ID A0A3P9PJ68_POERE Unreviewed; 811 AA.
AC A0A3P9PJ68;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Low density lipoprotein receptor {ECO:0000313|Ensembl:ENSPREP00000021780.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000021780.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000021780.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000021780.1};
RG Ensembl;
RL Submitted (SEP-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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 8081.ENSPREP00000021780; -.
DR Ensembl; ENSPRET00000022009.1; ENSPREP00000021780.1; ENSPREG00000014707.1.
DR GeneTree; ENSGT00940000154819; -.
DR OMA; GSEFRCK; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000014707; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:Ensembl.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00112; LDLa; 4.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
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; 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; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 5.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 5.
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};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; 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:UP000242638};
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 735..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 249..288
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 374..420
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 421..463
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 464..507
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 508..552
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 647..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 44..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 51..69
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 63..78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 83..95
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 90..108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 132..144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 139..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 151..166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 171..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 178..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 190..205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 219..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 811 AA; 90619 MW; E0C2E79079EDC3C1 CRC64;
FYFILFMFYR HVFCLCLVVS LNFSMLRKNX KIYIFTSIPV AKRCSNSEFR CTSGQCVSSS
FXCDKDADCD DGSDEASCPP XTCSGVSFQC NNTVCVPRLW TCDGDADCSD GSDEWPQNCA
SRTPTRSPIH QCSSQEYQCR NGECIHVSWR CDGDPDCLDR SDEDGCAHST CRPDEFECGD
GTCIHGSNQC NHHYDCTDMS DEVGCVNASH CDGPNQFKCR SGECISMERV CDNKRDCRDW
SDEPLRECGS NECLYNNGGC SHICNDLKIG YECLCPAGYT LVAKRRCEDI DECTNPETCS
QICINQMGGY KCDCEEGYHI DPATQACKAV GTTPYLFFTN RHEVRKMTLD RSEYTRVIPR
LKNVVALDMN VATQEMYWSD LSLKKIYRTP MDSAEDFSRH HVVIGSDIDG PEGIAFDWVH
GNLYWTDSIR KTVSVVTADG SRRKTLFHQD LSKPRAIVVD PHTNFIYWTD WGSPAKIEKG
GLNGVDRTAL VTDNIVWPNG ITIDLLNQRL YWVDSKLHTL SSIDMQGGGR RTLIIDEDKL
AHPLGLTVFE ERVFWTDVSN NAILSANRLT GGDIAPVAEH LSSPEDIVLY HNLKQPAGRN
WCQVSNSTCE FMCLAAPQIG THPPKYTCVC PDNMMLAGDM RTCVPVSSAS SESRASTTHP
PVVPTTPPKT TAPKTTQKPR VPITTTVPPI IPTTATKPVX RTTRPTVRTT TPLPKKPSPQ
PEKPKISQTT TAAPLTTPAI LCLVAVGGVL LWRYYRLQNT NTMHFHNPVY QKTTEDQVHI
WRSQSLEGYA YPKRQIVSLD EEADNPSFIE N
//