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Database: UniProt
Entry: A2ARV5_MOUSE
LinkDB: A2ARV5_MOUSE
Original site: A2ARV5_MOUSE 
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
//
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