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Database: UniProt
Entry: P98165
LinkDB: P98165
Original site: P98165 
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   13-FEB-2019, entry version 139.
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;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=White leghorn; TISSUE=Ovary;
RX   PubMed=7957081;
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
RT   member 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;
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: Binds VLDL and transports it into cells by endocytosis.
CC       In order to be internalized, the receptor-ligand complexes must
CC       first cluster into clathrin-coated pits. Binding to Reelin induces
CC       tyrosine phosphorylation of Dab1 and modulation of Tau
CC       phosphorylation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the extracellular matrix protein Reelin.
CC       Interacts with LDLRAP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Membrane, clathrin-coated pit; Single-pass type I
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Abundant in oocytes; much less in heart and
CC       skeletal muscle.
DR   EMBL; X80207; CAA56505.1; -; mRNA.
DR   PIR; S51789; S51789.
DR   RefSeq; NP_990560.1; NM_205229.1.
DR   UniGene; Gga.679; -.
DR   ProteinModelPortal; P98165; -.
DR   SMR; P98165; -.
DR   BioGrid; 676418; 2.
DR   STRING; 9031.ENSGALP00000016512; -.
DR   PaxDb; P98165; -.
DR   PRIDE; P98165; -.
DR   Ensembl; ENSGALT00000016531; ENSGALP00000016512; ENSGALG00000010166.
DR   GeneID; 396154; -.
DR   KEGG; gga:396154; -.
DR   CTD; 7436; -.
DR   eggNOG; ENOG410IPT5; Eukaryota.
DR   eggNOG; ENOG410YQ6J; LUCA.
DR   GeneTree; ENSGT00940000155460; -.
DR   HOGENOM; HOG000115656; -.
DR   HOVERGEN; HBG006250; -.
DR   InParanoid; P98165; -.
DR   KO; K20053; -.
DR   OrthoDB; 359795at2759; -.
DR   PhylomeDB; P98165; -.
DR   Reactome; R-GGA-8866376; Reelin signalling pathway.
DR   Reactome; R-GGA-8866427; VLDLR internalisation and degradation.
DR   PRO; PR:P98165; -.
DR   Proteomes; UP000000539; Chromosome Z.
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: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   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; PTHR43966:SF6; PTHR43966:SF6; 1.
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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Endocytosis; Glycoprotein; Lipid metabolism; Lipid transport;
KW   Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Steroid metabolism; Sterol metabolism; Transmembrane;
KW   Transmembrane helix; Transport; VLDL.
FT   SIGNAL        1     43       {ECO:0000255}.
FT   CHAIN        44    863       Very low-density lipoprotein receptor.
FT                                /FTId=PRO_0000017342.
FT   TOPO_DOM     44    785       Extracellular. {ECO:0000255}.
FT   TRANSMEM    786    809       Helical. {ECO:0000255}.
FT   TOPO_DOM    810    863       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       49     87       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       88    128       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      129    169       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      170    208       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      209    249       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      255    293       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      294    332       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      334    373       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      374    413       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      414    453       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT      457    498       LDL-receptor class B 1.
FT   REPEAT      499    544       LDL-receptor class B 2.
FT   REPEAT      545    587       LDL-receptor class B 3.
FT   REPEAT      588    631       LDL-receptor class B 4.
FT   REPEAT      632    674       LDL-receptor class B 5.
FT   REPEAT      675    717       LDL-receptor class B 6.
FT   DOMAIN      722    770       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   MOTIF       822    827       Endocytosis signal. {ECO:0000255}.
FT   CARBOHYD    169    169       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    773    773       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     51     63       {ECO:0000250}.
FT   DISULFID     58     76       {ECO:0000250}.
FT   DISULFID     70     85       {ECO:0000250}.
FT   DISULFID     90    102       {ECO:0000250}.
FT   DISULFID     97    115       {ECO:0000250}.
FT   DISULFID    109    126       {ECO:0000250}.
FT   DISULFID    131    145       {ECO:0000250}.
FT   DISULFID    138    158       {ECO:0000250}.
FT   DISULFID    152    167       {ECO:0000250}.
FT   DISULFID    172    184       {ECO:0000250}.
FT   DISULFID    179    197       {ECO:0000250}.
FT   DISULFID    191    206       {ECO:0000250}.
FT   DISULFID    211    223       {ECO:0000250}.
FT   DISULFID    218    236       {ECO:0000250}.
FT   DISULFID    230    247       {ECO:0000250}.
FT   DISULFID    257    269       {ECO:0000250}.
FT   DISULFID    264    282       {ECO:0000250}.
FT   DISULFID    276    291       {ECO:0000250}.
FT   DISULFID    296    308       {ECO:0000250}.
FT   DISULFID    303    321       {ECO:0000250}.
FT   DISULFID    315    330       {ECO:0000250}.
FT   DISULFID    336    349       {ECO:0000250}.
FT   DISULFID    344    362       {ECO:0000250}.
FT   DISULFID    356    373       {ECO:0000250}.
FT   DISULFID    378    389       {ECO:0000250}.
FT   DISULFID    385    398       {ECO:0000250}.
FT   DISULFID    400    412       {ECO:0000250}.
FT   DISULFID    418    428       {ECO:0000250}.
FT   DISULFID    424    437       {ECO:0000250}.
FT   DISULFID    439    452       {ECO:0000250}.
FT   DISULFID    726    739       {ECO:0000250}.
FT   DISULFID    735    754       {ECO:0000250}.
FT   DISULFID    756    769       {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
//
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