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Database: UniProt
Entry: O88204
LinkDB: O88204
Original site: O88204 
ID   LRP3_RAT                Reviewed;         770 AA.
AC   O88204;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAY-2019, entry version 119.
DE   RecName: Full=Low-density lipoprotein receptor-related protein 3;
DE            Short=LRP-3;
DE   AltName: Full=105 kDa low-density lipoprotein receptor-related protein;
DE            Short=rLRp105;
DE   Flags: Precursor;
GN   Name=Lrp3; Synonyms=Lrp105;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9693042; DOI=10.1006/geno.1998.5339;
RA   Ishii H., Kim D.-H., Fujita T., Endo Y., Saeki S., Yamamoto T.T.;
RT   "cDNA cloning of a new low-density lipoprotein receptor-related
RT   protein and mapping of its gene (LRP3) to chromosome bands 19q12-q13.
RT   2.";
RL   Genomics 51:132-135(1998).
RN   [2]
RP   INTERACTION WITH GGA1 AND GGA2.
RX   PubMed=11390366; DOI=10.1074/jbc.C100218200;
RA   Takatsu H., Katoh Y., Shiba Y., Nakayama K.;
RT   "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation
RT   factor-binding (GGA) proteins interact with acidic dileucine sequences
RT   within the cytoplasmic domains of sorting receptors through their
RT   Vps27p/Hrs/STAM (VHS) domains.";
RL   J. Biol. Chem. 276:28541-28545(2001).
CC   -!- FUNCTION: Probable receptor, which may be involved in the
CC       internalization of lipophilic molecules and/or signal
CC       transduction. Its precise role is however unclear, since it does
CC       not bind to very low density lipoprotein (VLDL) or to LRPAP1 in
CC       vitro (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds GGA1 and GGA2.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Membrane, coated pit
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
DR   EMBL; AB009463; BAA32331.1; -; mRNA.
DR   PIR; T00203; T00203.
DR   RefSeq; NP_445993.1; NM_053541.1.
DR   STRING; 10116.ENSRNOP00000015384; -.
DR   PhosphoSitePlus; O88204; -.
DR   PaxDb; O88204; -.
DR   PRIDE; O88204; -.
DR   Ensembl; ENSRNOT00000015384; ENSRNOP00000015384; ENSRNOG00000011451.
DR   GeneID; 89787; -.
DR   KEGG; rno:89787; -.
DR   UCSC; RGD:619729; rat.
DR   CTD; 4037; -.
DR   RGD; 619729; Lrp3.
DR   eggNOG; KOG1215; Eukaryota.
DR   eggNOG; ENOG410XP34; LUCA.
DR   GeneTree; ENSGT00940000160021; -.
DR   HOGENOM; HOG000013017; -.
DR   InParanoid; O88204; -.
DR   KO; K20050; -.
DR   OMA; DGWWHCP; -.
DR   OrthoDB; 135036at2759; -.
DR   PRO; PR:O88204; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000011451; Expressed in 10 organ(s), highest expression level in liver.
DR   Genevisible; O88204; RN.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00112; LDLa; 4.
DR   Gene3D; 2.60.120.290; -; 2.
DR   Gene3D; 4.10.400.10; -; 4.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00057; Ldl_recept_a; 3.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00192; LDLa; 5.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF57424; SSF57424; 4.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01209; LDLRA_1; 3.
DR   PROSITE; PS50068; LDLRA_2; 4.
PE   1: Evidence at protein level;
KW   Coated pit; Complete proteome; Disulfide bond; Endocytosis;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     36       {ECO:0000255}.
FT   CHAIN        37    770       Low-density lipoprotein receptor-related
FT                                protein 3.
FT                                /FTId=PRO_0000017324.
FT   TOPO_DOM     37    496       Extracellular. {ECO:0000255}.
FT   TRANSMEM    497    517       Helical. {ECO:0000255}.
FT   TOPO_DOM    518    770       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       43    159       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      165    201       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      211    250       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      254    365       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      415    453       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      454    490       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   COMPBIAS    682    685       Poly-Pro.
FT   CARBOHYD     71     71       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    199    199       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    359    359       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     43     72       {ECO:0000250}.
FT   DISULFID     99    120       {ECO:0000250}.
FT   DISULFID    166    178       {ECO:0000250}.
FT   DISULFID    173    191       {ECO:0000250}.
FT   DISULFID    185    200       {ECO:0000250}.
FT   DISULFID    212    227       {ECO:0000250}.
FT   DISULFID    219    240       {ECO:0000250}.
FT   DISULFID    234    249       {ECO:0000250}.
FT   DISULFID    254    282       {ECO:0000250}.
FT   DISULFID    416    430       {ECO:0000250}.
FT   DISULFID    423    443       {ECO:0000250}.
FT   DISULFID    437    452       {ECO:0000250}.
FT   DISULFID    455    467       {ECO:0000250}.
FT   DISULFID    462    480       {ECO:0000250}.
FT   DISULFID    474    489       {ECO:0000250}.
SQ   SEQUENCE   770 AA;  83017 MW;  9ECF3F8642FEB7C7 CRC64;
     MEKRAAAGPE GAPGARAPLA VVCLVNLFLT GRLSSAVPAL AACSGKLEQH TERRGVIYSP
     AWPLNYPPGT NCSWYIQGDR GDMITISFRN FDVEESHQCS LDWLLLGPAA PPRQEAFRLC
     GSAIPPAFIS ARDHVWIFFH SDASSSGQAQ GFRLSYIRGK LGQASCQTDE FRCDNGKCLP
     GPWQCNMVDE CGDGSDEGNC SAPASEPPGS LCPGGTFPCS GARSTRCLPV ERRCDGTQDC
     GDGSDEAGCP DLACGRRLGS FYGSFASPDL FGAARGPSDL HCTWLVDTQD PRRVLLQLEL
     RLGYDDYVQV YEGLGERGDR LLQTLSYRSN HRPVSLEAAQ GRLTVAYHAR ARSAGHGFNA
     TYQVKGYCLP WEQPCGSSSE GDDGSTGEQG CFSEPQRCDG WWHCASGRDE QGCPACPPDQ
     YPCEGGSGLC YAPADRCNNQ KSCPDGADEK NCFSCQPGTF HCGTNLCIFE TWRCDGQEDC
     QDGSDEHGCL AAVPRKVITA ALIGSLVCGL LLVIALGCAF KLYSLRTQEY RAFETQMTRL
     EAEFVRREAP PSYGQLIAQG LIPPVEDFPV YSASQASVLQ NLRTAMRRQM RRHASRRGPS
     RRRLGRLWNR LFHRPRAPRG QIPLLTAART SQTVLGDGLL QAAPGPVPDP PVPNTDTGSP
     REAGDGPPSG SGHAPEVGPS VPPPPLNLRD PEYRPEDKER KACVDPLEDS PAPVDTPPEP
     CLAQDPHPQT PTASGIQDPH SAEPLGVCRS PPPTCSPILE ASDDEALLVC
//
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