ID F1LPV2_RAT Unreviewed; 873 AA. AC F1LPV2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 91. DE SubName: Full=Very low density lipoprotein receptor {ECO:0000313|Ensembl:ENSRNOP00000036229.2}; GN Name=Vldlr {ECO:0000313|Ensembl:ENSRNOP00000036229.2, GN ECO:0000313|RGD:3963}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000036229.2, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000036229.2, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000036229.2, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000036229.2} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000036229.2}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. 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 RefSeq; NP_037287.2; NM_013155.2. DR RefSeq; XP_006231259.1; XM_006231197.2. DR RefSeq; XP_006231260.1; XM_006231198.3. DR AlphaFoldDB; F1LPV2; -. DR SMR; F1LPV2; -. DR jPOST; F1LPV2; -. DR Ensembl; ENSRNOT00000035814.4; ENSRNOP00000036229.2; ENSRNOG00000027491.5. DR GeneID; 25696; -. DR KEGG; rno:25696; -. DR CTD; 7436; -. DR RGD; 3963; Vldlr. DR GeneTree; ENSGT00940000155460; -. DR HOGENOM; CLU_008163_2_0_1; -. DR OMA; DEYACKN; -. DR OrthoDB; 3918101at2759; -. DR TreeFam; TF351700; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000027491; Expressed in skeletal muscle tissue and 19 other cell types or tissues. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043235; C:receptor complex; IEA:Ensembl. DR GO; GO:0034185; F:apolipoprotein binding; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl. DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:UniProt. 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; 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; SSF57196; EGF/Laminin; 3. 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; 1. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS01209; LDLRA_1; 4. DR PROSITE; PS50068; LDLRA_2; 8. DR PROSITE; PS51120; LDLRB; 4. DR Genevisible; F1LPV2; RN. 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Receptor {ECO:0000256|ARBA:ARBA00023170}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..873 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003266019" FT TRANSMEM 798..819 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 193..205 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 200..218 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 873 AA; 96473 MW; 6E70D1E0CE12C291 CRC64; MGTSARWALW LLLALCWAPR DSGATASGKK AKCDSSQFQC TNGRCITLLW KCDGDEDCTD GSDEKNCVKK TCAESDFVCK NGQCVPNRWQ CDGDPDCEDG SDESPEQCHM RTCRINEISC GARSTQCIPE SWRCDGENDC DNGEDEENCG NITCSADEFT CSSGRCVSRN FVCNGQDDCD DGSDELDCAP PTCGAHEFQC STSSCIPLSW VCDDDADCSD QSDESLEQCG RQPVIHTKCP TSEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDITKVCDQ EQDCRDWSDE PLKECHINEC LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA QKLFWADLSQ KAIFSASIDD KVGRHFKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTEDIQ WPNGITLDLV KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIIYHELVQP SGKNWCEEDM ENGGCEYLCL PAPQINDHSP KYTCSCPNGY NLEENGRECQ STSTPVTYSE TKDVNTTDIL RTSGLVPGGI NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA //