VLDLR_CHICK
ID VLDLR_CHICK Reviewed; 863 AA.
AC P98165;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Very low-density lipoprotein receptor;
DE Short=VLDL receptor;
DE Short=VLDL-R;
DE AltName: Full=Vitellogenin receptor;
DE Short=VTG receptor;
DE Flags: Precursor;
GN Name=VLDLR; Synonyms=VTGR;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Ovary;
RX PubMed=7957081; DOI=10.1002/j.1460-2075.1994.tb06847.x;
RA Bujo H., Hermann M., Kaderli M.O., Jacobsen L., Sugawara S., Nimpf J.,
RA Yamamoto T., Schneider W.J.;
RT "Chicken oocyte growth is mediated by an eight ligand binding repeat member
RT of the LDL receptor family.";
RL EMBO J. 13:5165-5175(1994).
RN [2]
RP PROTEIN SEQUENCE OF 510-518; 546-554 AND 819-827.
RC STRAIN=White leghorn; TISSUE=Ovarian follicle membrane;
RX PubMed=1655760; DOI=10.1016/s0021-9258(18)55128-0;
RA Barber D.L., Sanders E.J., Aebersold R., Schneider W.J.;
RT "The receptor for yolk lipoprotein deposition in the chicken oocyte.";
RL J. Biol. Chem. 266:18761-18770(1991).
CC -!- FUNCTION: Multifunctional cell surface receptor that binds VLDL and
CC transports it into cells by endocytosis and therefore plays an
CC important role in energy metabolism. Binds also to a wide range of
CC other molecules including Reelin/RELN or apolipoprotein E/APOE-
CC containing ligands as well as clusterin/CLU. In the off-state of the
CC pathway, forms homooligomers or heterooligomers with LRP8. Upon binding
CC to ligands, homooligomers are rearranged to higher order receptor
CC clusters that transmit the extracellular RELN signal to intracellular
CC signaling processes by binding to DAB1 (By similarity). This
CC interaction results in phosphorylation of DAB1 leading to the ultimate
CC cell responses required for the correct positioning of newly generated
CC neurons. Later, mediates a stop signal for migrating neurons,
CC preventing them from entering the marginal zone (By similarity).
CC {ECO:0000250|UniProtKB:P98155, ECO:0000250|UniProtKB:P98156}.
CC -!- SUBUNIT: Homooligomer. Binds to the extracellular matrix protein
CC Reelin/RELN. Interacts with LRP8 (By similarity). Interacts with
CC LDLRAP1 (By similarity). Interacts with SNX17 (By similarity).
CC Interacts with DAB1. Interacts with PCSK9. Interacts with PAFAH1B3 and
CC PAFAH1B2, the catalytic complex of (PAF-AH (I)) heterotetrameric
CC enzyme; these interactions may modulate the Reelin pathway. Interacts
CC with STX5; this interaction mediates VLDLR translocation from the
CC endoplasmic reticulum to the plasma membrane. Interacts with CLU (By
CC similarity). {ECO:0000250|UniProtKB:P98155,
CC ECO:0000250|UniProtKB:P98156}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Membrane, clathrin-coated pit; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Abundant in oocytes; much less in heart and
CC skeletal muscle.
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DR EMBL; X80207; CAA56505.1; -; mRNA.
DR PIR; S51789; S51789.
DR RefSeq; NP_990560.1; NM_205229.1.
DR AlphaFoldDB; P98165; -.
DR SMR; P98165; -.
DR BioGRID; 676418; 2.
DR STRING; 9031.ENSGALP00000016512; -.
DR PaxDb; P98165; -.
DR PRIDE; P98165; -.
DR ABCD; P98165; 1 sequenced antibody.
DR Ensembl; ENSGALT00000016531; ENSGALP00000016512; ENSGALG00000010166.
DR GeneID; 396154; -.
DR KEGG; gga:396154; -.
DR CTD; 7436; -.
DR VEuPathDB; HostDB:geneid_396154; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000155460; -.
DR InParanoid; P98165; -.
DR PhylomeDB; P98165; -.
DR PRO; PR:P98165; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000010166; Expressed in skeletal muscle tissue and 12 other tissues.
DR ExpressionAtlas; P98165; baseline and differential.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030228; F:lipoprotein particle receptor activity; IC:BHF-UCL.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR CDD; cd00112; LDLa; 8.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 4.10.400.10; -; 8.
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; 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 InterPro; IPR032931; VLDLR.
