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Database: UniProt
Entry: F7BW85_ORNAN
LinkDB: F7BW85_ORNAN
Original site: F7BW85_ORNAN 
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
//
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