LDLR1_XENLA
ID LDLR1_XENLA Reviewed; 909 AA.
AC Q99087;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Low-density lipoprotein receptor 1;
DE Short=LDL receptor 1;
DE Flags: Precursor;
GN Name=ldlr-a; Synonyms=ldlr1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH LDLRAP1, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Liver, and Oocyte;
RX PubMed=1709931; DOI=10.1016/s0021-9258(18)99240-9;
RA Mehta K.D., Chen W.J., Goldstein J.L., Brown M.S.;
RT "The low density lipoprotein receptor in Xenopus laevis. I. Five domains
RT that resemble the human receptor.";
RL J. Biol. Chem. 266:10406-10414(1991).
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:0000250|UniProtKB:P01130}.
CC -!- SUBUNIT: Interacts with ldlrap1. {ECO:0000269|PubMed:1709931}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:1709931};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}.
CC Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P01130}. Golgi
CC apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome
CC {ECO:0000250|UniProtKB:P01130}. Late endosome
CC {ECO:0000250|UniProtKB:P01130}. Lysosome
CC {ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon ligand
CC binding. {ECO:0000250|UniProtKB:P01130}.
CC -!- DOMAIN: The NPXY motif mediates the interaction with ldlrap1.
CC {ECO:0000250|UniProtKB:P01130}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; M62976; AAA49897.1; -; mRNA.
DR PIR; A40388; QRXLL1.
DR RefSeq; NP_001081290.1; NM_001087821.1.
DR AlphaFoldDB; Q99087; -.
DR SMR; Q99087; -.
DR GeneID; 397757; -.
DR KEGG; xla:397757; -.
DR CTD; 397757; -.
DR Xenbase; XB-GENE-6252601; ldlr.L.
DR OrthoDB; 359795at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 397757; Expressed in intestine and 19 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 4.10.400.10; -; 7.
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 Pfam; PF07645; EGF_CA; 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; SSF57184; 1.
DR SUPFAM; SSF57424; SSF57424; 7.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 7.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Cholesterol metabolism; Coated pit; Disulfide bond;
KW EGF-like domain; Endocytosis; Endosome; Glycoprotein; Golgi apparatus; LDL;
KW Lipid metabolism; Lipid transport; Lysosome; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Steroid metabolism; Sterol metabolism;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P01131"
FT CHAIN 22..909
FT /note="Low-density lipoprotein receptor 1"
FT /id="PRO_0000017315"
FT TOPO_DOM 22..836
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P01131"
FT TRANSMEM 837..858
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 859..909
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT DOMAIN 25..65
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 66..106
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 107..145
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 146..185
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 193..231
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 232..270
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 272..311
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 312..351
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 352..391
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 395..436
FT /note="LDL-receptor class B 1"
FT REPEAT 437..483
FT /note="LDL-receptor class B 2"
FT REPEAT 484..526
FT /note="LDL-receptor class B 3"
FT REPEAT 527..570
FT /note="LDL-receptor class B 4"
FT REPEAT 571..613
FT /note="LDL-receptor class B 5"
FT REPEAT 614..656
FT /note="LDL-receptor class B 6"
FT DOMAIN 661..710
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 717..813
FT /note="Clustered O-linked oligosaccharides"
FT REGION 717..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 871..876
FT /note="NPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P01130"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..39
FT /evidence="ECO:0000250"
FT DISULFID 34..52
FT /evidence="ECO:0000250"
FT DISULFID 46..63
FT /evidence="ECO:0000250"
FT DISULFID 68..82
FT /evidence="ECO:0000250"
FT DISULFID 75..95
FT /evidence="ECO:0000250"
FT DISULFID 89..104
FT /evidence="ECO:0000250"
FT DISULFID 109..121
FT /evidence="ECO:0000250"
FT DISULFID 116..134
FT /evidence="ECO:0000250"
FT DISULFID 128..143
FT /evidence="ECO:0000250"
FT DISULFID 148..161
FT /evidence="ECO:0000250"
FT DISULFID 155..174
FT /evidence="ECO:0000250"
FT DISULFID 168..183
FT /evidence="ECO:0000250"
FT DISULFID 195..207
FT /evidence="ECO:0000250"
FT DISULFID 202..220
FT /evidence="ECO:0000250"
FT DISULFID 214..229
FT /evidence="ECO:0000250"
FT DISULFID 234..246
FT /evidence="ECO:0000250"
FT DISULFID 241..259
FT /evidence="ECO:0000250"
FT DISULFID 253..268
FT /evidence="ECO:0000250"
FT DISULFID 274..287
FT /evidence="ECO:0000250"
FT DISULFID 282..300
FT /evidence="ECO:0000250"
FT DISULFID 294..311
FT /evidence="ECO:0000250"
FT DISULFID 316..327
FT /evidence="ECO:0000250"
FT DISULFID 323..336
FT /evidence="ECO:0000250"
FT DISULFID 338..350
FT /evidence="ECO:0000250"
FT DISULFID 356..366
FT /evidence="ECO:0000250"
FT DISULFID 362..375
FT /evidence="ECO:0000250"
FT DISULFID 377..390
FT /evidence="ECO:0000250"
FT DISULFID 665..679
FT /evidence="ECO:0000250"
FT DISULFID 675..694
FT /evidence="ECO:0000250"
FT DISULFID 696..709
FT /evidence="ECO:0000250"
SQ SEQUENCE 909 AA; 101296 MW; 6ED41F5402A16371 CRC64;
MMKPAASFPL LLLGLCHVSA ISGIRKCDRN EFQCGDGKCI PYKWICDGSA ECKDSSDESP
ETCREVTCGT DQFSCGGRLN RCIPMSWKCD GQTDCENGSD ENDCTHKVCA DDQFTCRSGK
CISLDFVCDE DLDCDDGSDE SYCPAPTCNP AMFQCKDKGI CIPKLWACDG DPDCEDGSDE
EHCEGREPIK TDKPCSPLEF HCGSGECIHM SWKCDGGFDC KDKSDEKDCV KPTCRPDQFQ
CNTGTCIHGS RQCDREYDCK DLSDEEGCVN VTKCEGPDVF KCRSGECITM DKVCNKKRDC
RDWSDEPLKE CGENECLRNN GGCSHICNDL KIGYECLCNE GYRLVDQKRC EDINECENPN
TCSQICINLV GGYKCECREG YQMDPVTASC KSIGTVAYLF FTNRHEVRKM TLDRSEYTSV
IPRLKNVVAL DMEIASNKIY WSDLTQRKIY SASMEKADNT SHHETVISNQ IQAPDGIAVD
WIHGNIYWTD SKFSTISVAN TEGSKRRTPP SDDLEKPRDI VVDPSQGFMY WTDWGLPAKI
EKGGLNGVDR YPLVTENIEW PNGITLDLIN QRLYWVDSKL HSLSCIDVTG ENRRTVISDE
THLAHPFGLT IFEDLVFWTD IENEAIFSAN RLTGRNIMKV AEDLLSPEDI VLYHNLRQPK
AENWCEAHHL GNGGCEYLCL PAPHITARSP KFTCACPDGM HLGDDMRSCV KEPVIPEASP
TTTTSAPVTT TTSAPVTTTT SAPVTTTSTT ARPTSRSTTL AKITSTTSTL APQRPKMAST
TIAPQRPTTN SPKTTLRMIT EKVPDHTTQQ PMTHSQLADN NFAKAGVVEN VRSHPTALYI
VLPIVILCLV AFGGFLVWKN WRLKNTNSIN FDNPVYQKTT EEDQVHICRS QDGYTYPSRQ
MVSLEDDIA