DR PANTHER; PTHR24270:SF16; PTHR24270:SF16; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57424; SSF57424; 8.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS01209; LDLRA_1; 8.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 5.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Coated pit; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein;
KW Lipid metabolism; Lipid transport; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Steroid metabolism; Sterol metabolism; Transmembrane;
KW Transmembrane helix; Transport; VLDL.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..863
FT /note="Very low-density lipoprotein receptor"
FT /id="PRO_0000017342"
FT TOPO_DOM 44..785
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..809
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..87
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 88..128
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 129..169
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 170..208
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 209..249
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 255..293
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 294..332
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 334..373
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 374..413
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 414..453
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 457..498
FT /note="LDL-receptor class B 1"
FT REPEAT 499..544
FT /note="LDL-receptor class B 2"
FT REPEAT 545..587
FT /note="LDL-receptor class B 3"
FT REPEAT 588..631
FT /note="LDL-receptor class B 4"
FT REPEAT 632..674
FT /note="LDL-receptor class B 5"
FT REPEAT 675..717
FT /note="LDL-receptor class B 6"
FT DOMAIN 722..770
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MOTIF 822..827
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..63
FT /evidence="ECO:0000250"
FT DISULFID 58..76
FT /evidence="ECO:0000250"
FT DISULFID 70..85
FT /evidence="ECO:0000250"
FT DISULFID 90..102
FT /evidence="ECO:0000250"
FT DISULFID 97..115
FT /evidence="ECO:0000250"
FT DISULFID 109..126
FT /evidence="ECO:0000250"
FT DISULFID 131..145
FT /evidence="ECO:0000250"
FT DISULFID 138..158
FT /evidence="ECO:0000250"
FT DISULFID 152..167
FT /evidence="ECO:0000250"
FT DISULFID 172..184
FT /evidence="ECO:0000250"
FT DISULFID 179..197
FT /evidence="ECO:0000250"
FT DISULFID 191..206
FT /evidence="ECO:0000250"
FT DISULFID 211..223
FT /evidence="ECO:0000250"
FT DISULFID 218..236
FT /evidence="ECO:0000250"
FT DISULFID 230..247
FT /evidence="ECO:0000250"
FT DISULFID 257..269
FT /evidence="ECO:0000250"
FT DISULFID 264..282
FT /evidence="ECO:0000250"
FT DISULFID 276..291
FT /evidence="ECO:0000250"
FT DISULFID 296..308
FT /evidence="ECO:0000250"
FT DISULFID 303..321
FT /evidence="ECO:0000250"
FT DISULFID 315..330
FT /evidence="ECO:0000250"
FT DISULFID 336..349
FT /evidence="ECO:0000250"
FT DISULFID 344..362
FT /evidence="ECO:0000250"
FT DISULFID 356..373
FT /evidence="ECO:0000250"
FT DISULFID 378..389
FT /evidence="ECO:0000250"
FT DISULFID 385..398
FT /evidence="ECO:0000250"
FT DISULFID 400..412
FT /evidence="ECO:0000250"
FT DISULFID 418..428
FT /evidence="ECO:0000250"
FT DISULFID 424..437
FT /evidence="ECO:0000250"
FT DISULFID 439..452
FT /evidence="ECO:0000250"
FT DISULFID 726..739
FT /evidence="ECO:0000250"
FT DISULFID 735..754
FT /evidence="ECO:0000250"
FT DISULFID 756..769
FT /evidence="ECO:0000250"
SQ SEQUENCE 863 AA; 94905 MW; 0672A8748F9A2245 CRC64;
MRSSRQRGDR SAATGGGCGA RRWALPRCGA LCLLLALGCL RTATDGAKAK CEESQFQCSN
GRCIPLLWKC DGDEDCSDGS DESACVKKTC AESDFVCNSG QCVPNRWQCD GDPDCEDGSD
ESAELCHMRT CRVNEISCGP QSTQCIPVSW KCDGEKDCDS GEDEENCGNV TCSAAEFTCS
SGQCISKSFV CNGQDDCSDG SDELECAPPT CGVHEFQCKS STCIPISWVC DDDADCSDHS
DESLEQCGRQ PAPPVKCSTS EVQCGSGECI HKKWRCDGDP DCKDGSDEIN CPSRTCRPDQ
FRCEDGNCIH GSRQCNGVRD CLDGTDEANC NNVIQCSGPG KFKCRSGECI DINKVCNHHG
DCKDWSDEPL KECNINECLV NNGGCSHICR DLVIGYECDC PAGFELVDRR TCGDIDECQN
PGICSQICIN LKGGYKCECS RGYQMDLATG VCKAVGKEPC LIFTNRRDIR KIGLERKEYI
QLVEQLRNTV ALDADIAEQK LYWADFSQKA IFSASIDTRD KVGTHTRILD NIHSPAGIAV
DWIYKNIYWT DSSAKTISVA SLNGKKRKVL FLSELREPAS IAVDPLSGFM YWSDWGEPAK
IEKAGMNGFD RQQLVTTEIQ WPNGIALDLV KSRLYWLDSK LHMLSSVDLN GQDRRLVLKS
HMFLPHPLAL TIFEDRVFWI DGENEAVYGA NKFTGAELVT LVNNLNDAQD IIVYHELVQP
SGRNWCEENM VNGGCSYLCL PAPQINEHSP KYTCTCPAGY FLQEDGLRCG GFNISSVVSE
VAARGAAGAW AVLPILLLVT AALAGYFMWR NWQHKNMKSM NFDNPVYLKT TEEDLTIDIG
RHSGSVGHTY PAISVVSTDD DML
