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Database: UniProt
Entry: Q98931
LinkDB: Q98931
Original site: Q98931 
ID   LRP8_CHICK              Reviewed;         917 AA.
AC   Q98931; Q90883;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-APR-2014, entry version 103.
DE   RecName: Full=Low-density lipoprotein receptor-related protein 8;
DE            Short=LRP-8;
DE   AltName: Full=Apolipoprotein E receptor 2;
DE   AltName: Full=Protein LR8B;
DE   Flags: Precursor;
GN   Name=LRP8; Synonyms=LR8B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=White leghorn; TISSUE=Brain;
RX   PubMed=8662771; DOI=10.1074/jbc.271.20.11732;
RA   Novak S., Hiesberger T., Schneider W.J., Nimpf J.;
RT   "A new LDL receptor homologue with 8 ligand binding repeats in brain
RT   of chicken and mouse.";
RL   J. Biol. Chem. 271:11732-11736(1996).
RN   [2]
RP   ALTERNATIVE SPLICING, AND INTERACTION WITH ALPHA2-MACROGLOBULIN.
RX   PubMed=11294845; DOI=10.1074/jbc.M102662200;
RA   Brandes C., Kahr L., Stockinger W., Hiesberger T., Schneider W.J.,
RA   Nimpf J.;
RT   "Alternative splicing in the ligand binding domain of mouse ApoE
RT   receptor-2 produces receptor variants binding reelin but not alpha2-
RT   macroglobulin.";
RL   J. Biol. Chem. 276:22160-22169(2001).
CC   -!- FUNCTION: Cell surface receptor for Reelin (RELN) and
CC       apolipoprotein E (apoE)-containing ligands. Also binds alpha2-
CC       macroglobulin. LRP8 participates in transmitting the extracellular
CC       Reelin signal to intracellular signaling processes, by binding to
CC       DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL
CC       receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine
CC       phosphorylation and microtubule function in neurons. LRP8 has
CC       higher affinity for Reelin than VLDLR. LRP8 is thus a key
CC       component of the Reelin pathway which governs neuronal layering of
CC       the forebrain during embryonic brain development (By similarity).
CC   -!- SUBUNIT: Reelin associates with two or more receptor molecules.
CC       Interacts with DAB1 and JNK-interacting proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced;
CC       Name=1;
CC         IsoId=Q98931-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Mainly in brain.
CC   -!- PTM: O-glycosylated (By similarity).
CC   -!- PTM: Tyrosine phosphorylated upon apoE binding (By similarity).
CC   -!- SIMILARITY: Belongs to the LDLR family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 7 LDL-receptor class A domains.
CC   -!- SIMILARITY: Contains 5 LDL-receptor class B repeats.
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DR   EMBL; X97001; CAA65729.1; -; mRNA.
DR   RefSeq; NP_990517.1; NM_205186.1.
DR   UniGene; Gga.3461; -.
DR   ProteinModelPortal; Q98931; -.
DR   SMR; Q98931; 270-308, 351-432.
DR   PaxDb; Q98931; -.
DR   PRIDE; Q98931; -.
DR   GeneID; 396102; -.
DR   KEGG; gga:396102; -.
DR   CTD; 7804; -.
DR   eggNOG; NOG255913; -.
DR   HOGENOM; HOG000115656; -.
DR   HOVERGEN; HBG006250; -.
DR   InParanoid; Q98931; -.
DR   PhylomeDB; Q98931; -.
DR   NextBio; 20816160; -.
DR   PRO; PR:Q98931; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
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; IPR026823; cEGF.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_N_dom.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00058; Ldl_recept_b; 5.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   SUPFAM; SSF57424; SSF57424; 7.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 7.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS51120; LDLRB; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Complete proteome; Disulfide bond;
KW   EGF-like domain; Endocytosis; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    917       Low-density lipoprotein receptor-related
FT                                protein 8.
FT                                /FTId=PRO_0000017334.
FT   TOPO_DOM     25    838       Extracellular (Potential).
FT   TRANSMEM    839    861       Helical; (Potential).
FT   TOPO_DOM    862    917       Cytoplasmic (Potential).
FT   DOMAIN       28     64       LDL-receptor class A 1.
FT   DOMAIN       67    105       LDL-receptor class A 2.
FT   DOMAIN      108    146       LDL-receptor class A 3.
FT   DOMAIN      148    184       LDL-receptor class A 4.
FT   DOMAIN      187    225       LDL-receptor class A 5.
FT   DOMAIN      272    308       LDL-receptor class A 6.
