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Database: UniProt
Entry: A0A1S3FM54_DIPOR
LinkDB: A0A1S3FM54_DIPOR
Original site: A0A1S3FM54_DIPOR 
ID   A0A1S3FM54_DIPOR        Unreviewed;       900 AA.
AC   A0A1S3FM54;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Low-density lipoprotein receptor-related protein 8 {ECO:0000313|RefSeq:XP_012877653.1};
GN   Name=Lrp8 {ECO:0000313|RefSeq:XP_012877653.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012877653.1};
RN   [1] {ECO:0000313|RefSeq:XP_012877653.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012877653.1};
RG   RefSeq;
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}.
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DR   RefSeq; XP_012877653.1; XM_013022199.1.
DR   AlphaFoldDB; A0A1S3FM54; -.
DR   STRING; 10020.ENSDORP00000022053; -.
DR   GeneID; 105989929; -.
DR   KEGG; dord:105989929; -.
DR   CTD; 7804; -.
DR   InParanoid; A0A1S3FM54; -.
DR   OrthoDB; 3918101at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00112; LDLa; 5.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
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:SF3; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 8; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00057; Ldl_recept_a; 5.
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; 5.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF57424; LDL receptor-like module; 5.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 4.
DR   PROSITE; PS50068; LDLRA_2; 5.
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   Lipoprotein {ECO:0000313|RefSeq:XP_012877653.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_012877653.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
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}.
FT   TRANSMEM        755..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          302..341
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          388..434
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          435..477
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          478..521
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          522..566
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        60..72
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        67..85
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        79..94
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        99..111
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        106..124
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        161..176
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        184..196
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        191..209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        203..218
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        232..250
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        306..316
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   900 AA;  99049 MW;  AB229C9596480105 CRC64;
     MGRPARGALR PCSSSISRRR RRRRIRCLTA KVRSASPGPG SAPPTKRGLE VGARGPAKEC
     EVDQFRCRNG RCIPSVWRCD EDDDCSDNSD EDDCPKKTCA DSDFTCDNGH CIPERWKCDG
     EEECPDGSDE WKATCTRQVC PAEKLSCGPT SHKCVPASWR CDGEKDCEGG ADEAGCATSA
     VGACGGDEFQ CGDGTCVLAI KRCNQEQDCP DGSDEAGCLQ ESTCEGPRRF QCKSGECVDS
     GKVCDAQRDC RDWSDELLKE CGLNECLHNN GGCSHICTDL KIGFECTCPA GFRLLDQKTC
     GDIDECEDPD ACSQICVNYK GYFKCECHPG YEMDALTKNC KAVAGKSPSL IFTNRHEVRR
     IDLVKRDYSR LIPMLKNVVA LDVEVVTNRI YWCDLSYRKI YSAYMDKASD PAEQEVLIDE
     QLHSPEGLAV DWVHKHIYWT DSGNKTISVA TVDGGRRCTL FNRDLSEPRA IAVDPLRGFM
     YWSDWGYQAK IEKSGLNGVD RQTLVSDNIE WPNGIALDLL NQRLYWVDSK LHQLSSIDFS
     GGNRKMLIFS TDFLSHPFGI AVFEDKVFWT DLENEAIFSA NRLNGLEISI LAENLNNPHD
     IVIFHELKQP RAADACELSA QPNGGCEYLC LPAPQIFSHS PKYTCACPDT MWLGPDMKRC
     YRTPQSTSTT TTTTTTSTPT TTRAVPVTTG APGTSHGPTS QNHSTTTASP AAAGPSSVSG
     PRAPSISLST PSPATSNHSQ HYGNEDDKMG STVTAAVIGI IVPIAVIALL CMSGYLIWRN
     WKRKNTKSMN FDNPVYRKTT EEEDEDELHI GRTTQIGHVY PAAISSFDRP LWAEPCVGET
     RELEDPAPAL KELFVLPGEP RSQLHQLPKN PLSELPVVKC KVAHWCSLVL ALGPVSLMVS
//
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