Lrp2
entrez
14725
canonical
uniprot
A2ARV4
canonical
ensembl
ENSMUSG00000027070
resolver
ensp
ENSMUSP00000079752
resolver
enst
ENSMUST00000080953
resolver
genesymbol
Lrp2
resolver
uniprot
P70215
resolver
uniprot
Q3TL35
resolver
uniprot
Q9JLB3
resolver
uniprot_entry
LRP2_MOUSE
resolver
uniprot_sec
P70215
resolver
uniprot_sec
Q3TL35
resolver
uniprot_sec
Q9JLB3
resolver
amino_acid_sequence
MERGAAAAAWMLLLAIAACLAPVSGQECGSGNFRCDNGYCIPASWRCDGTRDCLDDTDEIGCPPRSCGSGFFLCPAEGTCIPSSWVCDQDKDCSDGADEQQNCPGTTCSSQQLTCSNGQCVPIEYRCDHVSDCPDGSDERNCYYPTCDQLTCANGACYNTSQKCDHKVDCRDSSDEANCTTLCSQKEFQCGSGECILRAYVCDHDNDCEDNSDEHNCNYDTCGGHQFTCSNGQCINQNWVCDGDDDCQDSGDEDGCESNQRHHTCYPREWACPGSGRCISMDKVCDGVPDCPEGEDENNATSGRYCGTGLCSILNCEYQCHQTPYGGECFCPPGHIINSNDSRTCIDFDDCQIWGICDQKCESRQGRHQCLCEEGYILERGQHCKSNDSFSAASIIFSNGRDLLVGDLHGRNFRILAESKNRGIVMGVDFHYQKHRVFWTDPMQAKVFSTDINGLNTQEILNVSIDAPENLAVDWINNKLYLVETRVNRIDVVNLEGNQRVTLITENLGHPRGIALDPTVGYLFFSDWGSLSGQPKVERAFMDGSNRKDLVTTKLGWPAGITLDLVSKRVYWVDSRYDYIETVTYDGIQRKTVARGGSLVPHPFGISLFEEHVFFTDWTKMAVMKANKFTDTNPQVYHQSSLTPFGVTVYHALRQPNATNPCGNNNGGCAQICVLSHRTDNGGLGYRCKCEFGFELDADEHHCVAVKNFLLFSSQTAVRGIPFTLSTQEDVMVPVTGSPSFFVGIDFDAQHSTIFYSDLSKNIIYQQKIDGTGKEVITANRLQNVECLSFDWISRNLYWTDGGSKSVTVMKLADKSRRQIISNLNNPRSIVVHPAAGYMFLSDWFRPAKIMRAWSDGSHLMPIVNTSLGWPNGLAIDWSTSRLYWVDAFFDKIEHSNLDGLDRKRLGHVDQMTHPFGLTVFKDNVFLTDWRLGAIIRVRKSDGGDMTVVRRGISSIMHVKAYDADLQTGTNYCSQTTHPNGDCSHFCFPVPNFQRVCGCPYGMKLQRDQMTCEGDPAREPPTQQCGSSSFPCNNGKCVPSIFRCDGVDDCHDNSDEHQCGALNNTCSSSAFTCVHGGQCIPGQWRCDKQNDCLDGSDEQNCPTRSPSSTCPPTSFTCDNHMCIPKEWVCDTDNDCSDGSDEKNCQASGTCHPTQFRCPDHRCISPLYVCDGDKDCVDGSDEAGCVLNCTSSQFKCADGSSCINSRYRCDGVYDCKDNSDEAGCPTRPPGMCHPDEFQCQGDGTCIPNTWECDGHPDCIQGSDEHNGCVPKTCSPSHFLCDNGNCIYNSWVCDGDNDCRDMSDEKDCPTQPFHCPSSQWQCPGYSICVNLSALCDGVFDCPNGTDESPLCNQDSCLHFNGGCTHRCIQGPFGATCVCPIGYQLANDTKTCEDVNECDIPGFCSQHCVNMRGSFRCACDPEYTLESDGRTCKVTASENLLLVVASRDKIIMDNITAHTHNIYSLVQDVSFVVALDFDSVTGRVFWSDLLEGKTWSAFQNGTDKRVVHDSGLSLTEMIAVDWIGRNIYWTDYTLETIEVSKIDGSHRTVLISKNVTKPRGLALDPRMGDNVMFWSDWGHHPRIERASMDGTMRTVIVQEKIYWPCGLSIDYPNRLIYFMDAYLDYIEFCDYDGQNRRQVIASDLVLHHPHALTLFEDSVFWTDRGTHQVMQANKWHGRNQSVVMYSVPQPLGIIAIHPSRQPSSPNPCASATCSHLCLLSAQEPRHYSCACPSGWNLSDDSVNCVRGDQPFLISVRENVIFGISLDPEVKSNDAMVPISGIQHGYDVEFDDSEQFIYWVENPGEIHRVKTDGSNRTAFAPLSLLGSSLGLALDWVSRNIYYTTPASRSIEVLTLRGDTRYGKTLITNDGTPLGVGFPVGIAVDPARGKLYWSDHGTDSGVPAKIASANMDGTSLKILFTGNMEHLEVVTLDIQEQKLYWAVTSRGVIERGNVDGTERMILVHHLAHPWGLVVHGSFLYYSDEQYEVIERVDKSSGSNKVVFRDNIPYLRGLRVYHHRNAADSSNGCSNNPNACQQICLPVPGGMFSCACASGFKLSPDGRSCSPYNSFIVVSMLPAVRGFSLELSDHSEAMVPVAGQGRNVLHADVDVANGFIYWCDFSSSVRSSNGIRRIKPNGSNFTNIVTYGIGANGIRGVAVDWVAGNLYFTNAFVYETLIEVIRINTTYRRVLLKVSVDMPRHIVVDPKHRYLFWADYGQKPKIERSFLDCTNRTVLVSEGIVTPRGLAVDHDTGYIYWVDDSLDIIARIHRDGGESQVVRYGSRYPTPYGITVFGESIIWVDRNLRKVFQASKQPGNTDPPTVIRDSINLLRDVTIFDEHVQPLSPAELNNNPCLQSNGGCSHFCFALPELPTPKCGCAFGTLEDDGKNCATSREDFLIYSLNNSLRSLHFDPQDHNLPFQAISVEGMAIALDYDRRNNRIFFTQKLNPIRGQISYVNLYSGASSPTILLSNIGVTDGIAFDWINRRIYYSDFSNQTINSMAEDGSNRAVIARVSKPRAIVLDPCRGYMYWTDWGTNAKIERATLGGNFRVPIVNTSLVWPNGLTLDLETDLLYWADASLQKIERSTLTGSNREVVISTAFHSFGLTVYGQYIYWTDFYTKKIYRANKYDGSDLIAMTTRLPTQPSGISTVVKTQQQQCSNPCDQFNGGCSHICAPGPNGAECQCPHEGSWYLANDNKYCVVDTGARCNQFQFTCLNGRCISQDWKCDNDNDCGDGSDELPTVCAFHTCRSTAFTCANGRCVPYHYRCDFYNDCGDNSDEAGCLFRSCNSTTEFTCSNGRCIPLSYVCNGINNCHDNDTSDEKNCPPITCQPDFAKCQTTNICVPRAFLCDGDNDCGDGSDENPIYCASHTCRSNEFQCVSPHRCIPSYWFCDGEADCVDSSDEPDTCGHSLNSCSANQFHCDNGRCISSSWVCDGDNDCGDMSDEDQRHHCELQNCSSTEFTCINSRPPNRRCIPQHWVCDGDADCADALDELQNCTMRACSTGEFSCANGRCIRQSFRCDRRNDCGDYSDERGCSYPPCRDDQFTCQNGQCITKLYVCDEDNDCGDGSDEQEHLCHTPEPTCPPHQFRCDNGHCIEMGTVCNHVDDCSDNSDEKGCGINECQDSSISHCDHNCTDTITSFYCSCLPGYKLMSDKRTCVDIDECKETPQLCSQKCENVIGSYICKCAPGYIREPDGKSCRQNSNIEPYLVFSNRYYIRNLTIDGTSYSLILQGLGNVVALDFDRVEERLYWIDAEKQIIERMFLNKTNQETIISHRLRRAESLAVDWVSRKLYWLDAILDCLFVSDLEGRQRKMLAQHCVDANNTFCFENPRGIVLHPQRGYVYWADWGDHAYIARIGMDGTNKTVIISTKIEWPNAITIDYTNDLLYWADAHLGYIEFSDLEGHHRHTVYDGTLPHPFALTIFEDTVFWTDWNTRTVEKGNKYDGSGRVVLVNTTHKPFDIHVLHPYRQPIMSNPCATNNGGCSHLCLIKAGGRGFTCECPDDFQTVQLRDRTLCMPMCSSTQFLCGNNEKCIPIWWKCDGQKDCSDGSDESDLCPHRFCRLGQFQCRDGNCTSPQALCNARQDCADGSDEDRVLCEHHRCEANEWQCANKRCIPEYWQCDSVDDCLDNSDEDPSHCASRTCRPGQFKCNNGRCIPQSWKCDVDNDCGDYSDEPIHECMTAAYNCDNHTEFSCKTNYRCIPQWAVCNGFDDCRDNSDEQGCESVPCHPSGDFRCGNHHCIPLRWKCDGIDDCGDNSDEESCVPRECTESEFRCADQQCIPSRWVCDQENDCGDNSDERDCEMKTCHPEHFQCTSGHCVPKALACDGRADCLDASDESACPTRFPNGTYCPAAMFECKNHVCIQSFWICDGENDCVDGSDEEIHLCFNVPCESPQRFRCDNSRCIYGHQLCNGVDDCGDGSDEKEEHCRKPTHKPCTDTEYKCSNGNCVSQHYVCDNVDDCGDLSDETGCNLGENRTCAEKICEQNCTQLSNGGFICSCRPGFKPSTLDKNSCQDINECEEFGICPQSCRNSKGSYECFCVDGFKSMSTHYGERCAADGSPPLLLLPENVRIRKYNISSEKFSEYLEEEEHIQAIDYDWDPEGIGLSVVYYTVLSQGSQFGAIKRAYLPDFESGSNNPVREVDLGLKYLMQPDGLAVDWVGRHIYWSDAKSQRIEVATLDGRYRKWLITTQLDQPAAIAVNPKLGLMFWTDQGKQPKIESAWMNGEHRSVLASANLGWPNGLSIDYLNGDRIYWSDSKEDVIESIKYDGTDRRLIINDAMKPFSLDIFEDQLYWVAKEKGEVWRQNKFGKGNKEKLLVVNPWLTQVRIFHQLRYNQSVSNPCKQVCSHLCLLRPGGYSCACPQGSDFVTGSTVECDAASELPITMPSPCRCMHGGSCYFDENDLPKCKCSSGYSGEYCEIGLSRGIPPGTTMALLLTFAMVIIVGALVLVGFFHYRKTGSLLPSLPKLPSLSSLAKPSENGNGVTFRSGADVNMDIGVSPFGPETIIDRSMAMNEQFVMEVGKQPVIFENPMYAAKDSTSKVGLAVQGPSVSSQVTVPENVENQNYGRSIDPSEIVPEPKPASPGADETQGTKWNIFKRKPKQTTNFENPIYAEMDTEQKEAVAVAPPPSPSLPAKASKRSSTPGYTATEDTFKDTANLVKEDSDV