FT   DOMAIN      312    351       LDL-receptor class A 7.
FT   DOMAIN      346    390       EGF-like 1.
FT   DOMAIN      391    430       EGF-like 2; calcium-binding (Potential).
FT   REPEAT      476    522       LDL-receptor class B 1.
FT   REPEAT      523    565       LDL-receptor class B 2.
FT   REPEAT      566    609       LDL-receptor class B 3.
FT   REPEAT      610    652       LDL-receptor class B 4.
FT   REPEAT      653    695       LDL-receptor class B 5.
FT   REGION      754    813       Clustered O-linked oligosaccharides.
FT   CARBOHYD    158    158       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    196    196       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    532    532       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    628    628       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    782    782       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    820    820       N-linked (GlcNAc...) (Potential).
FT   DISULFID     29     41       By similarity.
FT   DISULFID     36     54       By similarity.
FT   DISULFID     48     63       By similarity.
FT   DISULFID     68     80       By similarity.
FT   DISULFID     75     93       By similarity.
FT   DISULFID     87    104       By similarity.
FT   DISULFID    109    123       By similarity.
FT   DISULFID    116    136       By similarity.
FT   DISULFID    130    145       By similarity.
FT   DISULFID    149    161       By similarity.
FT   DISULFID    156    174       By similarity.
FT   DISULFID    168    183       By similarity.
FT   DISULFID    188    200       By similarity.
FT   DISULFID    195    213       By similarity.
FT   DISULFID    207    224       By similarity.
FT   DISULFID    234    246       By similarity.
FT   DISULFID    241    259       By similarity.
FT   DISULFID    253    268       By similarity.
FT   DISULFID    273    285       By similarity.
FT   DISULFID    280    298       By similarity.
FT   DISULFID    292    307       By similarity.
FT   DISULFID    313    326       By similarity.
FT   DISULFID    321    339       By similarity.
FT   DISULFID    333    350       By similarity.
FT   DISULFID    355    366       By similarity.
FT   DISULFID    362    375       By similarity.
FT   DISULFID    377    389       By similarity.
FT   DISULFID    395    405       By similarity.
FT   DISULFID    401    414       By similarity.
FT   DISULFID    416    429       By similarity.
SQ   SEQUENCE   917 AA;  101379 MW;  EF85E4D49441436A CRC64;
     MCRPALARLL LLQLLLLKLY LGKGAMKECD KDQFQCRNER CIPAVWACDE DNDCSDNSDE
     ADCPKKTCAE TDFACDNGHC IPDRWKCDGE EECSDGSDES EAACTKQVCP AEKISCGDLS
     NKCIPSSWRC DGQKDCESGI DEAGCAPACS PDEFQCSNKT CISINFVCDG YNNCGDGSDE
     KKCSPLTCSP NEFQCNNSVC IPQLWVCDNQ ADCEDHSDES IERCGYDAKA FNTCAAHEFQ
     CGNGECILLN WKCDGDEDCK DKSDEQDCPL VTCRPDEFQC GDGTCIHGAK QCDKVHDCPD
     NSDEAGCVQE SACESPSKFQ CKSGECIDGG KVCDLHRDCR DWSDEPLKEC GINECSLNNG
     GCSHICKDLK IGYECECPPG YKLLDKKTCG DIDECENPDA CSQICINYKG DYKCECYEGY
     EMDTLSKNCK AVGKSPYLIF TNRHEVRKID LVKRDYSRII PMLKNVVALD VEVATNRIYW
     CDLFYRKIYS AYIDKASDTA EQVILIDSQL NSPEGVAIDW VHKNIYWTDS GNKTISVATA
     DGSRRRTVFN SDLSEPRAIA VDPTRRFMYW SDWGDKAKIE KAGLNGVGRQ VLVSDNIEWP
     NGITLDLLNQ RLYWVDSKLH SLSCIDFNGS NREVLISSID DLSHPFGLAV FEDRVFWTDL
     ENEAIFSANR LSGLDISVLA ENLNNPHDIV VFHELKQPKA PDSCELSPQP NGGCEYLCLP
     APHISPRSPK FTCACPDNMW LGPDMKKCYK ELPTTPATVE VPTTTTSHPA ATSTVTVTGS
     ANTTTAVIPR AVSEATTAIP SSHSTTSLLI DSEMTTGNSN LSQHYSNNGQ GFDSTVTAAV
     IGIVIPVVVI GLLCMGGYLI WRNWKRKNTK SMNFDNPVYR KTTEEEDEDE IHIGRTAQIG
     HVYPARVALS LEDDGLP
//
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