ID W5MM69_LEPOC Unreviewed; 859 AA.
AC W5MM69;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Low density lipoprotein receptor {ECO:0000313|Ensembl:ENSLOCP00000009478.1};
GN Name=LDLR {ECO:0000313|Ensembl:ENSLOCP00000009478.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009478.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009478.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AHAT01007645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015204644.1; XM_015349158.1.
DR AlphaFoldDB; W5MM69; -.
DR SMR; W5MM69; -.
DR STRING; 7918.ENSLOCP00000009478; -.
DR Ensembl; ENSLOCT00000009489.1; ENSLOCP00000009478.1; ENSLOCG00000007795.1.
DR GeneID; 102688974; -.
DR KEGG; loc:102688974; -.
DR CTD; 3949; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000161046; -.
DR HOGENOM; CLU_008163_2_0_1; -.
DR InParanoid; W5MM69; -.
DR OMA; GSRQCNK; -.
DR OrthoDB; 3918101at2759; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000007795; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0071813; F:lipoprotein particle binding; IBA:GO_Central.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IBA:GO_Central.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IBA:GO_Central.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
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:SF66; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 2.
DR Pfam; PF00057; Ldl_recept_a; 7.
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; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
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; 7.
DR PROSITE; PS51120; LDLRB; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
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:UP000018468};
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}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..859
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004867969"
FT TRANSMEM 786..807
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..359
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 445..491
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 492..534
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 535..578
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 579..623
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 719..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 32..44
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 39..57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 94..109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 114..126
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 121..139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 133..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 153..165
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 160..178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 203..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 210..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 222..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 242..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 249..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 261..276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 290..308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 859 AA; 94312 MW; 7FAFD2E9EF9010D6 CRC64;
MFASRQQRTL PALALLLVVL NHVVTPTLSA TCSAGLFQCA NEKCITTRWV CDGTDDCGDG
SDEVTSVCMA KTCKPSEFSC GGRLNQCVPS GWRCDGKKDC ENGADEESCA PRECADDEFR
CRNGNCVSVS FVCDEEDDCE DGSDEASCPA PTCGPASFQC NNSVCVPRLW ACDGDADCAD
GSDEGPAACG GQAGPAPPHA ARCSPLEFQC GGGQCIHSSW RCDGSNDCPD HSDEDNCIKP
TCSPDEFQCS DGACIHGSRQ CDKEYDCKDL SDELGCSNVT KCEGPSKFRC RSGECIGVDK
VCDRQRDCRD WSDEPVKECD NNECLINNGG CSHTCNDLKI GFECLCPEGF HLVDKKRCED
IDECANPDTC SQICVNLEGS YKCECEEGYQ IDPVTKSCKA IGTVAYLFFT NRHEVRKMTL
DRSEYTRLIP RLKNVVALDM EIPSNKIYWS DLSQKKIYST HMDKAGNSSH HSTVIESGIE
APEGIAVDWI HGNIYWTDSV FGTISVATTD GHRRKTLISE RLARPRAIVV DPVHNFMYWT
DWGTPAKIEK GGLNGVDRVP LVTENIEWPN GITLDLLNQR LYWVDSKLHS LSSIDVRGGN
RREVIMDEEK LAHPFSLTVF EEKVFWTDIE NSAILSANRL TGGDIVAVVE NVALPEDIVL
YHNLKQPTGE NWCESGKLPN GGCEYLCLPA PQINRHSAKY TCACPDHLTL GPDMRKCVPV
SSEPKTSTAK PPATPTASPR TPPARPDNTA RPTARPTAQD VVTLSQIDAR NGVAAEATEV
HSSPTALYIV IPIVILCLMA FGGVLLWRNW RLKNTNSINF DNPVYQKTTE DEVHICRSQS
QEGYSYPSRQ MVSLEEDLA
//