uniprot
proteins
function
FUNCTION: Multiligand endocytic receptor. Acts together with CUBN to mediate endocytosis of high-density lipoproteins (PubMed:10766831). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin (PubMed:22841573). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (PubMed:24825475). 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 (PubMed:10052453). Mediates renal uptake of metallothionein-bound heavy metals (By similarity). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (PubMed:18174160). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (PubMed:23825075). 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 (By similarity). Also mediates ShhN transcytosis (By similarity). 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 (PubMed:15623804). 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 (PubMed:22340494). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (PubMed:24639464). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (PubMed:20460439). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (PubMed:20637285). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (PubMed:22354480). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (PubMed:26439398). 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 (By similarity). Also mediates endocytosis of angiotensin 1-7 (By similarity). 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 (PubMed:26822476). Required for normal hearing, possibly through interaction with estrogen in the inner ear (PubMed:17846082). {ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98158, ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:10052453, ECO:0000269|PubMed:10766831, ECO:0000269|PubMed:15623804, ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:18174160, ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:20637285, ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480, ECO:0000269|PubMed:22841573, ECO:0000269|PubMed:23825075, ECO:0000269|PubMed:24639464, ECO:0000269|PubMed:24825475, ECO:0000269|PubMed:26439398, ECO:0000269|PubMed:26822476, ECO:0000269|PubMed:28659595}.
