LRP10_HUMAN
ID LRP10_HUMAN Reviewed; 713 AA.
AC Q7Z4F1; A8K4R5; D3DS31; O95882; Q14CK7; Q86T02; Q8NCZ4; Q9HC42; Q9UG33;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Low-density lipoprotein receptor-related protein 10;
DE Short=LRP-10;
DE Flags: Precursor;
GN Name=LRP10; ORFNames=MSTP087, SP220, UNQ389/PRO724;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Cervix carcinoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 100-713 (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-713 (ISOFORM 1).
RC TISSUE=Aorta;
RA Lu H., Liu B.H., Qin B.M., Sheng H., Zhang Q., Liu Y.Q., Zhao B., Liu B.,
RA Wang X.Y., Song L., Ji X.J., Xu H.S., Chen J.Z., Zheng W.Y., Teng C.Y.,
RA Liu Q., Yu L.T., Lin J., Gong J., Gao R.L., Hui R.T.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 329-713 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-713 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11123907; DOI=10.1021/bi001583s;
RA Sugiyama T., Kumagai H., Morikawa Y., Wada Y., Sugiyama A., Yasuda K.,
RA Yokoi N., Tamura S., Kojima T., Nosaka T., Senba E., Kimura S.,
RA Kadowaki T., Kodama T., Kitamura T.;
RT "A novel low-density lipoprotein receptor-related protein mediating
RT cellular uptake of apolipoprotein E-enriched beta-VLDL in vitro.";
RL Biochemistry 39:15817-15825(2000).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-596, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Probable receptor, which is involved in the internalization
CC of lipophilic molecules and/or signal transduction. May be involved in
CC the uptake of lipoprotein APOE in liver (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q7Z4F1; Q92843: BCL2L2; NbExp=3; IntAct=EBI-2830349, EBI-707714;
CC Q7Z4F1; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-2830349, EBI-1045797;
CC Q7Z4F1; Q15125: EBP; NbExp=3; IntAct=EBI-2830349, EBI-3915253;
CC Q7Z4F1; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2830349, EBI-18304435;
CC Q7Z4F1; Q96LL3: FIMP; NbExp=3; IntAct=EBI-2830349, EBI-12887376;
CC Q7Z4F1; O95377: GJB5; NbExp=3; IntAct=EBI-2830349, EBI-3909454;
CC Q7Z4F1; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-2830349, EBI-3917143;
CC Q7Z4F1; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-2830349, EBI-373355;
CC Q7Z4F1; O14880: MGST3; NbExp=3; IntAct=EBI-2830349, EBI-724754;
CC Q7Z4F1; P30301: MIP; NbExp=3; IntAct=EBI-2830349, EBI-8449636;
CC Q7Z4F1; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-2830349, EBI-750085;
CC Q7Z4F1; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-2830349, EBI-17490746;
CC Q7Z4F1; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-2830349, EBI-16427978;
CC Q7Z4F1; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-2830349, EBI-949945;
CC Q7Z4F1; Q14973: SLC10A1; NbExp=3; IntAct=EBI-2830349, EBI-3923031;
CC Q7Z4F1; Q15849: SLC14A2; NbExp=3; IntAct=EBI-2830349, EBI-1573290;
CC Q7Z4F1; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-2830349, EBI-12188413;
CC Q7Z4F1; Q969X2: ST6GALNAC6; NbExp=3; IntAct=EBI-2830349, EBI-949146;
CC Q7Z4F1; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-2830349, EBI-11724423;
CC Q7Z4F1; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-2830349, EBI-10982110;
CC Q7Z4F1; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-2830349, EBI-12887458;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Membrane, coated pit {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z4F1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4F1-2; Sequence=VSP_009820;
CC -!- TISSUE SPECIFICITY: Expressed in blood leukocyte, lung, placenta, small
CC intestine, liver, kidney, spleen, thymus, colon, skeletal muscle and
CC heart. {ECO:0000269|PubMed:11123907}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20037.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG17980.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ13610.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD39174.2; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence={ECO:0000305};
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DR EMBL; AY358399; AAQ88765.1; -; mRNA.
