GenomeNet

Database: UniProt
Entry: C0HL13
LinkDB: C0HL13
Original site: C0HL13 
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   10-APR-2019, entry version 7.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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
RP   CLU.
RX   PubMed=9228033;
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
CC       together with CUBN to mediate endocytosis of high-density
CC       lipoproteins (By similarity). Mediates receptor-mediated uptake of
CC       polybasic drugs such as aprotinin, aminoglycosides and polymyxin B
CC       (By similarity). In the kidney, mediates the tubular uptake and
CC       clearance of leptin (By similarity). Also mediates transport of
CC       leptin across the blood-brain barrier through endocytosis at the
CC       choroid plexus epithelium (By similarity). Endocytosis of leptin
CC       in neuronal cells is required for hypothalamic leptin signaling
CC       and leptin-mediated regulation of feeding and body weight (By
CC       similarity). Mediates endocytosis and subsequent lysosomal
CC       degradation of CST3 in kidney proximal tubule cells (By
CC       similarity). Mediates renal uptake of 25-hydroxyvitamin D3 in
CC       complex with the vitamin D3 transporter GC/DBP (By similarity).
CC       Mediates renal uptake of metallothionein-bound heavy metals (By
CC       similarity). Together with CUBN, mediates renal reabsorption of
CC       myoglobin (By similarity). Mediates renal uptake and subsequent
CC       lysosomal degradation of APOM (By similarity). Plays a role in
CC       kidney selenium homeostasis by mediating renal endocytosis of
CC       selenoprotein SEPP1 (By similarity). Mediates renal uptake of the
CC       antiapoptotic protein BIRC5/survivin which may be important for
CC       functional integrity of the kidney (By similarity). Mediates renal
CC       uptake of matrix metalloproteinase MMP2 in complex with
CC       metalloproteinase inhibitor TIMP1 (By similarity). Mediates
CC       endocytosis of Sonic hedgehog protein N-product (ShhN), the active
CC       product of SHH (By similarity). Also mediates ShhN transcytosis
CC       (By similarity). In the embryonic neuroepithelium, mediates
CC       endocytic uptake and degradation of BMP4, is required for correct
CC       SHH localization in the ventral neural tube and plays a role in
CC       patterning of the ventral telencephalon (By similarity). Required
CC       at the onset of neurulation to sequester SHH on the apical surface
CC       of neuroepithelial cells of the rostral diencephalon ventral
CC       midline and to control PTCH1-dependent uptake and intracellular
CC       trafficking of SHH (By similarity). During neurulation, required
CC       in neuroepithelial cells for uptake of folate bound to the folate
CC       receptor FOLR1 which is necessary for neural tube closure (By
CC       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
CC       ALB which is required for the synthesis of the neurotrophic factor
CC       oleic acid (By similarity). Involved in neurite branching (By
CC       similarity). During optic nerve development, required for SHH-
CC       mediated migration and proliferation of oligodendrocyte precursor
CC       cells (By similarity). Mediates endocytic uptake and clearance of
CC       SHH in the retinal margin which protects retinal progenitor cells
CC       from mitogenic stimuli and keeps them quiescent (By similarity).
CC       Plays a role in reproductive organ development by mediating uptake
CC       in reproductive tissues of androgen and estrogen bound to the sex
CC       hormone binding protein SHBG (By similarity). Mediates endocytosis
CC       of angiotensin-2 (By similarity). Also mediates endocytosis of
CC       angiotensis 1-7 (By similarity). Binds to the complex composed of
CC       beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis
CC       and lysosomal degradation (PubMed:9228033). Required for embryonic
CC       heart development (By similarity). Required for normal hearing,
CC       possibly through interaction with estrogen in the inner ear (By
CC       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
CC       complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase,
CC       lactoferrin, CLU/clusterin and calcium (By similarity). Forms a
CC       multimeric complex together with LRPAP1 (By similarity). Interacts
CC       (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats) (By
CC       similarity). Interacts with LRP2BP (By similarity). Interacts (via
CC       NPXY motif) with DAB2; the interaction is not affected by tyrosine
CC       phosphorylation of the NPXY motif (By similarity). Interacts with
CC       MB (By similarity). Interacts with BMP4 (By similarity). Interacts
CC       with the Sonic hedgehog protein N-product which is the active
CC       product of SHH (PubMed:11964399). Interacts with CST3 in a
CC       calcium-dependent manner (By similarity). Interacts with the
CC       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
CC       (By similarity). Interacts with APOM (By similarity). Interacts
CC       with selenoprotein SEPP1 (By similarity). Interacts with LEP (By
CC       similarity). Interacts with ALB (By similarity). Interacts with
CC       the antiapoptotic protein BIRC5/survivin (By similarity).
CC       Interacts with matrix metalloproteinase MMP2 in complex with
CC       metalloproteinase inhibitor TIMP1 (By similarity). In neurons,
CC       forms a trimeric complex with APP and APPB1/FE65 (By similarity).
