ID G3SLK2_LOXAF Unreviewed; 858 AA.
AC G3SLK2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Low-density lipoprotein receptor {ECO:0000256|ARBA:ARBA00039475};
GN Name=LDLR {ECO:0000313|Ensembl:ENSLAFP00000000302.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000000302.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000000302.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000302.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000000302.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000302.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of
CC plasma, and transports it into cells by endocytosis. In order to be
CC internalized, the receptor-ligand complexes must first cluster into
CC clathrin-coated pits. {ECO:0000256|ARBA:ARBA00037220}.
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000256|ARBA:ARBA00004603}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR AlphaFoldDB; G3SLK2; -.
DR STRING; 9785.ENSLAFP00000000302; -.
DR Ensembl; ENSLAFT00000000360.3; ENSLAFP00000000302.3; ENSLAFG00000000360.3.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000161046; -.
DR HOGENOM; CLU_008163_2_0_1; -.
DR InParanoid; G3SLK2; -.
DR OMA; GSRQCNK; -.
DR TreeFam; TF351700; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:1990666; C:PCSK9-LDLR complex; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0036477; C:somatodendritic compartment; IEA:Ensembl.
DR GO; GO:0097443; C:sorting endosome; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IEA:Ensembl.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IEA:Ensembl.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0070508; P:cholesterol import; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl.
DR GO; GO:0061889; P:negative regulation of astrocyte activation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:1903979; P:negative regulation of microglial cell activation; IEA:Ensembl.
DR GO; GO:0001920; P:negative regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR GO; GO:0015914; P:phospholipid transport; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; IEA:Ensembl.
DR GO; GO:0061771; P:response to caloric restriction; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
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; 6.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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 PANTHER; PTHR24270:SF21; LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 4.
PE 4: Predicted;
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW LDL {ECO:0000256|ARBA:ARBA00022710};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 785..808
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..340
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT DOMAIN 365..380
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 427..473
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 474..516
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 517..560
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 561..605
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 704..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 11..23
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 18..36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 73..88
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 93..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 100..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 112..127
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 185..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 192..210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 204..219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 224..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 231..249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 243..258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 272..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 858 AA; 94869 MW; E9105741E3C08165 CRC64;
AFSSLSAGDK CGRKEFQCRD GKCISYKWVC DGSAECQDGS DESQETCKSV TCQSGDFSCG
GRVNRCIPQF WRCDGQVDCE NGSDEQYCAP KTCSQDQFRC HDGKCISQVF VCDSDQDCLD
GSDEDACPVT MTTCGPANFQ CNTSTCIPEL WACDGDPDCE DGSDEWLQHC EGRNTSAPQR
DNGPCSSFEF HCRSGECIHT SWRCDAAPDC KDKSDEEDCA VATCRPDQFQ CGDGTCIHGS
RQCDKEYDCK DLSDEVGCIN VTLCEGPNKF KCHSGECITL DKVCNSVRDC RDWSDEPLKE
CGTNECLDNK GGCSHVCNDL KIGYECLCPE GFRLVDQRRC EDIDECQDPD SCSQICVNLE
GGYKCECHKG FQIDPHTKAC KAVGTIAYLF FTNRHEVRKM TLDRSEYTSL ITNLKNVVAL
DTEVASNRIY WSDLSQRKIY STQIDRAHSF SSYDTVISKD LHAPDGLAVD WVHSHIYWTD
SVLGTVSVAD TRGVKRKTLF KEKDSKPRAI VVDPAHGFMY WTDWGTPAKI KKGGLNGVDI
YSLVTEDIQW PNGITLDLSS GRLYWVDSKL HSISSIDVNG SNRKTVLEDK NRLAHPFSLA
IFEDKVFWTD IINEAIFSAN RLTGSDINLV AGNLLSPEDM VLFHNLMQPR GVNWCEKTSL
HNGGCQYLCL PAPQINPHSP KFTCACPDGM LLAKDMRSCI TAEAEPAATT EGSTTKGSST
AGSTFRQMVS SVATEPKQTA SPPAPSTSRQ PTASTEFTTA EMATVSHQAL GDVAGRGTEE
KPRRVGALSI ILPIVLLVLL CSGAFLLWKN WRLKSINSIN FDNPVYQKTT EDEVHICRSQ
DGYTYPSRQM VSLEDDMA
//
