ID F7BW85_ORNAN Unreviewed; 936 AA.
AC F7BW85;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Very low density lipoprotein receptor {ECO:0000313|Ensembl:ENSOANP00000023595.3};
GN Name=VLDLR {ECO:0000313|Ensembl:ENSOANP00000023595.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000023595.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000023595.3, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000023595.3,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000023595.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000023595.3};
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:PRU00076}.
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DR AlphaFoldDB; F7BW85; -.
DR STRING; 9258.ENSOANP00000023595; -.
DR Ensembl; ENSOANT00000023599.3; ENSOANP00000023595.3; ENSOANG00000014993.3.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000155460; -.
DR HOGENOM; CLU_008163_2_0_1; -.
DR InParanoid; F7BW85; -.
DR OMA; DEYACKN; -.
DR TreeFam; TF351700; -.
DR Proteomes; UP000002279; Chromosome X5.
DR Bgee; ENSOANG00000014993; Expressed in ovary and 7 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0034185; F:apolipoprotein binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0038025; F:reelin receptor activity; IEA:Ensembl.
DR GO; GO:0034189; F:very-low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IEA:Ensembl.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0034436; P:glycoprotein transport; IEA:Ensembl.
DR GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0021517; P:ventral spinal cord development; IEA:Ensembl.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 8.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
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; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 4.
PE 4: Predicted;
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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 861..882
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 419..458
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 459..494
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 544..589
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 590..632
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 633..676
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 677..721
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 96..108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 103..121
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 115..130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 135..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 142..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 197..212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 217..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 224..242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 236..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 256..268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 263..281
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 302..314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 309..327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 321..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 341..353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 348..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 360..375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 389..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 463..473
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 936 AA; 101946 MW; BD38F3658F6DF095 CRC64;
MRKLGIGSLG RPTGEPRGGG LRRSPPLYPL PDAPLRGAAS RSREDGAAAK LLGGRGGGGG
GSGAMGSSSP WGLGLLVALY CLCGELSSVH GAREKCEVSQ FQCSNGRCIT LLWKCDGDED
CSDGSDESSC VKKTCAESDF VCNNGQCVPN RWQCDGDPDC EDGSDESPEQ CHMRTCRINE
ISCGAGSTQC IPVSWKCDGE SDCDSEEDEE NCGNITCSTE EFTCFSGRCI SKNFVCNGHD
DCSDGSDELD CAPPTCGAHE FQCSTSSCIP SSWVCDNDPD CSDQSDESLE RCGRQPAPHA
KCPSSEIQCD SGECIHKKWR CDGDPDCKDG SDEINCPSRT CRPDQFKCED GNCIHGSRQC
NGVRDCVDGS DEVNCKNANQ CSGPGKFKCR SGECIDISKV CNQQQDCKDW SDEPLKECNI
NECLLNNGGC SHICKDLVIG YECDCAAGFE LIDRKTCGDI DECQNPGICS QICINLKGGY
KCECSRGYQM DLATGVCKAI GKEPSLIFTN RRDIRKIGLE RKEYIQLVEQ LRNTVALDAD
IAAQKLFWAD LSQKAIFSAS IDARDKVGRH VKMIDSVYNP AAIAVDWIYK NIYWTDVASK
TISVASLDGT KRKILFNSDL REPTSIAVDP LSGFAYWSDW GEPAKIEKAG MNGFDRRQLV
TTDIQWPNGI TLDLVKSRLY WLDSKLHMLS SVDLNGQDRR IVLKSLEFLA HPLAVTIFED
RVYWIDGENE AVYGANKFTG SELATLVNNL NDAQDIIVYH ELVQPSGKNW CDEDTPNGGC
EYLCLPAPQI NDHSPKYTCS CPSGYKLEDG GQGCRSTATV VYETRDTSTT EQSPTVGLIA
GGANVTTTVS EVSASPKGRS AVWAVLPVLL LTIAAAGGYF MWRNWQHKNM KSMNFDNPVY
LKTTEEDLTI DIGRHSTSVG HTYPAISVVS TDDDLA
//