ID A0A2D0S5U2_ICTPU Unreviewed; 875 AA.
AC A0A2D0S5U2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Low-density lipoprotein receptor {ECO:0000313|RefSeq:XP_017337806.1};
GN Name=ldlrb {ECO:0000313|RefSeq:XP_017337806.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017337806.1};
RN [1] {ECO:0000313|RefSeq:XP_017337806.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017337806.1};
RG RefSeq;
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 RefSeq; XP_017337806.1; XM_017482317.3.
DR AlphaFoldDB; A0A2D0S5U2; -.
DR STRING; 7998.ENSIPUP00000024350; -.
DR Ensembl; ENSIPUT00000025376; ENSIPUP00000024350; ENSIPUG00000016428.
DR GeneID; 108273208; -.
DR KEGG; ipu:108273208; -.
DR CTD; 393460; -.
DR OMA; TINDHEC; -.
DR OrthoDB; 3918101at2759; -.
DR Proteomes; UP000221080; Chromosome 12.
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; cd00054; EGF_CA; 2.
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; 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 PANTHER; PTHR24270:SF21; LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 4.
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; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 6.
DR SUPFAM; SSF63825; YWTD domain; 1.
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; 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:PRU00076};
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 Lipoprotein {ECO:0000313|RefSeq:XP_017337806.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_017337806.1}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|SAM:SignalP};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..875
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013288380"
FT TRANSMEM 799..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..351
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 352..391
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 438..484
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 485..527
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 528..571
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 572..616
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 724..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 29..41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 36..54
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 91..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 111..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 118..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 130..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 150..162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 157..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 195..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 202..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 214..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 234..246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 241..259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 253..268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 282..300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 356..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 875 AA; 96599 MW; 222526EB5A5DA58D CRC64;
MLLRKNCSVV LSCVLLGLIS LPLSRAATCN ERQFQCGNKK CITNRWVCDG TDDCGDGTDE
LPATCTEKKC LPSEFTCNGS PIQCVSSRWR CDGKADCENG TDELNCALKN CTADEFRCAD
GQCISTSFVC DEDADCSDGS DEASCPKPTC IAGSFQCNNT VCVPQLWACD GDADCADGSD
EWSEHCGQKP IPSPCSEQEF QCSNGKCIHS MWRCDGGFDC TDHSDEANCT VATCRPDEFQ
CNDGSCIPGI HQCDGEIHCK DLSDEKDCAT VSKCDGPDTF QCRSGECISI DKVCDKKRDC
RDLSDEPIKE CNVNECLENN GGCSHDCKDL KIGYECLCPS GYRLVDQKRC EDIDECADPD
TCAQVCLNLV GGFKCDCQEG YEMDPMTKEC KAVSDNIPYL YFTNHHEVRK MTLDKKEYTC
LIPRLKNVVA LDMDVSSETI FWADLFHKKI YSTPIDKAAY PTNHITLIDS QISSPEGLAV
DWVHGNIYWT DSFFQSISVA TKDGSKRKTL IKVGLNKPHD IVVDPERNFM YWTDCGNPAR
IEKSGLNGAD RTALVTDNIV WPSGITLDLV NQRLYWLDSK LHMLSSIGVD GGLRHTLIVD
EWQLANPFSL AVFEEKVFWT DASNGSIRSA NRLTGKSIMT VVKNLLSPKD IVLYHNLKQP
SGTNWCEEGN HVNGGCDYLC LPAPRVNQHS PKYTCTCPDH MILGPDMRKC VEVLKPVAST
AVVPPPVPAG TTPKRPAIQS TTTTTRTTTK QTPRTTGSMT SSGAAGSRKN IPETKTEISP
REGSNDVYVA VTSPSQHSLA LYVILPIAVL CLTAIGAVLL WRHWRLKNTN TIHFDNPVYQ
KTTEDQVHIC RSQSQDGYVY PPHQMLCLDD EEDIA
//
