ID A0A3Q1JNQ6_ANATE Unreviewed; 865 AA.
AC A0A3Q1JNQ6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Low density lipoprotein receptor a {ECO:0000313|Ensembl:ENSATEP00000016411.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000016411.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000016411.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of
CC plasma, and transports it into cells by endocytosis. In order to be
CC internalized, the receptor-ligand complexes must first cluster into
CC clathrin-coated pits. {ECO:0000256|ARBA:ARBA00037220}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3Q1JNQ6; -.
DR Ensembl; ENSATET00000016691.2; ENSATEP00000016411.2; ENSATEG00000011318.2.
DR GeneTree; ENSGT00940000154819; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
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; 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:SF21; LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 3.
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; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 4.
PE 4: Predicted;
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
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 LDL {ECO:0000256|ARBA:ARBA00022710};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 787..806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 317..356
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 442..488
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 489..531
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 532..575
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 576..620
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 95..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 115..127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 122..140
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 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 287..305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 865 AA; 95625 MW; 137B488DB10EB30F CRC64;
MGIKSSKFSC SAVFCLKSNG FLCGVHTYAL TTCGTNQFQC GNGKCITVRW VCDGTDDCGD
GTDELPGTCS VKTCRPTEFS CADRLNQCIP SSWRCDGKAD CENGADEVNC APKQCTAAEF
SCRNSQCVSS SFVCDDEADC DDGSDEASCP PVTCSSMSFQ CNSTVCIPRL WLCDGDVDCS
DGSDEWAQTC GTKRPASAAT HQCSSLEFQC GSGECIHGSW KCDGGADCLD RSDETDCARP
TCRPDEFQCG DGSCIHGSRQ CNQQYDCRDM SDELGSTHCE GPTRFKCHSG ECISMERVCD
KQRDCRDWSD EPLRECGSNE CLYNNGGCSH VCNDLKIGYE CLCPAGYSLV DNKRCEDIDV
CGNLDTCSQI CINQMGSYKC QCEEGYQVDP ATKACKAIGT IAYLIFTNHH EVRKMTLDKS
EYTRVIPRLK NAVALDMNME TKEIYWSDLS QKKIYRAQMD SAGDSAHHSI VIGNNVDAPE
GIAFDWIHGN LYWTDSVRRT ISVVTADGRR RKTLFNQDLL KPRAIVVDPH SNFVYWTDWG
SPAKIEKGGL NGVDRTSLVT DNIVWPNGIT LDLLNQRLYW VDSKLHTLSS IDVQGGGRRT
LIIDEHQLAH PLGLTVFEER VFWTDVSNNA ILSANRLTGD DITPVAEHLS SPEDIILYHN
LKQPAGMNWC QVSNGGCEFM CLAAPQVGRH PPKYTCVCPD NMMLASDMRA CVPGRLALSN
WVSFSFRYPT RVTCSRTKDH LHHPSSCLRC PTSGYVAPAD AAKTASSPQI KNPNSDNSAN
NSYRYCAWSI CAALVCLVAV GGVLLWRNYR QKNTNTIHFD NPVYQKTTED QVHIWRSHSP
DGYSYPKRQV VSLDEEADNP AFTEN
//
