Lrp2
entrez
29216
canonical
uniprot
P98158
canonical
ensembl
ENSRNOG00000056184
resolver
ensembl
ENSRNOG00055023755
resolver
ensembl
ENSRNOG00060003241
resolver
ensp
ENSRNOP00000075159
resolver
ensp
ENSRNOP00055033167
resolver
ensp
ENSRNOP00060003934
resolver
enst
ENSRNOT00000082624
resolver
enst
ENSRNOT00055040830
resolver
enst
ENSRNOT00060005346
resolver
genesymbol
Lrp2
resolver
uniprot
A0A0G2K9W7
resolver
uniprot_entry
A0A0G2K9W7_RAT
resolver
uniprot_entry
LRP2_RAT
resolver
amino_acid_sequence
MERGAAAAAWMLLLAIAACLEPVSSQECGSGNFRCDNGYCIPASWRCDGTRDCLDDTDEIGCPPRSCESGLFLCPAEGTCIPSSWVCDEDKDCSDGADEQQNCAGTTCSAQQMTCSNGQCIPSEYRCDHVSDCPDGSDERNCHYPTCDQLTCANGACYNTSQRCDQKVDCRDSSDEANCTTLCSQKEFECGSGECILRAYVCDHDNDCEDNSDERNCNYDTCGGHQFTCSNGQCINQNWVCDGDDDCQDSGDEDGCESNQSHHRCYPREWACPGSGRCISIDKVCDGVPDCPEGDDENNVTSGRTCGMGVCSVLNCEYQCHQTPFGGECFCPPGHIINSNDSRTCIDFDDCQIWGICDQKCENRQGRHQCLCEEGYILERGQHCKSSDSFSAASVIFSNGRDLLVGDLHGRNFRILAESKNRGMVMGVDFHYQKHRVFWTDPMQEKVFSTDINGLNTQEILNVSVDTPENLAVDWINNKLYLVETKVNRIDVVNLEGNQRVTLITENLGHPRGIALDPTVGYLFFSDWGSLSGQPKVERAFMDGSNRKDLVTTKVGWPAGITLDLVSKRVYWVDSRYDYIETVTYDGIQRKTVARGGSLVPHPFGISLFEEHVFFTDWTKMAVMKASKFTETNPQVYHQSSLRPHGVTVYHALRQPNATNPCGSNNGGCAQVCVLSHRTDNGGLGYRCKCEFGFELDDDEHRCVAVKNFLLFSSKTAVRGIPFTLSTQEDVMVPVTGSPSFFVGIDFDAQHSTVFYSDLSKDIIYKQKIDGTGKEVITANRLESVECLTFDWISRNLYWTDGGLKSVTVLRLADKSRRQIISNLNNPRSIVVHPTAGYMFLSDWFRPAKIMRAWSDGSHLMPIVNTSLGWPNGLAIDWSASRLYWVDAFFDKIEHSTLDGLDRKRLGHVDQMTHPFGLTVFKDNVFITDWRLGAIIRVRKSDGGDMTVIRRGISSVMHVKAYDADLQTGSNYCSQTTHANGDCSHFCFPVPNFQRVCGCPYGMKLQRDQMTCEGDPAREPPTQQCGSLSFPCNNGKCVPSFFRCDGVDDCHDNSDEHQCGVFNNTCSPSAFACVRGGQCIPGQWHCDRQNDCLDGSDEQNCPTHATSSTCPSTSFTCDNHVCIPKDWVCDTDNDCSDGSDEKNCQASGTCQPTQFRCPDHRCISPLYVCDGDKDCADGSDEAGCVLNCTSAQFKCADGSSCINSRYRCDGVYDCRDNSDEAGCPTRPPGMCHPDEFQCQGDGTCIPNTWECDGHPDCIHGSDEHTGCVPKTCSPTHFLCDNGNCIYKAWICDGDNDCRDMSDEKDCPTQPFHCPSTQWQCPGYSTCINLSALCDGVFDCPNGTDESPLCNQDSCSHFNGGCTHQCMQGPFGATCLCPLGYQLANDTKTCEDINECDIPGFCSQHCVNMRGSFRCACDPEYTLESDGRTCKVTGSENPLLVVASRDKIIVDNITAHTHNLYSLVQDVSFVVALDFDSVTGRVFWSDLLQGKTWSVFQNGTDKRVVHDSGLSVTEMIAVDWIGRNLYWTDYALETIEVSKIDGSHRTVLISKNVTKPRGLALDPRMGDNVMFWSDWGHHPRIERASMDGTMRTVIVQEKIYWPCGLSIDYPNRLIYFMDAYLDYIEFCDYDGHNRRQVIASDLVLHHPHALTLFEDFVYWTDRGTRQVMQANKWHGGNQSVVMYSVHQPLGITAIHPSRQPPSRNPCASASCSHLCLLSAQAPRHYSCACPSGWNLSDDSVNCVRGDQPFLMSVRDNIIFGISLDPEVKSNDAMVPISGIQHGYDVEFDDSEQFIYWVENPGEIHRVKTDGSNRTVFAPLSLLGSSLGLALDWVSRNIYYTTPASRSIEVLTLKGDTRYGKTLIANDGTPLGVGFPVGIAVDPARGKLYWSDHGTDSGVPAKIASANMDGTSLKILFTGNLQHLEVVTLDIQEQKLYWAVTSRGVIERGNVDGTERMILVHHLAHPWGLVVYGSFLYYSDEQYEVIERVDKSSGNNKVVLRDNVPYLRGLRVYHRRNAADSSNGCSNNPNACQQICLPVPGGMFSCACASGFKLSPDGRSCSPYNSFMVVSMLPAVRGFSLELSDHSEAMVPVAGQGRNVLHADVDVANGFIYWCDFSSSVRSSNGIRRIKPDGSNFTNVVTYGIGANGIRGVALDWAAGNLYFTNAFVYETLIEVLRINTTYRRVLLKVSVDMPRHIIVDPKHRYLFWADYGQKPKIERSFLDCTNRTVLVSEGIVTPRGLAMDHDTGYIYWVDDSLDLIARIHLDGGESQVVRYGSRYPTPYGITVFGESIIWVDRNLKKVFQASKQPGNTDPPVVIRDKINLLRDVTIFDEHAQPLSPAELNNNPCLQSNGGCSHFCFALPELPTPRCGCAFGTLGNDGKSCATSQEDFLIYSLNNSLRSLHFDPRDHSLPFQVISVAGTAIALDYDRRNNRIFFTQKLNSLRGQISYVSLYSGSSSPTVLLSNIGVTDGIAFDWINRRIYYSDFSNQTINSMAEDGSNRAVIARVSKPRAIVLDPCRGYMYWTDWGTNAKIERATLGGNFRVPIVNTSLVWPNGLALDLETDLLYWADASLQKIERSTLTGTNREVVVSTAFHSFGLTVYGQYIYWTDLYTRKIYRANKYDGSDLVAMTTRLPTQPSGISTVVKTQRQQCSNPCDQFNGGCSHICAPGPNGAECQCPHEGNWYLANDNKYCVVDTGTRCNQLQFTCLNGHCINQDWKCDNDNDCGDGSDELPTVCAFHTCRSTAFTCGNGRCVPYHYRCDYYNDCGDNSDEAGCLFRNCNSTTEFTCSNGRCIPLSYVCNGINNCHDNDTSDEKNCPPHTCPPDFTKCQTTNICVPRAFLCDGDNDCGDGSDENPIYCASHTCRSNEFQCLSPQRCIPSYWFCDGEADCADGSDEPDTCGHSVNTCRASQFQCDNGRCISGNWVCDGDNDCGDMSDEDQRHHCELQNCSSTQFTCVNSRPPNRRCIPQYWVCDGDADCSDALDELQNCTMRTCSAGEFSCANGRCVRQSFRCDRRNDCGDYSDERGCSYPPCHANQFTCQNGRCIPRFFVCDEDNDCGDGSDEQEHLCHTPEPTCPLHQFRCDNGHCIEMGRVCNHVDDCSDNSDEKGCGINECLDSSISRCDHNCTDTITSFYCSCLPGYKLMSDKRSCVDIDECKESPQLCSQKCENVVGSYICKCAPGYIREPDGKSCRQNSNIEPYLIFSNRYYIRNLTTDGSSYSLILQGLGNVVALDFDRVEKRLYWIDAEKQIIERMFLNKTNRETIINHRLRRAESLAVDWVSRKLYWLDAILDCLFVSDLEGRHRKMIAQHCVDANNTFCFEHPRGIVLHPQRGHVYWADWGVHAYIGRIGMDGTNKSVIISTKIEWPNAITIDYTNDLLYWADAHLGYIEFSDLEGHHRHTVYDGSLPHPFALTIFEDTVFWTDWNTRTVEKGNKYDGSGRVVLVNTTHKPFDIHVYHPYRQPIMSNPCGTNNGGCSHLCLIKAGGRGFTCACPDDFQTVQLRDRTLCMPMCSSTQFLCGNNEKCIPIWWKCDGQKDCSDGSDEPDLCPHRFCRLGQFQCRDGNCTSPQALCNARQDCADGSDEDRVLCEHHRCESNEWQCANKRCIPQSWQCDSVNDCLDNSDEDTSHCASRTCRPGQFKCNNGRCIPQSWKCDVDNDCGDYSDEPIDECTTAAYNCDNHTEFSCKTNYRCIPQWAVCNGFDDCRDNSDEQGCESVPCHPSGDFRCANHHCIPLRWKCDGTDDCGDNSDEENCVPRECSESEFRCADQQCIPSRWVCDQENDCGDNSDERDCEMKTCHPEHFQCTSGHCVPKALACDGRADCLDASDESACPTRFPNGTYCPAAMFECKNHVCIQSFWICDGENDCVDGSDEEIHLCFNIPCESPQRFRCDNSRCVYGHQLCNGVDDCGDGSDEKEEHCRKPTHKPCTDTEYKCSNGNCISQHYVCDNVNDCGDLSDETGCNLGDNRTCAENICEQNCTQLSSGGFICSCRPGFKPSTSDKNSCQDINECEEFGICPQSCRNSKGSYECFCVDGFKSMSTHYGERCAADGSPPLLLLPENVRIRKYNTSSEKFSEYLEEEEHIQTIDYDWDPEHIGLSVVYYTVLAQGSQFGAIKRAYIPNFESGSNNPIREVDLGLKYLMQPDGLAVDWVGRHIYWSDAKSQRIEVATLDGRYRKWLITTQLDQPAAIAVNPKLGLMFWTDQGKQPKIESAWMNGEHRSVLVSENLGWPNGLSIDYLNDDRVYWSDSKEDVIEAIKYDGTDRRLIINEAMKPFSLDIFEDKLYWVAKEKGEVWRQNKFGKENKEKVLVVNPWLTQVRIFHQLRYNQSVSNPCKQVCSHLCLLRPGGYSCACPQGSDFVTGSTVQCDAASELPVTMPPPCRCMHGGNCYFDENELPKCKCSSGYSGEYCEVGLSRGIPPGTTMAVLLTFVIVIIVGALVLVGLFHYRKTGSLLPTLPKLPSLSSLAKPSENGNGVTFRSGADVNMDIGVSPFGPETIIDRSMAMNEHFVMEVGKQPVIFENPMYAAKDNTSKVALAVQGPSTGAQVTVPENVENQNYGRPIDPSEIVPEPKPASPGADEIQGKKWNIFKRKPKQTTNFENPIYAEMDSEVKDAVAVAPPPSPSLPAKASKRNLTPGYTATEDTFKDTANLVKEDSDV