uniprot
proteins
mass_dalton
519208
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:0000250|UniProtKB:P98158}.; PTM: N-glycosylation is required for ligand binding. Contains core-fucosylated N-glycans in kidney proximal convoluted tubules (PCTs) and hybrid-type N-glycans in proximal straight tubules (PSTs). Interacts with ligands in a glycoform-dependent manner. Retinol-binding protein and the vitamin D carrier GC/DBP are endocytosed primarily by PCTs, albumin is endocytosed equally by PCTs and PSTs, and the aminoglycoside kanamycin is endocytosed primarily by PSTs. {ECO:0000269|PubMed:27773703}.
uniprot
proteins
protein_family
LDLR family
uniprot
proteins
pubmed
10052453
uniprot
proteins
pubmed
10766831
uniprot
proteins
pubmed
10772929
uniprot
proteins
pubmed
11247302
uniprot
proteins
pubmed
11964399
uniprot
proteins
pubmed
12724130
uniprot
proteins
pubmed
15467006
uniprot
proteins
pubmed
15623804
uniprot
proteins
pubmed
16099815
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16143106
uniprot
proteins
pubmed
16380466
uniprot
proteins
pubmed
17462596
uniprot
proteins
pubmed
17846082
uniprot
proteins
pubmed
18174160
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20460439
uniprot
proteins
pubmed
20637285
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22340494
uniprot
proteins
pubmed
22354480
uniprot
proteins
pubmed
22841573
uniprot
proteins
pubmed
23825075
uniprot
proteins
pubmed
24639464
uniprot
proteins
pubmed
24825475
uniprot
proteins
pubmed
26439398
uniprot
proteins
pubmed
26822476
uniprot
proteins
pubmed
27773703
uniprot
proteins
pubmed
28659595
uniprot
proteins
sequence_length
4660
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480}; Single-pass type I membrane protein {ECO:0000255}. Endosome lumen {ECO:0000250|UniProtKB:P98158}. Membrane, coated pit {ECO:0000269|PubMed:22340494}. Cell projection, dendrite {ECO:0000269|PubMed:20637285}. Cell projection, axon {ECO:0000269|PubMed:20637285}. Note=Localizes to brush border membranes in the kidney. In the endolymphatic sac of the inner ear, located in the lumen of endosomes as a soluble form. {ECO:0000250|UniProtKB:P98158}.
uniprot
proteins
transmembrane_region
TRANSMEM 4426..4446; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins