REPDGRSCRQ NTNIEPYLIF SNRYYLRNLT IDGHIYSLIL QGLGNAVALD FDRVEERLYW
LDIENKVIER MFLNKTNREA VIKYNIPGTE SLAVDWVTRK LYWSDSYLNC LSVSDLNGRY
RRKLAEHCVD VNNTFCFDKP RGIALHPRYG YVYWADWTDR AYIGRVGMDG RNKSLIISSK
IKWPNGITID YTNDLLYWTD AHLGYIEYSD LEGSHRHTVY ETGTLSHPFA VTIFEDTIYW
TDWNTKTVEK GNKYNGSNRE VLVNTTHRPY DIHVYHPYRQ PFVSNPCGTN NGGCSHLCLI
KAGGNGFTCE CPDNFYTIQH GDTTQCLPMC SSTQFLCANN EMCIPIWWKC DGQKDCLDGS
DEPNTCPQRF CRLGQFQCSD GNCTSSNFIC NARQDCPDGS DEDAVLCEHH RCESNQWQCA
NKRCIPESWQ CDSLNDCGDN SDEDSSHCAR RTCLPGYFKC ANGHCIPQSW KCDVDNDCGD
YSDEPLQECM GPAYRCDNYT EFDCKTNYRC IPKWAVCNGF DDCRDNSDEQ NCESLTCKPS
GEFRCTNHHC IPLRWRCDGH NDCGDNSDEE NCVPRQCSES EFRCDDQTCI PSRWICDQNN
DCGDNSDERD CEVMTCHPGY FQCSSGHCIP DQMRCDGFAD CLDASDEATC PTRFPNGAYC
PATLFECKNH VCVQPSWKCD GDNDCGDGSD EELHLCLNIT CDLTNRFRCD NNRCIYRHEL
CNHEDDCGDG SDEKKENCLA PTPRPCTEGE FKCSNGHCIS QHLVCDDVDD CGDHFDETGC
NTGEERSCAE NLCEHNCTQL IGGGFICSCR PGFKASSLNR NSCEDINECE QFGVCPQNCH
NTKGSYECTC AEGFRSMSEH YGERCAAEGN PPLLLLPENV RVRKYNLSSE KFSDYLEDQE
RIQALDYDWD PEGTGLSVVY YTVLGHGSKF GAIKRAYIPN FESGSNNPVK EVNLGLKYIV
QPDGIAVDWV GRHIYWSDAK TQRIEVAELD GRYRKWLITT LLDQPAAIVV NPKQGLMYWT
DWGKNPKIEI AWMDGQHRKV LVQEDLGWPT GLSIDYVNSD RIYWSDLKED VIETIKHDGT
DRKVVVTAAM NPYSLDIFES QLYWISKDKG EIWVQDKFER DRKEKLLIVN PWLTQVRIFH
QRRYNQSVPN RCKKVCSHLC LLKPEGYTCA CPQGSRFIAG SVTECDAAIE SPVTMPPPCR
CMNEGNCYFD KNNLPKCKCP SGYMGEYCEI GLSKGISPGT TVAVLVTLIL IIIIGGLVAL
GFFHYRKTGS ILISMPRLPS LSNLSKYTEN GNGVTFRSGE DVNMDIGVSG FGPESAIDRS
MAMSEHFAMD LEKPPIIFEN PMYTSKDGTI RMAQPTTTQV SESGNVYNKN YGSPVNPDEL
APDTKPASPS ADETQVTKWN IFKRKPKQNT NFENPIYAET ENEPKVGAAV TPPPSPSPPA
KKTQKKGTTP AYSATEDTFK DTANLVREDS EA