uniprot
proteins
function
FUNCTION: Multiligand endocytic receptor. Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (PubMed:19202329, PubMed:7544804). In the kidney, mediates the tubular uptake and clearance of leptin (By similarity). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (PubMed:17324488). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (By similarity). Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (PubMed:17462596). Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (By similarity). Mediates renal uptake of metallothionein-bound heavy metals (PubMed:15126248). Together with CUBN, mediates renal reabsorption of myoglobin (PubMed:12724130). Mediates renal uptake and subsequent lysosomal degradation of APOM (PubMed:16099815). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (By similarity). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (By similarity). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (PubMed:28659595). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (PubMed:11964399, PubMed:16801528). Also mediates ShhN transcytosis (PubMed:16801528). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (By similarity). Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (By similarity). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (By similarity). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (By similarity). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (PubMed:18466341). Involved in neurite branching (By similarity). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (By similarity). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (By similarity). Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (PubMed:16143106). Mediates endocytosis of angiotensin-2 (PubMed:15467006). Also mediates endocytosis of angiotensin 1-7 (PubMed:16380466). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity). Required for embryonic heart development (By similarity). Required for normal hearing, possibly through interaction with estrogen in the inner ear (PubMed:17846082). {ECO:0000250|UniProtKB:A2ARV4, ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:11964399, ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:15126248, ECO:0000269|PubMed:15467006, ECO:0000269|PubMed:16099815, ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:16801528, ECO:0000269|PubMed:17324488, ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:18466341, ECO:0000269|PubMed:19202329, ECO:0000269|PubMed:28659595, ECO:0000269|PubMed:7544804}.
