ID A0A3P9DCX1_9CICH Unreviewed; 815 AA.
AC A0A3P9DCX1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Low-density lipoprotein receptor 1 {ECO:0000313|Ensembl:ENSMZEP00005032001.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005032001.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005032001.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005032001.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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:PRU00124}.
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DR AlphaFoldDB; A0A3P9DCX1; -.
DR Ensembl; ENSMZET00005033035.1; ENSMZEP00005032001.1; ENSMZEG00005023863.1.
DR GeneTree; ENSGT00940000154819; -.
DR Proteomes; UP000265160; LG6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.40.128.620; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
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; 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; PF12662; cEGF; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
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:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; 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};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..815
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018191408"
FT DOMAIN 331..346
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT DOMAIN 371..386
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 434..480
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 481..523
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 524..567
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 568..612
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 794..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 24..36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 31..49
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 86..101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 106..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 113..131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 125..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 145..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 152..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 192..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 199..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 232..244
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 277..295
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 815 AA; 90217 MW; 7964535E0FAEDDCB CRC64;
MCVFCFIFVF LSCIISLHYA AYICNANQFK CGNGRCITRR WICDGSDDCG DGTDELPASC
GVKICRDSQF NCGDPTSQCI SKDWQCDGKA DCTNGADEKN CTAKYCDDHE FRCANGQCIS
KSFVCDSNET CSDGSDEVSC SNTTCSPHSF QCNNSVCVPA VWRCDGDIDC PDGSDEWPQN
CEGREPEKKT HCQTHEFQCV NGSCIKDNWK CDGMFDCQDD GSDEASCSKT NCNPHFFQCN
SSMCVPAVWR CNGDINCDDG SDEWPQNLCE GPNKFQCRSG ECIDTEKVCN KQNDCKDGSD
EPAKECDNNE CLTGNGGCSH YCNDLKIGYN CSCPAGYRLK ADNKTCEDID ECAEPDTCTQ
ICINLPGSYK CDCEEGYMID PATKTCKAES GTVPTLYFTI KHEVRKLTVD RSEYVRVIPQ
LKNAVALDMD MPNKMIFWSD LSLKKIYSSM IDVAGNSSHH NVVVESGIEA PEGIAVDWIH
GNIYWTDSVL KTISVATTDG GMRKTLIATD LDKPRAITVD PVNNLMYWTD WGEEAKIEKS
GLNGADRTTL VKDNIVWPNG ITLDMVNQRL YWVDAKLHSL SSIDVNGGAR HSLIINEEKL
FHPLSLTVFE EKVFWTDMRK AAVFSANRLT GSDITELAKN LGQLKDIVLH HNLKQPASAN
WCTNGGCEFL CLPAPQNDPQ SPRYTCACPD GMVLRPDMKK CVAGKHLHLL LLKKMELKSN
LEIQPAAPPL KDKTAAPLPP QGPTNPSSLS FLATLSLLCL YSWSSVILKA RFLLNSLPST
HLCTLLGPLH TPPHGLPLQT VTKRRRNQQD RCRPV
//