DR EMBL; BX161500; CAD61944.1; -; mRNA.
DR EMBL; AK291030; BAF83719.1; -; mRNA.
DR EMBL; AL080164; CAB45753.1; -; mRNA.
DR EMBL; AL834518; CAD39174.2; ALT_SEQ; mRNA.
DR EMBL; CH471078; EAW66232.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66235.1; -; Genomic_DNA.
DR EMBL; BC064901; AAH64901.1; -; mRNA.
DR EMBL; BC113714; AAI13715.1; -; mRNA.
DR EMBL; BC113716; AAI13717.1; -; mRNA.
DR EMBL; AF172816; AAQ13610.1; ALT_FRAME; mRNA.
DR EMBL; AF177336; AAG17980.1; ALT_FRAME; mRNA.
DR EMBL; AF131760; AAD20037.1; ALT_INIT; mRNA.
DR CCDS; CCDS86372.1; -. [Q7Z4F1-2]
DR CCDS; CCDS9578.1; -. [Q7Z4F1-1]
DR PIR; T12469; T12469.
DR RefSeq; NP_001316155.1; NM_001329226.1. [Q7Z4F1-2]
DR RefSeq; NP_054764.2; NM_014045.4. [Q7Z4F1-1]
DR AlphaFoldDB; Q7Z4F1; -.
DR SMR; Q7Z4F1; -.
DR BioGRID; 117491; 133.
DR IntAct; Q7Z4F1; 59.
DR MINT; Q7Z4F1; -.
DR STRING; 9606.ENSP00000352601; -.
DR GlyConnect; 1465; 1 N-Linked glycan (1 site).
DR GlyGen; Q7Z4F1; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q7Z4F1; -.
DR PhosphoSitePlus; Q7Z4F1; -.
DR SwissPalm; Q7Z4F1; -.
DR BioMuta; LRP10; -.
DR DMDM; 46396347; -.
DR EPD; Q7Z4F1; -.
DR jPOST; Q7Z4F1; -.
DR MassIVE; Q7Z4F1; -.
DR MaxQB; Q7Z4F1; -.
DR PaxDb; Q7Z4F1; -.
DR PeptideAtlas; Q7Z4F1; -.
DR PRIDE; Q7Z4F1; -.
DR ProteomicsDB; 69172; -. [Q7Z4F1-1]
DR ProteomicsDB; 69173; -. [Q7Z4F1-2]
DR Antibodypedia; 95; 117 antibodies from 24 providers.
DR DNASU; 26020; -.
DR Ensembl; ENST00000359591.9; ENSP00000352601.4; ENSG00000197324.9. [Q7Z4F1-1]
DR Ensembl; ENST00000546834.5; ENSP00000447559.1; ENSG00000197324.9. [Q7Z4F1-2]
DR GeneID; 26020; -.
DR KEGG; hsa:26020; -.
DR MANE-Select; ENST00000359591.9; ENSP00000352601.4; NM_014045.5; NP_054764.2.
DR UCSC; uc001whd.4; human. [Q7Z4F1-1]
DR CTD; 26020; -.
DR DisGeNET; 26020; -.
DR GeneCards; LRP10; -.
DR HGNC; HGNC:14553; LRP10.
DR HPA; ENSG00000197324; Low tissue specificity.
DR MIM; 609921; gene.
DR neXtProt; NX_Q7Z4F1; -.
DR OpenTargets; ENSG00000197324; -.
DR PharmGKB; PA38383; -.
DR VEuPathDB; HostDB:ENSG00000197324; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000160783; -.
DR HOGENOM; CLU_013747_2_0_1; -.
DR InParanoid; Q7Z4F1; -.
DR OMA; DWLMCLP; -.
DR OrthoDB; 135036at2759; -.
DR PhylomeDB; Q7Z4F1; -.
DR TreeFam; TF332149; -.
DR PathwayCommons; Q7Z4F1; -.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; Q7Z4F1; -.
DR BioGRID-ORCS; 26020; 19 hits in 1081 CRISPR screens.
DR ChiTaRS; LRP10; human.
DR GeneWiki; LRP10; -.
