LRP3_RAT
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 03-AUG-2022, entry version 131.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 protein and
RT mapping of its gene (LRP3) to chromosome bands 19q12-q13. 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 transduction. Its
CC precise role is however unclear, since it does not bind to very low
CC density lipoprotein (VLDL) or to LRPAP1 in vitro (By similarity).
CC {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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB009463; BAA32331.1; -; mRNA.
DR PIR; T00203; T00203.
DR RefSeq; NP_445993.1; NM_053541.1.
DR AlphaFoldDB; O88204; -.
DR STRING; 10116.ENSRNOP00000015384; -.
DR GlyGen; O88204; 3 sites.
DR PhosphoSitePlus; O88204; -.
DR PaxDb; O88204; -.
DR PRIDE; O88204; -.
DR GeneID; 89787; -.
DR KEGG; rno:89787; -.
DR UCSC; RGD:619729; rat.
DR CTD; 4037; -.
DR RGD; 619729; Lrp3.
DR VEuPathDB; HostDB:ENSRNOG00000011451; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_013747_1_0_1; -.
DR InParanoid; O88204; -.
DR OMA; KACREPL; -.
DR OrthoDB; 135036at2759; -.
DR PRO; PR:O88204; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000011451; Expressed in liver and 18 other tissues.
DR Genevisible; O88204; RN.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
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; Disulfide bond; Endocytosis; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..770
FT /note="Low-density lipoprotein receptor-related protein 3"
FT /id="PRO_0000017324"
FT TOPO_DOM 37..496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..159
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 165..201
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 211..250
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 254..365
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 415..453
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 454..490
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 639..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..72
FT /evidence="ECO:0000250"
FT DISULFID 99..120
FT /evidence="ECO:0000250"
FT DISULFID 166..178
FT /evidence="ECO:0000250"
FT DISULFID 173..191
FT /evidence="ECO:0000250"
FT DISULFID 185..200
FT /evidence="ECO:0000250"
FT DISULFID 212..227
FT /evidence="ECO:0000250"
FT DISULFID 219..240
FT /evidence="ECO:0000250"
FT DISULFID 234..249
FT /evidence="ECO:0000250"
FT DISULFID 254..282
FT /evidence="ECO:0000250"
FT DISULFID 416..430
FT /evidence="ECO:0000250"
FT DISULFID 423..443
FT /evidence="ECO:0000250"
FT DISULFID 437..452
FT /evidence="ECO:0000250"
FT DISULFID 455..467
FT /evidence="ECO:0000250"
FT DISULFID 462..480
FT /evidence="ECO:0000250"
FT DISULFID 474..489
FT /evidence="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
