ID A0A8C4LGS3_EQUAS Unreviewed; 793 AA.
AC A0A8C4LGS3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Low-density lipoprotein receptor {ECO:0000256|ARBA:ARBA00039475};
GN Name=LDLR {ECO:0000313|Ensembl:ENSEASP00005008450.2};
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793 {ECO:0000313|Ensembl:ENSEASP00005008450.2, ECO:0000313|Proteomes:UP000694387};
RN [1] {ECO:0000313|Ensembl:ENSEASP00005008450.2, ECO:0000313|Proteomes:UP000694387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33293529;
RA Wang, C., Li, H., Guo, Y., Huang, J., Sun, Y., Min, J., Wang, J., Fang, X.,
RA Zhao, Z., Wang, S., Zhang, Y., Liu, Q., Jiang, Q., Wang, X., Guo, Y., Yang,
RA C., Wang, Y., Tian, F., Zhuang, G., Fan, Y., Gao, Q., Li, Y., Ju, Z., Li,
RA J., Li, R., Hou, M., Yang, G., Liu, G., Liu, W., Guo, J., Pan, S., Fan, G.,
RA Zhang, W., Zhang, R., Yu, J., Zhang, X., Yin, Q., Ji, C., Jin, Y., Yue, G.,
RA Liu, M., Xu, J., Liu, S., Jordana, J., Noce, A., Amills, M., Wu, D.D., Li,
RA S., Zhou, X. and Zhong, J.;
RT "Donkey genomes provide new insights into domestication and selection for
RT coat color.";
RL Nat. Commun. 11:6014-6014(2020).
RN [2] {ECO:0000313|Ensembl:ENSEASP00005008450.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSEASP00005008450.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Binds low density lipoprotein /LDL, the major cholesterol-
CC carrying lipoprotein of plasma, and transports it into cells by
CC endocytosis. In order to be internalized, the receptor-ligand complexes
CC must first cluster into clathrin-coated pits. Forms a ternary complex
CC with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL
CC internalization. {ECO:0000256|ARBA:ARBA00045488}.
CC -!- SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain); the
CC interaction is impaired by tyrosine phosphorylation of the NPXY motif.
CC Interacts (via NPXY motif) with LDLRAP1 (via PID domain). Interacts
CC with ARRB1. Interacts with SNX17. Interacts with the full-length
CC immature form of PCSK9 (via C-terminus). Interacts with PGRMC1 and
CC TMEM97; the interaction increases LDL internalization.
CC {ECO:0000256|ARBA:ARBA00046540}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Early endosome {ECO:0000256|ARBA:ARBA00004412}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Late endosome
CC {ECO:0000256|ARBA:ARBA00004603}. Lysosome
CC {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the LDLR family.
CC {ECO:0000256|ARBA:ARBA00009939}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A8C4LGS3; -.
DR Ensembl; ENSEAST00005009208.2; ENSEASP00005008450.2; ENSEASG00005005990.2.
DR GeneTree; ENSGT00940000161046; -.
DR Proteomes; UP000694387; Chromosome 20.
DR GO; GO:0016324; C:apical plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042562; F:hormone binding; IEA:TreeGrafter.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:TreeGrafter.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 5.
DR FunFam; 4.10.400.10:FF:000072; Low density lipoprotein receptor; 1.
DR FunFam; 4.10.400.10:FF:000084; Low density lipoprotein receptor; 1.
DR FunFam; 4.10.400.10:FF:000116; Low-density lipoprotein receptor; 1.
DR FunFam; 2.10.25.10:FF:000009; Low-density lipoprotein receptor isoform 1; 1.
DR FunFam; 2.10.25.10:FF:000052; low-density lipoprotein receptor isoform X1; 1.
DR FunFam; 2.120.10.30:FF:000002; low-density lipoprotein receptor isoform X1; 1.
DR FunFam; 4.10.400.10:FF:000113; Low-density lipoprotein receptor-related protein 8; 1.
DR FunFam; 4.10.400.10:FF:000006; Putative low-density lipoprotein receptor; 1.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_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; IPR051221; LDLR-related.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR049883; NOTCH1_EGF-like.
DR PANTHER; PTHR22722:SF15; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 2.
DR Pfam; PF00057; Ldl_recept_a; 5.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 5.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 5.
DR PROSITE; PS51120; LDLRB; 4.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000694387};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 720..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 291..330
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 376..422
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 423..465
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 466..509
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 513..557
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 45..57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 52..70
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 64..79
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 84..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 91..109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 134..146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 141..159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 153..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 173..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 180..198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 192..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 221..239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 295..305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 793 AA; 87577 MW; A06A00E18F74CBBA CRC64;
CEPWGLLTGW GLRWAGCPHL RRGRCWRLPG DAAVVSPCPA APKTCAQDEF RCLDGKCIAR
EFVCDADRDC LDGSDEASCP APTCGPASFQ CNSSTCIPEL WACDGDPDCK DGSDEWPQRC
GARDAAPPRD DSPCSALEFH CGSGECVHSS WRCDGDPDCR DKSDEDNCAV ATCQPDEFQC
SDGTCIHGSR QCDKEYDCKD MSDELGCVNV TLCEGPSKFK CRSGECIPLD KVCNSARDCQ
DWSDEPLRQC GTNECLDNNG GCSHICSDLK IGHECLCPEG FRLVDQRRCE DIDECQDPDA
CSQLCVNLEG GYKCECEAGF QLDPLTKACK ATGTIAYLFF TNRHEVRKMT LDRSEYTSLI
PNLKNVVALD TEVASNRVYW SDLSQRKIYS TQIDRAPSFS SYDTVIGEDL QAPDGLAVDW
IHGNIYWTDS VLGTVSVADT KGLKRKTLFK EKDSKPRAIV VDPVHGFMYW TDWGTPAKIK
KGGLNGVDIY SLVTEDIQWP NGITLGTFIF PVGRLYWVDS KLHSISSIDV NGGDRKTILE
DKKKLAHPFS LAVFEDKVFW TDIINEAIFS ANRLTGSDIH LMAENLLSPE DIVLFHNLTQ
PRGVNWCERT ALHNGGCQYL CLPAPQINPR SPKFTCACPD GMVLAKDMRS CHTGEGASPA
PSPCWLDPPE PLFPHLTMRS VQCFLWPVAL ALDLSAPCPF SLAALGDAAG RGGEERPRGV
GALSIVLPIA LLIVLCFGTF LLWKNWRLKN VNSIHFDNPV YQKTTEDEVH ICRSQDGYTY
PSRQMVSLED DVA
//
