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Database: UniProt
Entry: Q99088
LinkDB: Q99088
Original site: Q99088 
ID   LDLR2_XENLA             Reviewed;         892 AA.
AC   Q99088;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JAN-2019, entry version 120.
DE   RecName: Full=Low-density lipoprotein receptor 2;
DE            Short=LDL receptor 2;
DE   Flags: Precursor;
GN   Name=ldlr-b; Synonyms=ldlr2;
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].
RC   TISSUE=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.
CC   -!- SUBUNIT: Interacts with ldlrap1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Membrane, clathrin-coated pit; Single-pass type I
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
DR   EMBL; M62978; AAA49898.1; -; mRNA.
DR   PIR; B40388; QRXLL2.
DR   RefSeq; NP_001079111.1; NM_001085642.2.
DR   UniGene; Xl.821; -.
DR   ProteinModelPortal; Q99088; -.
DR   SMR; Q99088; -.
DR   PRIDE; Q99088; -.
DR   GeneID; 373644; -.
DR   KEGG; xla:373644; -.
DR   CTD; 373644; -.
DR   Xenbase; XB-GENE-962375; ldlr.
DR   HOVERGEN; HBG006250; -.
DR   KO; K12473; -.
DR   OrthoDB; 359795at2759; -.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
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; 6.
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; 4.
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   2: Evidence at transcript level;
KW   Cholesterol metabolism; Coated pit; Disulfide bond; EGF-like domain;
KW   Endocytosis; Glycoprotein; LDL; Lipid metabolism; Lipid transport;
KW   Membrane; Receptor; Repeat; Signal; Steroid metabolism;
KW   Sterol metabolism; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    892       Low-density lipoprotein receptor 2.
FT                                /FTId=PRO_0000017316.
FT   TOPO_DOM     22    819       Extracellular. {ECO:0000255}.
FT   TRANSMEM    820    841       Helical. {ECO:0000255}.
FT   TOPO_DOM    842    892       Cytoplasmic. {ECO:0000255}.
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       854    859       Endocytosis signal. {ECO:0000255}.
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   892 AA;  99824 MW;  F84AF0BB4278F4D5 CRC64;
     MMKPAVSFPL LLLGLCHVSA FSGIGKCDRN EFQCGDGKCI PYKWICDGSA ECKDGSDESS
     ETCRALTCGA DQFSCGGRLN RCIPMSWKCD GQTDCENGSD ENDCTRKVCA DDQFTCRSGK
     CISLDFVCDQ DQDCDDGSDE SYCPAPTCNP AMFQCKDKGI CIPKLWACDG DRDCEDGSDE
     DHCEGREPIK TDKPCAPLEF HCGSGECIHM SWKCDAGYDC KHKSDDKDCV KPTCRPDQFQ
     CNDGTCIHGS RQCDREYDCK DLSDEEGCVN VTKCQGPDVF KCRSGECITM DKVCHKKRDC
     RDWTDEPIKE CGENECLRNN GGCSHICNDL KIGYECLCNE GYRLVDQKRC EDINECENPN
     TCTQICINLH GGYKCECREG YQMDPVTASC KSIGTVAYLF FTNRHEVRKM TLDRSEYTSF
     IPRLKNVVAL DMEIASNKIY WSDLTQRKIY SASMDKADNT SHHETVISNQ IQAPDGIAVD
     WIHGNIYWTD SKFSTISVAN TEGSKRKTLF TDDLAKPRDI VVDPSQGFMY WTDWGLPAKI
     EKGGLNGVDR YPLVTDNIEW PNGITLDLIS QRLYWVDSKL HSLSCIDITG ENRRTVLSDE
     THLAHPFGLT IFEDLVFWTD IENEAIFSAK RLTGENIMKV AEHLLSPEDI VLYHNLRQPK
     AENWCESHHL GNGGCGYLCL PAPHVNARSP KFTCACPDGM HLGTDMRNCM KEPVTQEATT
     STTTSAPVTT TSTARPSSRI TTLAKIASTT STLAPQRPKM VSTTVPPRRP TTNSPKTTLR
     MNTEKVPAHT TQEPMTHSQL ARNKFAEAGV VESARSHPTA LYIVLPILIL CLVSFGGFLL
     WKNWRLKNTN SINFDNPVYQ KTTEEDQVHI CRSQDGYTYP SRQMVSLEDH IA
//
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