CC       Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the
CC       endocytic recycling compartment (By similarity). Does not interact
CC       with beta-amyloid protein 40 alone but interacts with the complex
CC       composed of beta-amyloid protein 40 and CLU/APOJ (PubMed:9228033).
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
CC       protein {ECO:0000255}. Endosome lumen
CC       {ECO:0000250|UniProtKB:P98158}. Membrane, clathrin-coated pit
CC       {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, dendrite
CC       {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
CC       ear, 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
CC       apical cell membrane. {ECO:0000250|UniProtKB:P98158}.
CC   -!- PTM: A fraction undergoes proteolytic cleavage of the
CC       extracellular domain at the cell membrane to generate a
CC       cytoplasmic tail fragment. This is internalized into the early
CC       endosome from where it trafficks in an LDLRAP1/ARH-dependent
CC       manner to the endocytic recycling compartment (ERC). In the ERC,
CC       it is further cleaved by gamma-secretase to release a fragment
CC       which translocates to the nucleus and mediates transcriptional
CC       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}.
DR   EMBL; GL881906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   UniGene; Ssc.4289; -.
DR   STRING; 9823.ENSSSCP00000016881; -.
DR   Proteomes; UP000008227; 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:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
DR   GO; GO:0008144; F:drug binding; ISS:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0035258; F:steroid hormone receptor binding; ISS:UniProtKB.
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   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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;
KW   Complete proteome; Disulfide bond; EGF-like domain; Endocytosis;
KW   Endosome; Glycoprotein; Hearing; Membrane; Metal-binding;
KW   Neurogenesis; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   SH3-binding; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26   4652       Low-density lipoprotein receptor-related
FT                                protein 2. {ECO:0000255}.
FT                                /FTId=PRO_0000441957.
FT   TOPO_DOM     26   4422       Extracellular. {ECO:0000305}.
FT   TRANSMEM   4423   4443       Helical. {ECO:0000255}.
FT   TOPO_DOM   4444   4652       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN       27     63       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       66    104       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      108    144       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      142    181       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      183    219       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      223    259       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      267    308       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      348    386       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT      436    478       LDL-receptor class B 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      479    521       LDL-receptor class B 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      522    568       LDL-receptor class B 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      569    613       LDL-receptor class B 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      753    795       LDL-receptor class B 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      796    837       LDL-receptor class B 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      838    881       LDL-receptor class B 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      882    925       LDL-receptor class B 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   DOMAIN     1025   1061       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1066   1104       LDL-receptor class A 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1110   1146       LDL-receptor class A 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1150   1186       LDL-receptor class A 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1188   1225       LDL-receptor class A 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1231   1269       LDL-receptor class A 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1272   1308       LDL-receptor class A 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1313   1351       LDL-receptor class A 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   REPEAT     1480   1522       LDL-receptor class B 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1523   1565       LDL-receptor class B 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1568   1611       LDL-receptor class B 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1612   1654       LDL-receptor class B 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1655   1696       LDL-receptor class B 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1789   1831       LDL-receptor class B 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1832   1881       LDL-receptor class B 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1882   1929       LDL-receptor class B 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1930   1971       LDL-receptor class B 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1972   2012       LDL-receptor class B 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2105   2154       LDL-receptor class B 19.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2155   2199       LDL-receptor class B 20.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2200   2243       LDL-receptor class B 21.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2244   2287       LDL-receptor class B 22.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2429   2475       LDL-receptor class B 23.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2476   2516       LDL-receptor class B 24.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2517   2560       LDL-receptor class B 25.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2561   2602       LDL-receptor class B 26.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2603   2644       LDL-receptor class B 27.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   DOMAIN     2696   2734       LDL-receptor class A 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2737   2773       LDL-receptor class A 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2776   2815       LDL-receptor class A 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2818   2857       LDL-receptor class A 19.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2860   2897       LDL-receptor class A 20.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2902   2941       LDL-receptor class A 21.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2944   2986       LDL-receptor class A 22.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2989   3025       LDL-receptor class A 23.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3028   3066       LDL-receptor class A 24.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3071   3107       LDL-receptor class A 25.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3149   3189       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT     3236   3278       LDL-receptor class B 28.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     3279   3321       LDL-receptor class B 29.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     3330   3373       LDL-receptor class B 30.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     3374   3417       LDL-receptor class B 31.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     3418   3458       LDL-receptor class B 32.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   DOMAIN     3509   3547       LDL-receptor class A 26.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3550   3588       LDL-receptor class A 27.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3591   3629       LDL-receptor class A 28.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3632   3670       LDL-receptor class A 29.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3675   3713       LDL-receptor class A 30.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3716   3753       LDL-receptor class A 31.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3756   3792       LDL-receptor class A 32.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3795   3831       LDL-receptor class A 33.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3839   3877       LDL-receptor class A 34.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3880   3919       LDL-receptor class A 35.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3925   3961       LDL-receptor class A 36.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3964   4004       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4005   4046       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT     4152   4194       LDL-receptor class B 33.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     4195   4238       LDL-receptor class B 34.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     4240   4281       LDL-receptor class B 35.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   DOMAIN     4375   4409       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION     4588   4601       Interaction with DAB2.
