ID L5LKG4_MYODS Unreviewed; 795 AA.
AC L5LKG4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Low-density lipoprotein receptor-related protein 8 {ECO:0000313|EMBL:ELK26737.1};
GN ORFNames=MDA_GLEAN10023995 {ECO:0000313|EMBL:ELK26737.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26737.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SIMILARITY: Belongs to the LDLR family.
CC {ECO:0000256|ARBA:ARBA00009939}.
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; KB110890; ELK26737.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LKG4; -.
DR eggNOG; KOG1215; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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; 4.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
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; PTHR22722:SF11; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2; 1.
DR PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 4.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 4.
DR PROSITE; PS51120; LDLRB; 4.
PE 3: Inferred from homology;
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|EMBL:ELK26737.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:ELK26737.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 281..320
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 367..413
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 414..456
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 457..500
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 501..545
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 647..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 81..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 88..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 100..115
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 120..132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 127..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 182..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 204..216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 211..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 223..238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 285..295
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 795 AA; 86903 MW; 6BBBEC9B78355948 CRC64;
MEGTPKLFDT DCVCPASSCQ GTACHPGIPP PLFADRGSPR APGLLHRPLS FTAGDPARCL
GCRVRGPSHA PSPRAGLAKE CEEDQFRCQN GRCIPSVWRC DEDDDCSDNS DEDDCPKKTC
MDTDFTCDNG HCIPERWKCD GEEECSDGSD EFQATCPKQV CPAEKLSCGP TSHKCVPASW
RCDGEKDCES GADEAGCATS LGTCRGDEFQ CGDGACVPAV KRCDQEQDCP DGSDEAGCLM
GLNECLHNNG GCSHICNDLK VGFECTCPAG YRLLDQKTCG DIDECEDPDA CSQICVNYKG
YFKCECHPGY EMDTLTKNCK AVAGRSPSLI FTNRHEVRRI DLVKRDYSRL IPMLKNVVAL
DVEVATNRIY WCDLSYRKIY SAYMDKASDP AEQEVLIDEQ LHSPEGLAVD WVHKHIYWTD
SGNKTISVAT VDGSRRRTLF SHDLSEPRAI AVDPLRGFMY WSDWGYQAKI EKSGLNGADR
HTLVSDDIEW PNGITLDLLS QRLYWVDSKL HQLSSIDFSG GHRKMLISSP HFLGHPFGVA
VFEDKVFWTD LENEAIFSAN RLTGLEISVL AENLNNPHDI VIFHELKQPR AGDACELSAL
PSGGCEYLCL PAPQLSSHSP KYTCACPDTM WLGPDMKRCY RAPQSTSTTA LASTTVRTEA
DSARGPGTAI HSPTHQNHST EMPRLAAAAP SSVTVPRASS IGPSTPSPAT SNHSQHYGNE
GGNTGSTVTA AVIGTIVPMV DYFALPEHCT KPATFLSNGI MKALAEMAFQ KQGKLKFHLF
TFDGMIIFTI DGDNL
//