DR GenomeRNAi; 26020; -.
DR Pharos; Q7Z4F1; Tbio.
DR PRO; PR:Q7Z4F1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q7Z4F1; protein.
DR Bgee; ENSG00000197324; Expressed in stromal cell of endometrium and 202 other tissues.
DR ExpressionAtlas; Q7Z4F1; baseline and differential.
DR Genevisible; Q7Z4F1; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IBA:GO_Central.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0006869; P:lipid transport; IEA:Ensembl.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 4.10.400.10; -; 4.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 4.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF57424; SSF57424; 2.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Disulfide bond; Endocytosis;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..713
FT /note="Low-density lipoprotein receptor-related protein 10"
FT /id="PRO_0000017335"
FT TOPO_DOM 17..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..136
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 139..175
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 192..305
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 307..354
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 355..397
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 398..434
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 564..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..57
FT /evidence="ECO:0000250"
FT DISULFID 80..98
FT /evidence="ECO:0000250"
FT DISULFID 140..152
FT /evidence="ECO:0000250"
FT DISULFID 147..165
FT /evidence="ECO:0000250"
FT DISULFID 159..174
FT /evidence="ECO:0000250"
FT DISULFID 192..220
FT /evidence="ECO:0000250"
FT DISULFID 308..331
FT /evidence="ECO:0000250"
FT DISULFID 315..344
FT /evidence="ECO:0000250"
FT DISULFID 338..353
FT /evidence="ECO:0000250"
FT DISULFID 356..374
FT /evidence="ECO:0000250"
FT DISULFID 363..387
FT /evidence="ECO:0000250"
FT DISULFID 381..396
FT /evidence="ECO:0000250"
FT DISULFID 399..411
FT /evidence="ECO:0000250"
FT DISULFID 406..424
FT /evidence="ECO:0000250"
FT DISULFID 418..433
FT /evidence="ECO:0000250"
FT VAR_SEQ 557..713
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009820"
FT VARIANT 48
FT /note="R -> W (in dbSNP:rs2273837)"
FT /id="VAR_018172"
FT VARIANT 139
FT /note="M -> V (in dbSNP:rs28534929)"
FT /id="VAR_034097"
FT CONFLICT 365
FT /note="A -> T (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="S -> C (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="R -> H (in Ref. 4; CAB45753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 76193 MW; A463FB5584322220 CRC64;
MLLATLLLLL LGGALAHPDR IIFPNHACED PPAVLLEVQG TLQRPLVRDS RTSPANCTWL
ILGSKEQTVT IRFQKLHLAC GSERLTLRSP LQPLISLCEA PPSPLQLPGG NVTITYSYAG
ARAPMGQGFL LSYSQDWLMC LQEEFQCLNH RCVSAVQRCD GVDACGDGSD EAGCSSDPFP
GLTPRPVPSL PCNVTLEDFY GVFSSPGYTH LASVSHPQSC HWLLDPHDGR RLAVRFTALD
LGFGDAVHVY DGPGPPESSR LLRSLTHFSN GKAVTVETLS GQAVVSYHTV AWSNGRGFNA
TYHVRGYCLP WDRPCGLGSG LGAGEGLGER CYSEAQRCDG SWDCADGTDE EDCPGCPPGH
FPCGAAGTSG ATACYLPADR CNYQTFCADG ADERRCRHCQ PGNFRCRDEK CVYETWVCDG
QPDCADGSDE WDCSYVLPRK VITAAVIGSL VCGLLLVIAL GCTCKLYAIR TQEYSIFAPL
SRMEAEIVQQ QAPPSYGQLI AQGAIPPVED FPTENPNDNS VLGNLRSLLQ ILRQDMTPGG
GPGARRRQRG RLMRRLVRRL RRWGLLPRTN TPARASEARS QVTPSAAPLE ALDGGTGPAR
EGGAVGGQDG EQAPPLPIKA PLPSASTSPA PTTVPEAPGP LPSLPLEPSL LSGVVQALRG
RLLPSLGPPG PTRSPPGPHT AVLALEDEDD VLLVPLAEPG VWVAEAEDEP LLT
