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   03-AUG-2022, entry version 129.
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; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=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.
CC   -!- SUBUNIT: Interacts with ldlrap1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC       Membrane, clathrin-coated pit; Single-pass type I membrane protein.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR   EMBL; M62978; AAA49898.1; -; mRNA.
DR   PIR; B40388; QRXLL2.
DR   RefSeq; NP_001079111.1; NM_001085642.2.
DR   AlphaFoldDB; Q99088; -.
DR   SMR; Q99088; -.
DR   GeneID; 373644; -.
DR   KEGG; xla:373644; -.
DR   CTD; 373644; -.
DR   Xenbase; XB-GENE-962375; ldlr.S.
DR   OrthoDB; 359795at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 373644; Expressed in intestine and 19 other tissues.
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   Gene3D; 4.10.400.10; -; 6.
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; 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; Reference proteome; Repeat; Signal; Steroid metabolism;
KW   Sterol metabolism; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..892
FT                   /note="Low-density lipoprotein receptor 2"
FT                   /id="PRO_0000017316"
FT   TOPO_DOM        22..819
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        820..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        842..892
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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          715..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..813
FT                   /note="Clustered O-linked oligosaccharides"
FT   REGION          752..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           854..859
FT                   /note="Endocytosis signal"
FT                   /evidence="ECO:0000255"
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   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