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 22-NOV-2017, entry version 123.
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 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] (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. Not required for
CC endocytic uptake of SEPP1 in the kidney which is mediated by LRP2
CC (By similarity). {ECO:0000250|UniProtKB:Q14114,
CC ECO:0000250|UniProtKB:Q924X6}.
CC -!- SUBUNIT: Reelin associates with two or more receptor molecules.
CC Interacts with DAB1 and JNK-interacting proteins (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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. {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated upon apoE binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
DR EMBL; X97001; CAA65729.1; -; mRNA.
DR RefSeq; NP_990517.1; NM_205186.2. [Q98931-1]
DR UniGene; Gga.3461; -.
DR ProteinModelPortal; Q98931; -.
DR SMR; Q98931; -.
DR BioGrid; 676368; 2.
DR STRING; 9031.ENSGALP00000017370; -.
DR PaxDb; Q98931; -.
DR GeneID; 396102; -.
DR KEGG; gga:396102; -.
DR CTD; 7804; -.
DR eggNOG; ENOG410IPT5; Eukaryota.
DR eggNOG; ENOG410YQ6J; LUCA.
DR HOGENOM; HOG000115656; -.
DR HOVERGEN; HBG006250; -.
DR InParanoid; Q98931; -.
DR KO; K20052; -.
DR PhylomeDB; Q98931; -.
DR PRO; PR:Q98931; -.
DR Proteomes; UP000000539; Unplaced.
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 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; 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 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; 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 {ECO:0000255}.
FT CHAIN 25 917 Low-density lipoprotein receptor-related
FT protein 8.
FT /FTId=PRO_0000017334.
FT TOPO_DOM 25 838 Extracellular. {ECO:0000255}.
FT TRANSMEM 839 861 Helical. {ECO:0000255}.
FT TOPO_DOM 862 917 Cytoplasmic. {ECO:0000255}.
FT DOMAIN 28 64 LDL-receptor class A 1.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 67 105 LDL-receptor class A 2.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 108 146 LDL-receptor class A 3.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 148 184 LDL-receptor class A 4.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 187 225 LDL-receptor class A 5.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 272 308 LDL-receptor class A 6.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 312 351 LDL-receptor class A 7.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 346 390 EGF-like 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 391 430 EGF-like 2; calcium-binding.
FT {ECO:0000255|PROSITE-ProRule:PRU00076}.
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...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 532 532 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 782 782 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 820 820 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT DISULFID 29 41 {ECO:0000250}.
FT DISULFID 36 54 {ECO:0000250}.
FT DISULFID 48 63 {ECO:0000250}.
FT DISULFID 68 80 {ECO:0000250}.
FT DISULFID 75 93 {ECO:0000250}.
FT DISULFID 87 104 {ECO:0000250}.
FT DISULFID 109 123 {ECO:0000250}.
FT DISULFID 116 136 {ECO:0000250}.
FT DISULFID 130 145 {ECO:0000250}.
FT DISULFID 149 161 {ECO:0000250}.
FT DISULFID 156 174 {ECO:0000250}.
FT DISULFID 168 183 {ECO:0000250}.
FT DISULFID 188 200 {ECO:0000250}.
FT DISULFID 195 213 {ECO:0000250}.
FT DISULFID 207 224 {ECO:0000250}.
FT DISULFID 234 246 {ECO:0000250}.
FT DISULFID 241 259 {ECO:0000250}.
FT DISULFID 253 268 {ECO:0000250}.
FT DISULFID 273 285 {ECO:0000250}.
FT DISULFID 280 298 {ECO:0000250}.
FT DISULFID 292 307 {ECO:0000250}.
FT DISULFID 313 326 {ECO:0000250}.
FT DISULFID 321 339 {ECO:0000250}.
FT DISULFID 333 350 {ECO:0000250}.
FT DISULFID 355 366 {ECO:0000250}.
FT DISULFID 362 375 {ECO:0000250}.
FT DISULFID 377 389 {ECO:0000250}.
FT DISULFID 395 405 {ECO:0000250}.
FT DISULFID 401 414 {ECO:0000250}.
FT DISULFID 416 429 {ECO:0000250}.
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
//