FT                                {ECO:0000250|UniProtKB:P98164}.
FT   MOTIF      4450   4459       SH3-binding. {ECO:0000255}.
FT   MOTIF      4453   4458       PxLPxI/L motif 1; mediates interaction
FT                                with ANKRA2.
FT                                {ECO:0000250|UniProtKB:P98158}.
FT   MOTIF      4456   4461       PxLPxI/L motif 2; mediates interaction
FT                                with ANKRA2.
FT                                {ECO:0000250|UniProtKB:P98158}.
FT   MOTIF      4518   4523       Endocytosis signal. {ECO:0000255}.
FT   MOTIF      4594   4597       NPXY motif. {ECO:0000255}.
FT   MOTIF      4597   4600       SH2-binding. {ECO:0000255}.
FT   MOTIF      4610   4621       SH3-binding. {ECO:0000255}.
FT   METAL      1128   1128       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1131   1131       Calcium. {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1133   1133       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1135   1135       Calcium. {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1141   1141       Calcium. {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1142   1142       Calcium. {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1207   1207       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P98158}.
FT   METAL      1210   1210       Calcium. {ECO:0000250|UniProtKB:P98158}.
FT   METAL      1212   1212       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P98158}.
FT   METAL      1214   1214       Calcium. {ECO:0000250|UniProtKB:P98158}.
FT   METAL      1220   1220       Calcium. {ECO:0000250|UniProtKB:P98158}.
FT   METAL      1221   1221       Calcium. {ECO:0000250|UniProtKB:P98158}.
FT   MOD_RES    4460   4460       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2ARV4}.
FT   MOD_RES    4568   4568       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2ARV4}.
FT   MOD_RES    4615   4615       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P98158}.
FT   MOD_RES    4629   4629       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:A2ARV4}.
FT   MOD_RES    4650   4650       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2ARV4}.
FT   CARBOHYD    160    160       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    179    179       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    341    341       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    388    388       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    771    771       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    866    866       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1015   1015       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1064   1064       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1102   1102       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1188   1188       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1329   1329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1385   1385       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1452   1452       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1498   1498       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1552   1552       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1677   1677       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1809   1809       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2053   2053       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2175   2175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2222   2222       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2485   2485       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2698   2698       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2778   2778       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2806   2806       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2807   2807       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2944   2944       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2984   2984       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2989   2989       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3122   3122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3208   3208       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3254   3254       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3312   3312       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3352   3352       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3435   3435       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3444   3444       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3562   3562       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3678   3678       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3878   3878       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   3976   3976       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   4066   4066       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   4325   4325       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID     28     40       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     35     53       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     47     62       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     67     80       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     74     93       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     87    103       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    109    121       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    116    134       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    128    143       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    143    158       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    153    171       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    165    180       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    184    196       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    191    209       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    203    218       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    224    236       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    231    249       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    243    258       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    268    281       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    275    294       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    288    307       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    352    362       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    358    371       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    373    385       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1026   1038       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1033   1051       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1045   1060       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1067   1081       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1074   1094       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1088   1103       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1111   1123       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1118   1136       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1130   1145       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1151   1163       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1158   1176       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1170   1185       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1189   1202       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1196   1215       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1209   1224       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1232   1245       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1239   1258       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1252   1268       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1273   1285       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1280   1298       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1292   1307       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1314   1327       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1321   1340       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1334   1350       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2697   2709       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2704   2722       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2716   2733       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2738   2750       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2745   2763       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2757   2772       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2777   2790       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2785   2803       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2797   2814       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2819   2832       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2826   2845       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2839   2856       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2861   2873       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2868   2886       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2880   2896       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2903   2915       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2910   2928       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2922   2940       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2945   2962       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2952   2975       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2969   2985       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2990   3002       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2997   3015       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3009   3024       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3029   3041       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3036   3054       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3048   3065       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3072   3084       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3079   3097       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3091   3106       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3153   3164       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3160   3173       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3175   3188       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3510   3523       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3517   3536       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3530   3546       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3551   3563       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3558   3576       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3570   3587       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3592   3604       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3599   3617       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3611   3628       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3633   3645       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3640   3658       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3652   3669       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3676   3690       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3684   3703       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3697   3712       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3717   3730       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3725   3743       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3737   3752       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3757   3769       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3764   3782       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3776   3791       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3796   3808       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3803   3821       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3815   3830       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3840   3852       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3847   3865       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3859   3876       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3881   3894       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3889   3907       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3901   3918       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3926   3938       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3933   3951       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3945   3960       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3968   3977       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3973   3987       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3989   4003       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4009   4019       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4015   4028       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4030   4045       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4379   4387       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4381   4397       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4399   4408       {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
//
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