ID O77505_BOVIN Unreviewed; 845 AA.
AC O77505;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1999, sequence version 2.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=Very low density lipoprotein receptor VLDL-R2 {ECO:0000313|EMBL:AAD03484.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAD03484.1};
RN [1] {ECO:0000313|EMBL:AAD03484.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9799803;
RA Magrane J., Reina M., Pagan R., Luna A., Casaroli-Marano R.P., Angelin B.,
RA Gafvels M., Vilaro S.;
RT "Bovine aortic endothelial cells express a variant of the very low density
RT lipoprotein receptor that lacks the O-linked sugar domain.";
RL J. Lipid Res. 39:2172-2181(1998).
RN [2] {ECO:0000313|EMBL:AAD03484.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10356983; DOI=10.1016/S0014-5793(99)00494-9;
RA Magrane J., Casaroli-Marano R.P., Reina M., Gafvels M., Vilaro S.;
RT "The role of O-linked sugars in determining the very low density
RT lipoprotein receptor stability or release from the cell.";
RL FEBS Lett. 451:56-62(1999).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF016537; AAD03484.1; -; mRNA.
DR RefSeq; NP_776914.1; NM_174489.2.
DR AlphaFoldDB; O77505; -.
DR GeneID; 282123; -.
DR KEGG; bta:282123; -.
DR CTD; 7436; -.
DR OrthoDB; 3918101at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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; 2.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 6.
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; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 4.
PE 2: Evidence at transcript level;
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
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 metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipoprotein {ECO:0000313|EMBL:AAD03484.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:AAD03484.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
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 SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..845
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004159880"
FT TRANSMEM 770..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 396..431
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 481..524
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 525..567
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 568..611
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 612..656
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 33..45
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 40..58
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 52..67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 72..84
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 79..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 134..149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 154..166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 161..179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 173..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 246..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 258..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 278..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 285..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 297..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 326..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 400..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 845 AA; 93299 MW; 2849300E4679C639 CRC64;
MGTSARWALW LLLALCWAPR ESGATGAGRK AKCEANQFQC TNGRCITLLW KCDGDEDCTD
GSDEKNCVKK TCAESDFVCN NGQCVPNRWQ CDGDPDCEDG SDESPEQCHM RTCRINEISC
GARSTQCIPV SWRCDGENDC YSGEDEENCG NVTCSSDEFT CSSGRCISRN FMCNGQDDCS
DGSDELDCAP PTVGPTSSSA APPPCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTRCP
ASEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI
RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ KQDCRDWSDE PLKECHVNEC
LVNNGGCSHI CKDLVIGYEC YCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE
CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA
QKLFWADLSQ KAIFSASIDD KVVRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA
TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRALVTADIQ
WPNGITLDLI KGRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI
DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEEDV ENGGCEYLCL
PAPQINDHSP KYTCSCPNGY NLEDNGRECH RINVTTAVSE VSVPPKGTSA AWAILPLLLS
AMAAVGGYLM WRNWQHKNMK SMNFDNPVYL KTTEENLSID IGRHSASVGH TYPAISVVST
DDDLA
//
