ID A0A0D9R9E9_CHLSB Unreviewed; 1451 AA.
AC A0A0D9R9E9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=LDL receptor related protein 5 {ECO:0000313|Ensembl:ENSCSAP00000005238.1};
GN Name=LRP5 {ECO:0000313|Ensembl:ENSCSAP00000005238.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005238.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005238.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005238.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; AQIB01078308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01078309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01078310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01078311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01078312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01078313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01078314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 60711.ENSCSAP00000005238; -.
DR Ensembl; ENSCSAT00000007050.1; ENSCSAP00000005238.1; ENSCSAG00000008983.1.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000156574; -.
DR OMA; HTPCEDN; -.
DR Proteomes; UP000029965; Chromosome 1.
DR Bgee; ENSCSAG00000008983; Expressed in adrenal cortex and 5 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR GO; GO:0042813; F:Wnt receptor activity; IEA:Ensembl.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:Ensembl.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0006865; P:amino acid transport; IEA:Ensembl.
DR GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0048539; P:bone marrow development; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0060764; P:cell-cell signaling involved in mammary gland development; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR GO; GO:1990963; P:establishment of blood-retinal barrier; IEA:Ensembl.
DR GO; GO:0035426; P:extracellular matrix-cell signaling; IEA:Ensembl.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0006007; P:glucose catabolic process; IEA:Ensembl.
DR GO; GO:0008078; P:mesodermal cell migration; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0110135; P:Norrin signaling pathway; IEA:Ensembl.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0061304; P:retinal blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
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; PTHR46513:SF16; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 5; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF14670; FXa_inhibition; 4.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00058; Ldl_recept_b; 12.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00135; LY; 17.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS51120; LDLRB; 12.
PE 4: Predicted;
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, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1222..1243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 1..42
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 43..85
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 134..173
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 221..263
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 264..306
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 307..350
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 351..393
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 440..477
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 523..565
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 566..608
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 609..651
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 652..693
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 741..778
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 915..959
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 960..1002
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1052..1090
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 1311..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1116..1131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1134..1146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1141..1159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1153..1168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1172..1184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1179..1197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1191..1206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1451 AA; 161574 MW; 15A255392F1A179B CRC64;
MYWTDWGETP RIERAGMDGS TRKIIVDSDI YWPNGLTIDL EEQKLYWADA KLSFIHRANL
DGSFRQKVVE GSLTHPFALT LSGDTLYWTD WQTRSIHACN KRTGGKRKEI LSALYSPMDI
QVLSQERQPF FHTRCEEDNG GCSHLCLLSP REPFYTCACP TGVQLQDNGR TCKAGAEEVL
LLARRTDLRR ISLDTPDFTD IVLQVDDIRH AIAIDYDPLE GYVYWTDDEV RAIRRAYLDG
SGAQTLVNTE INDPDGIAVD WVARNLYWTD TGTDRIEVTR LNGTSRKILV SEDLDEPRAI
ALHPVMGLMY WTDWGENPKI ECANLDGQER RVLVNASLGW PNGLALDLQE GKLYWGDAKT
DKIEVINVDG TKRRTLLEDK LPHIFGFTLL GDFIYWTDWQ RRSIERVHKV KASRDVIIDQ
LPDLMGLKAV NVAKVVGTNP CADRNGGCSH LCFFTPHATR CGCPIGLELL SDMKTCIVPE
AFLVFTSRAA IHRISLETNN NDVAIPLTGV KEASALDFDV SNNHIYWTDV SLKTISRAFM
NGSSVEHVVE FGLDYPEGMA VDWMGKNLYW ADTGTNRIEV ARLDGQFRQV LVWRDLDNPR
SLALDPTKGY IYWTEWGGKP RIVRAFMDGT NCMTLVDKVG RANDLTIDYA DQRLYWTDLD
TNMIESSNML GQERVVIADD LPHPFGLTQY SDYIYWTDWN LHSIERADKT SGRNRTLIQG
HLDFVMDILV FHSSRQDGLN DCMHNNGQCG QLCLAIPGGH RCGCASHHTL DPSSRNCSPP
TTFLLFSQKS AISRMIPDDQ HSPDLILPLH GLRNVKAIDY DPLDKFIYWV DGRQNIKRAK
DDGTQPFVLT SLSQGQNPDR QPHDLSIDIY SRTLFWTCEA TNTINVHRLS GEAMGVVLRG
DRDKPRAIVV NAERGYLYFT NMQDRAAKIE RAALDGTERE VLFTTGLIRP VALVVDNTLG
KLFWVDADLK RIESCDLSGA NRLTLEDANI VQPLGLTVLG KHLYWIDRQQ QMIERVEKTT
GDKRTRVQGR VAHLTGIHAV EEVSLEEFSA HPCARDNGGC SHICIAKGDG TPRCSCPVHL
VLLQNLLTCG EPPTCSPDQF ACATGEIDCI PGAWRCDGFP ECDDQSDEEG CPVCSAAQFP
CARGQCVDLR LRCDGEADCQ DRSDEADCDA ICLPNQFRCA SGQCVLIKQQ CDSFPDCIDG
SDELMCEITK PPSDDSPAHS SAIGPVIGII LSLFVMGGVY FVCQRVVCQR YAGANGPFPH
EYVSGTPHVP LNFIAPGGSQ HGPFTGIACG KSMMSSVSLM GGRGGVPLYD RNHVTGASSS
SSSSTKATLY PPILNPPPSP ATDPSLYNMD MFYSSNIPAT ARPYRPYIIR GMAPPTTPCS
TDVCDSDYSA SRWKASKYYL DLNSDSDPYP PPPTPHSQYL SAEDSCPPSP ATERSYFHLF
PPPPSPCTDS S
//
