ID A0A2K6UD35_SAIBB Unreviewed; 873 AA.
AC A0A2K6UD35;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Very low density lipoprotein receptor {ECO:0000313|Ensembl:ENSSBOP00000029793.1};
GN Name=VLDLR {ECO:0000313|Ensembl:ENSSBOP00000029793.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000029793.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000029793.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_003935703.1; XM_003935654.2.
DR AlphaFoldDB; A0A2K6UD35; -.
DR STRING; 39432.ENSSBOP00000029793; -.
DR Ensembl; ENSSBOT00000046676.1; ENSSBOP00000029793.1; ENSSBOG00000031091.1.
DR GeneID; 101050258; -.
DR CTD; 7436; -.
DR GeneTree; ENSGT00940000155460; -.
DR OrthoDB; 3918101at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; 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; 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.
PE 4: Predicted;
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..873
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014407273"
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; 96256 MW; 4D55154C3E85F038 CRC64;
MGTSARWALW LLLALCWGPR ESCATGTGRK AKCEASQFQC TNGRCITLLW KCDGDEDCVD
GSDEKNCVKK TCAESDFVCS NGQCVPSRWK CDGDPDCEDG SDETPEQCHM RTCRINEISC
GAHSTQCIPV SWRCDGENDC DSGEDEENCG NITCSPDEFT CSSGRCISRN FVCNGQDDCS
DGSDELDCAP PTCGTHEFQC STSSCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTKCP
ASEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI
RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ EQDCRDWSDE PLKECHINEC
LINNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE
CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA
QKLFWADLSQ KAIFSASIDD KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA
TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTVDIQ
WPNGITLDLI KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI
DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEEDM ENGGCEYLCL
PAPQINDHSP KYTCSCPSGY NLEENGRDCQ STATTVTYSE TKDTNTTEIS PTSGLVPGGI
NVTTAVSEVS VPPKGTSAAW AILPLLLLMM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT
TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA
//
