GenomeNet

Database: UniProt
Entry: Q99087
LinkDB: Q99087
Original site: Q99087 
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   16-JAN-2019, entry version 121.
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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;
RA   Mehta K.D., Chen W.J., Goldstein J.L., Brown M.S.;
RT   "The low density lipoprotein receptor in Xenopus laevis. I. Five
RT   domains 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
CC       be internalized, the receptor-ligand complexes must first cluster
CC       into 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
CC       {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit
CC       {ECO:0000250|UniProtKB:P01130}. Golgi apparatus
CC       {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
CC       ligand 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}.
DR   EMBL; M62976; AAA49897.1; -; mRNA.
DR   PIR; A40388; QRXLL1.
DR   RefSeq; NP_001081290.1; NM_001087821.1.
DR   UniGene; Xl.820; -.
DR   ProteinModelPortal; Q99087; -.
DR   SMR; Q99087; -.
DR   GeneID; 397757; -.
DR   KEGG; xla:397757; -.
DR   CTD; 397757; -.
DR   Xenbase; XB-GENE-6252601; ldlr.
DR   HOVERGEN; HBG006250; -.
DR   KO; K12473; -.
DR   OrthoDB; 359795at2759; -.
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:0005886; C:plasma membrane; 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   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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;
KW   LDL; Lipid metabolism; Lipid transport; Lysosome; Membrane; Receptor;
KW   Repeat; Signal; Steroid metabolism; Sterol metabolism; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     21       {ECO:0000250|UniProtKB:P01131}.
FT   CHAIN        22    909       Low-density lipoprotein receptor 1.
FT                                /FTId=PRO_0000017315.
FT   TOPO_DOM     22    836       Extracellular.
FT                                {ECO:0000250|UniProtKB:P01131}.
FT   TRANSMEM    837    858       Helical. {ECO:0000255}.
FT   TOPO_DOM    859    909       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P01130}.
FT   DOMAIN       25     65       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       66    106       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      107    145       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      146    185       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      193    231       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      232    270       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      272    311       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      312    351       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      352    391       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT      395    436       LDL-receptor class B 1.
FT   REPEAT      437    483       LDL-receptor class B 2.
FT   REPEAT      484    526       LDL-receptor class B 3.
FT   REPEAT      527    570       LDL-receptor class B 4.
FT   REPEAT      571    613       LDL-receptor class B 5.
FT   REPEAT      614    656       LDL-receptor class B 6.
FT   DOMAIN      661    710       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION      717    813       Clustered O-linked oligosaccharides.
FT   MOTIF       871    876       NPXY motif.
FT                                {ECO:0000250|UniProtKB:P01130}.
FT   CARBOHYD     97     97       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    270    270       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    459    459       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     27     39       {ECO:0000250}.
FT   DISULFID     34     52       {ECO:0000250}.
FT   DISULFID     46     63       {ECO:0000250}.
FT   DISULFID     68     82       {ECO:0000250}.
FT   DISULFID     75     95       {ECO:0000250}.
FT   DISULFID     89    104       {ECO:0000250}.
FT   DISULFID    109    121       {ECO:0000250}.
FT   DISULFID    116    134       {ECO:0000250}.
FT   DISULFID    128    143       {ECO:0000250}.
FT   DISULFID    148    161       {ECO:0000250}.
FT   DISULFID    155    174       {ECO:0000250}.
FT   DISULFID    168    183       {ECO:0000250}.
FT   DISULFID    195    207       {ECO:0000250}.
FT   DISULFID    202    220       {ECO:0000250}.
FT   DISULFID    214    229       {ECO:0000250}.
FT   DISULFID    234    246       {ECO:0000250}.
FT   DISULFID    241    259       {ECO:0000250}.
FT   DISULFID    253    268       {ECO:0000250}.
FT   DISULFID    274    287       {ECO:0000250}.
FT   DISULFID    282    300       {ECO:0000250}.
FT   DISULFID    294    311       {ECO:0000250}.
FT   DISULFID    316    327       {ECO:0000250}.
FT   DISULFID    323    336       {ECO:0000250}.
FT   DISULFID    338    350       {ECO:0000250}.
FT   DISULFID    356    366       {ECO:0000250}.
FT   DISULFID    362    375       {ECO:0000250}.
FT   DISULFID    377    390       {ECO:0000250}.
FT   DISULFID    665    679       {ECO:0000250}.
FT   DISULFID    675    694       {ECO:0000250}.
FT   DISULFID    696    709       {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
//
DBGET integrated database retrieval system