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Database: UniProt
Entry: L5LKG4_MYODS
LinkDB: L5LKG4_MYODS
Original site: L5LKG4_MYODS 
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}.
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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
//
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