uniprot
proteins
mass_dalton
519276
uniprot
proteins
mutagenesis
MUTAGEN 4527; /note="Y->C: Reduced interaction with ARH and dynein."; /evidence="ECO:0000269|PubMed:23836931
uniprot
proteins
post_translational_modification
PTM: A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved by gamma-secretase to release a fragment which translocates to the nucleus and mediates transcriptional repression. {ECO:0000269|PubMed:23836931}.; PTM: N-glycosylation is required for ligand binding. {ECO:0000250|UniProtKB:A2ARV4}.
uniprot
proteins
protein_family
LDLR family
uniprot
proteins
pubmed
11964399
uniprot
proteins
pubmed
12519751
uniprot
proteins
pubmed
12724130
uniprot
proteins
pubmed
1400426
uniprot
proteins
pubmed
15126248
uniprot
proteins
pubmed
15467006
uniprot
proteins
pubmed
16099815
uniprot
proteins
pubmed
16143106
uniprot
proteins
pubmed
16380466
uniprot
proteins
pubmed
16801528
uniprot
proteins
pubmed
17063000
uniprot
proteins
pubmed
17245526
uniprot
proteins
pubmed
17324488
uniprot
proteins
pubmed
17462596
uniprot
proteins
pubmed
17846082
uniprot
proteins
pubmed
18466341
uniprot
proteins
pubmed
19202329
uniprot
proteins
pubmed
22649097
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
23836931
uniprot
proteins
pubmed
28659595
uniprot
proteins
pubmed
6752952
uniprot
proteins
pubmed
7510321
uniprot
proteins
pubmed
7544804
uniprot
proteins
pubmed
7937880
uniprot
proteins
sequence_length
4660
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12519751, ECO:0000269|PubMed:18466341, ECO:0000269|PubMed:19202329, ECO:0000269|PubMed:6752952}; Single-pass type I membrane protein {ECO:0000255}. Endosome lumen {ECO:0000269|PubMed:17063000}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, dendrite {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, axon {ECO:0000250|UniProtKB:A2ARV4}. Note=Localizes to brush border membranes in the kidney (PubMed:12724130, PubMed:6752952). In the endolymphatic sac of the inner ear, located in the lumen of endosomes as a soluble form (PubMed:17063000). {ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:6752952}.
uniprot
proteins
transmembrane_region
TRANSMEM 4426..4446; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins