ID E9Q202_MOUSE Unreviewed; 3357 AA.
AC E9Q202;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Low density lipoprotein-related protein 1B {ECO:0000313|Ensembl:ENSMUSP00000129192.3};
GN Name=Lrp1b {ECO:0000313|Ensembl:ENSMUSP00000129192.3,
GN ECO:0000313|MGI:MGI:2151136};
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:ENSMUSP00000129192.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000129192.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000129192.3,
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:ENSMUSP00000129192.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000129192.3};
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; E9Q202; -.
DR ProteomicsDB; 351021; -.
DR Antibodypedia; 33599; 75 antibodies from 18 providers.
DR Ensembl; ENSMUST00000167270.5; ENSMUSP00000129192.3; ENSMUSG00000049252.18.
DR AGR; MGI:2151136; -.
DR MGI; MGI:2151136; Lrp1b.
DR VEuPathDB; HostDB:ENSMUSG00000049252; -.
DR GeneTree; ENSGT00940000157521; -.
DR HOGENOM; CLU_000085_2_1_1; -.
DR OMA; GRDEFHC; -.
DR ChiTaRS; Lrp1b; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000049252; Expressed in animal zygote and 69 other cell types or tissues.
DR ExpressionAtlas; E9Q202; baseline and differential.
DR Genevisible; E9Q202; MM.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00112; LDLa; 20.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 22.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 7.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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 InterPro; IPR032485; LRP1-like_beta_prop.
DR PANTHER; PTHR22722:SF5; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 1B; 1.
DR PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF16472; DUF5050; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 4.
DR Pfam; PF00057; Ldl_recept_a; 21.
DR Pfam; PF00058; Ldl_recept_b; 9.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00192; LDLa; 22.
DR SMART; SM00135; LY; 33.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 22.
DR SUPFAM; SSF63825; YWTD domain; 7.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS01209; LDLRA_1; 11.
DR PROSITE; PS50068; LDLRA_2; 22.
DR PROSITE; PS51120; LDLRB; 20.
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:E9Q202,
KW ECO:0007829|PeptideAtlas:E9Q202}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 64..79
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 181..223
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 224..267
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 454..496
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 497..542
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 543..592
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 593..636
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1186..1232
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1233..1275
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1276..1322
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1323..1367
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1504..1546
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1591..1630
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1808..1850
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1851..1893
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1894..1937
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1938..1981
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 2216..2260
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 2261..2303
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 2837..2852
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 2985..3027
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 3028..3071
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 731..743
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 738..756
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 772..784
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 779..797
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 813..825
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 820..838
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 861..879
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 873..888
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 892..904
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 899..917
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 959..974
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1002..1017
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2404..2422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2438..2450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2445..2463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2457..2472
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2477..2489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2484..2502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2496..2511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2545..2560
