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Database: UniProt
Entry: H9YWX0_MACMU
LinkDB: H9YWX0_MACMU
Original site: H9YWX0_MACMU 
ID   H9YWX0_MACMU            Unreviewed;       860 AA.
AC   H9YWX0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Low-density lipoprotein receptor isoform 1 {ECO:0000313|EMBL:AFH28186.1};
GN   Name=LDLR {ECO:0000313|EMBL:AFH28186.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFH28186.1};
RN   [1] {ECO:0000313|EMBL:AFH28186.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Thymus {ECO:0000313|EMBL:AFH28186.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
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:PRU00076}.
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DR   EMBL; JU471382; AFH28186.1; -; mRNA.
DR   AlphaFoldDB; H9YWX0; -.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00112; LDLa; 7.
DR   Gene3D; 4.10.1220.10; EGF-type module; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
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; 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   PANTHER; PTHR22722:SF11; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2; 1.
DR   PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 2.
DR   Pfam; PF00057; Ldl_recept_a; 7.
DR   Pfam; PF00058; Ldl_recept_b; 5.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 7.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 7.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 3.
DR   PROSITE; PS50068; LDLRA_2; 7.
DR   PROSITE; PS51120; LDLRB; 4.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipoprotein {ECO:0000313|EMBL:AFH28186.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:AFH28186.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..860
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003623420"
FT   TRANSMEM        787..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          354..393
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          439..485
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          486..528
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          529..572
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          573..617
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DISULFID        27..39
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        34..52
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        89..104
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        109..121
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        116..134
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        128..143
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        148..160
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        155..173
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        197..209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        204..222
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        216..231
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        236..248
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        243..261
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        255..270
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        284..302
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        358..368
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   860 AA;  95506 MW;  4E3C9C25DFBD3125 CRC64;
     MGPWGWKLRW TVAFLLAAAE AAVGDRCERN EFQCEDGKCI SYKWVCDGTA ECQDGSDESQ
     ETCLSVTCKS GDFSCGGRVN RCIPQFWRCD GEVDCENGSD EQDCPPKTCS QDEFRCHDGK
     CIYRQFVCDS DRDCLDGSDE ASCPVLTCGP ASFQCNSSTC IPQLWACDND PDCEDGSDEW
     PQHCQGLEVP KRDSSPCSAF EFHCRSGECI HSGWRCDGGP DCKDKSDEEN CPVATCRPDE
     FQCSDGTCIH GSRQCDREYD CKDMSDEVGC INVTLCEGPN KFKCHSGECI SLDKVCNMAR
     DCRDWSDEPI KECGTNECLD NNGGCSHICN DLKIGYECLC PDGFQLVAQR RCEDIDECQD
     PDTCSQLCVN LEGSYKCQCE EGFQLDPHTK ACKAVGSIAY LIFTNRHEVR KMTLDRSEYT
     SLIPNLRNVV ALDTEVASNR IYWSDLSQRM IYSTQLDRAH SVSSYDTVIS RDLQAPDGLA
     VDWIHSNIYW TDSVLGTVSV ADTKGVKRKT LFRENGSKPR AIVVDPVHGF MYWTDWGTPA
     KIKKGGLNGV DIYSLVTENI EWPNGITLDF PSGRLYWVDS KLHSISSIDV NGGNRKTVLE
     DKERLAHPFS LAIFEDKVFW TDIINEAIFS ANRLTGSDIN LLAENLLSPE DMVLFHNLTQ
     PRGVNWCERT TLSNGGCQYL CLPAPQINPQ SPKFTCTCPD GMLLAKDMRS CLTEAEAAVA
     TQETSTVRLM VSSKAVATQH TTTRPVPNTS QLPGATPGLT TAETVTMSHQ ALGDVAGRGN
     EKKPKSVGAL SIVLPTVLLV FLCLGAFLLW KNWRLKSINS INFDNPVYQK TTEDEVHICR
     NQDGYSYPSR QMVSLEDDVA
//
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