ID A2ARV5_MOUSE Unreviewed; 1363 AA.
AC A2ARV5;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE SubName: Full=Low density lipoprotein receptor-related protein 2 {ECO:0000313|Ensembl:ENSMUSP00000097628.3};
GN Name=Lrp2 {ECO:0000313|Ensembl:ENSMUSP00000097628.3,
GN ECO:0000313|MGI:MGI:95794};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000097628.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000097628.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000097628.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000097628.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000097628.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the LDLR family.
CC {ECO:0000256|ARBA:ARBA00009939}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR SMR; A2ARV5; -.
DR jPOST; A2ARV5; -.
DR MaxQB; A2ARV5; -.
DR PeptideAtlas; A2ARV5; -.
DR ProteomicsDB; 364014; -.
DR Antibodypedia; 962; 421 antibodies from 35 providers.
DR Ensembl; ENSMUST00000100051.9; ENSMUSP00000097628.3; ENSMUSG00000027070.15.
DR UCSC; uc008jyd.1; mouse.
DR AGR; MGI:95794; -.
DR MGI; MGI:95794; Lrp2.
DR VEuPathDB; HostDB:ENSMUSG00000027070; -.
DR GeneTree; ENSGT00940000157232; -.
DR HOGENOM; CLU_268220_0_0_1; -.
DR OMA; GKTVIHG; -.
DR ChiTaRS; Lrp2; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000027070; Expressed in vestibular membrane of cochlear duct and 140 other cell types or tissues.
DR ExpressionAtlas; A2ARV5; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 15.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 15.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
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 PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR Pfam; PF00057; Ldl_recept_a; 14.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00192; LDLa; 15.
DR SMART; SM00135; LY; 10.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 14.
DR SUPFAM; SSF63825; YWTD domain; 2.
DR PROSITE; PS01209; LDLRA_1; 8.
DR PROSITE; PS50068; LDLRA_2; 15.
DR PROSITE; PS51120; LDLRB; 6.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Proteomics identification {ECO:0007829|MaxQB:A2ARV5,
KW ECO:0007829|PeptideAtlas:A2ARV5}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1363
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002642750"
FT DOMAIN 107..143
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 310..346
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 347..385
FT /note="EGF-like calcium-binding"
FT /evidence="ECO:0000259|SMART:SM00179"
FT DOMAIN 350..385
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 435..477
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 478..520
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 521..567
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 568..612
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 661..704
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 795..836
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 881..924
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 972..1013
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1065..1102
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1134..1176
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DISULFID 28..40
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 35..53
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 47..62
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 108..120
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 115..133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 127..142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 152..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 164..179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 183..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 190..208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 202..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 222..234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 229..247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 241..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1025..1037
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1032..1050
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1044..1059
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1086..1101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1110..1122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1117..1135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1129..1144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1150..1162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1157..1175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1169..1184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1208..1223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1272..1284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1279..1297
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1291..1306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1363 AA; 150683 MW; 8A2A0742C72AE006 CRC64;
MERGAAAAAW MLLLAIAACL APVSGQECGS GNFRCDNGYC IPASWRCDGT RDCLDDTDEI
GCPPRSCGSG FFLCPAEGTC IPSSWVCDQD KDCSDGADEQ QNCPGTTCSS QQLTCSNGQC
VPIEYRCDHV SDCPDGSDER NCYYPTCDQL TCANGACYNT SQKCDHKVDC RDSSDEANCT
TLCSQKEFQC GSGECILRAY VCDHDNDCED NSDEHNCNYD TCGGHQFTCS NGQCINQNWV
CDGDDDCQDS GDEDGCESNQ RHHTCYPREW ACPGSGRCIS MDKVCDGVPD CPEGEDENNA
TSGRYCGTGL CSILNCEYQC HQTPYGGECF CPPGHIINSN DSRTCIDFDD CQIWGICDQK
CESRQGRHQC LCEEGYILER GQHCKSNDSF SAASIIFSNG RDLLVGDLHG RNFRILAESK
NRGIVMGVDF HYQKHRVFWT DPMQAKVFST DINGLNTQEI LNVSIDAPEN LAVDWINNKL
YLVETRVNRI DVVNLEGNQR VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA
FMDGSNRKDL VTTKLGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
PHPFGISLFE EHVFFTDWTK MAVMKANKFT DTNPQVYHQS SLTPFGVTVY HALRQPNATN
PCGNNNGGCA QICVLSHRTD NGGLGYRCKC EFGFELDADE HHCVAVKNFL LFSSQTAVRG
IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ HSTIFYSDLS KNIIYQQKID GTGKEVITAN
RLQNVECLSF DWISRNLYWT DGGSKSVTVM KLADKSRRQI ISNLNNPRSI VVHPAAGYMF
LSDWFRPAKI MRAWSDGSHL MPIVNTSLGW PNGLAIDWST SRLYWVDAFF DKIEHSNLDG
LDRKRLGHVD QMTHPFGLTV FKDNVFLTDW RLGAIIRVRK SDGGDMTVVR RGISSIMHVK
AYDADLQTGT NYCSQTTHPN GDCSHFCFPV PNFQRVCGCP YGMKLQRDQM TCEGDPAREP
PTQQCGSSSF PCNNGKCVPS IFRCDGVDDC HDNSDEHQCG ALNNTCSSSA FTCVHGGQCI
PGQWRCDKQN DCLDGSDEQN CPTRSPSSTC PPTSFTCDNH MCIPKEWVCD TDNDCSDGSD
EKNCQASGTC HPTQFRCPDH RCISPLYVCD GDKDCVDGSD EAGCVLNCTS SQFKCADGSS
CINSRYRCDG VYDCKDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE CDGHPDCIQG
SDEHNGCVPK TCSPSHFLCD NGNCIYNSWV CDGDNDCRDM SDEKDCPTQP FHCPSSQWQC
PGYSICVNLS ALCDGVFDCP NGTDESPLCS KFPDHSLLDT NLF
//