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2568..2580
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2575..2593
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2587..2602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2606..2618
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2613..2631
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2691..2703
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2698..2716
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2731..2743
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2777..2789
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2784..2802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2796..2811
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3203..3215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3210..3228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3243..3255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3250..3268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3262..3277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3302..3317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3342..3357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 3357 AA; 376338 MW; 16C69D489B7C952B CRC64;
ELLPSCQQLN CQFKCAMVRN ATRCYCEDGF EVAEDGRSCK DQDECSIYGI CSQTCKNTYG
SYACSCVEGY IMQSDNRSCK VKHEPTDKAP MLLISSLETI ELFYINGSKM TTLSSANRNE
IHTLDFIYSE EMICWIESRE SSNQLKCGQI TKAGRLTDQR IINSLQSFQN VEQMAFDWLT
RNIYFVDHVS DRIFVCNFNG SVCVTLIESE LHNPKAIAAD PIAGKLFFTD YGNVPKIERC
DLDGMNRTRI VYSKAEQPSA LALDLVNRLV YWVDLYLDYV GVVDYQGKNR HTIVQGRQVK
HLYGITVFED YLYATSSDNF NIIRINRFNG TDIHSIIKME SARGIRTYQK RTQPTVRSHA
CEVDAYGMPG GCSHICLLSS SYKTRTCRCR TGFNMGSDGR SCKRPKNELF LFYGKGRPGI
VRGMDLNTKI ADECMIPIEN LVNPRALDFH AEANYIYFAD TTSFLIGRQK IDGTERETIL
KDDLDNVEGI AVDWIGNNLY WTNDGHRKTI NVARLEKASQ SRKTLLEGGM SHPRAIVVDP
VNGWMYWTDW KEDKIDDSVG RIEKAWMDGV NRQVFVTSKM LWPNGLTLDF HTSTLYWCDA
YYDHIEKVFL NGTHRKVVYS GKELNHPFGL SHHGNYVFWT DYMNGSIFQL DLMTNEVTLL
RHERAPLFGL QIYDPRKQQG DNMCRINNGG CGTLCLAIPA GRVCACADNQ LLDENGTTCT
FNPEEIRFHI CKPGEFRCKN KHCIQARWKC DGDDDCLDGS DEDSVTCFNH SCPDDQFKCQ
NNRCIPKRWL CDGANDCGSN EDESNQTCTA RTCQADQFSC GNGRCIPTAW LCDREDDCGD
QTDEVASCEF PTCEPLTQFI CKSGRCISNK WHCDTDDDCG DRSDEVGCVH SCLDDQFRCS
SGRCIPGHWA CDGDNDCGDF SDETHINCTK EEARSPAGCI GNEFQCRPDG NCIPDLWRCD
GEKDCEDGSD EKGCNGTIRL CDHKTKFSCR STGRCINNAW VCDGDVDCED QSDEEDCDSF
LCGPPKYPCA NDTSVCLQPE KLCNGRKDCP DGSDEGDLCD ECSLNNGGCS NHCSVVPGRG
IVCSCPEGHQ LKKDNRTCEI VDYCASHLRC SQVCEQQKHM VKCSCYEGWA LGTDGESCTS
VDSFEAFIIF SIRHEIRRID LHKGDYSLLV PGLRNTIALD FHFNQSLLYW TDVVEDRIYR
GKLSESGGVS AIEVVVEHGL ATPEGLTVDW IAGNIYWIDS NLDQIEVSKL DGSLRATLIA
GAMEHPRAIA LDPRYGILFW TDWDANFPRI ESASMSGAGR KTIYKDMKTG AWPNGLTVDH
FERRIVWTDA RSDAIYSAFY DGTNMIEIIR GHEYLSHPFA VSLYGSEVYW TDWRTNTLAK
ANKWTGQNVS VIQKTSAQPF DLQIYHPSRQ PQAPNPCAAN EGRGPCSHLC LINHNRSAAC
ACPHLMKLSS DKKTCYEMKK FLLYARRSEI RGVDIDNPYV NFITAFTVPD IDDVAVIDFD
ASEERLYWTD IKTQTITRAF INGTGLETVI SRDIQSIRGL AVDWVSRNLY WISSEFDETQ
INVARLDGSL KTSIIHGIDK PQCLAAHPVR GKLYWTDGNT INMANMDGSN SKILFQNQKE
PVGLSIDYVE NKLYWISSGN GTINRCNLDG GNLEVIESMK EELTKATALT IMDKKLWWAD
QNLAQLGTCN KRDGRNPSIL RNKTSGVVHM KVYDKEAQQG SNSCQVNNGG CSQLCLPTSE
TTRTCMCTVG YYLQKNRMSC QGIESFLMYS VHEGIRGIPL EPRDKVDALM PISGAAFAVG
IDFHAENDTI YWTDMGLNKI SRAKRDQTWK EDVVTNGLGR VEGIAVDWIA GNIYWTDHGF
NLIEVARLNG SFRYVIISQG LDQPRSIAVH PEKGFLFWTE WGQVPCIGKA RLDGSEKVMI
VSVGITWPNG ISIDYEENKL YWCDARSDKI ERIDLDTGAN REVLLSGSNV DLFSVAVFGA
YIYWSDRAHA NGSVRRGHKN DATETVTMRT GLGVNLKEIK IFNRVREKGT NVCAKENGGC
QQLCLYRGNS RRTCACAHGY LAGDGVTCLR HEGYLLYSGR TILKSIHLSD ETNLNSPVRP
YENPNYFKNI IALAFDYNQR REGTNRIFYS DAHFGNIQLI KDNWEDRQVI VENVGSVEGL
AYHRAWDTLY WTSSSTSSIT RHTVDQTRPG AIDREAVITM SEDDHPHVLA LDECQNLMFW
TNWNEQHPSI MRATLTGKNA HVVVSTDILT PNGLTIDHRA EKLYFSDGSL GKIERCEYDG
SQRHVIVKSG PGTFLSLAVY DSYIFWSDWG RRAILRSNKY TGGETKILRS DIPHQPMGII
AVANDTNSCE LSPCALLNGG CHDLCLLTPD GRVNCSCRGD RVLLANNRCV TKNSSCNIYS
EFECGNGDCV DYVLTCDGIP HCKDKSDEKL LYCENRSCRS GFKPCYNRRC VPHGKLCDGT
NDCGDSSDEL DCKVSTCSTV EFRCADGTCI PRSARCNQNM DCSDASDEKG CNNTDCTHFY
KLGVKSTGFI RCNSTSLCVL PSWICDGSND CGDYSDELKC PVQNKHKCEE NYFGCPSGRC
ILNTWVCDGQ KDCEDGLDEL HCDSSCSWNQ FACSVKKCIS KHWICDGEDD CGDSLDESDS
ICGAVTCAAD MFSCQGSHAC VPQHWLCDGE RDCPDGSDEL SSAGCAPNNT CDENAFMCHN
KVCIPKQFVC DHDDDCGDGS DEFLQCGYRQ CGPEEFRCAD GRCLVNTLWQ CDGDFDCPDS
SDEAPINPRC RSAEHSCNSS FFMCKNGRCI PSDGLCDIRD DCGDGSDETN CHINECLSKK
ISGCSQDCQD LPVSYKCKCW PGFQLKDDGK TCVDIDECSS GFPCSQQCIN TYGTYKCHCA
EGYETQPDNP NGCRSLSDEE PFLILADQHE IRKISTDGSN YTLLKQGLNN VIALDFDYRE
EFIYWIDSSR PNGSRINRMC LNGSDIKVVH NTAVPNALAV DWIGKNLYWS DTEKRIIEVS
KLNGLYPTVL VSKRLKFPRD LSLDPRAGNL YWIDCCEYPH IGRVGMDGTN QSVVIETKIS
RPMALTIDYV NHRLYWADEN HIEFSNMDGS HRHKVPNQDI PGVIALTLFE DYIYWTDGKT
KSLSRVHKTS GADRLSLINS WHAITDIQVY HSYRQPDVSK HLCTVNNGGC SHLCLLGPGK
THTCACPTNF YLAADNRTCL SNCTASQFRC KTDKCIPFWW KCDTVDDCGD GSDEPDDCPE
FKCQPGRFQC GTGLCALPAF ICDGENDCGD NSDELNCDTH VCLAGQFKCT KNKKCIPVNL
RCNGQDDCGD EEDEKDCPEN SCSPDYFQCK TTKHCISKLW VCDEDPDCAD ASDEANC
//
