ID A0A3P9DCX3_9CICH Unreviewed; 796 AA.
AC A0A3P9DCX3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Low-density lipoprotein receptor 1 {ECO:0000313|Ensembl:ENSMZEP00005032007.1};
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:ENSMZEP00005032007.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005032007.1, 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:ENSMZEP00005032007.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the LDLR family.
CC {ECO:0000256|ARBA:ARBA00009939}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3P9DCX3; -.
DR Ensembl; ENSMZET00005033041.1; ENSMZEP00005032007.1; 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:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 8.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
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; 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; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
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; 3.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 4.
PE 3: Inferred from homology;
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 378..393
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT DOMAIN 418..433
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 481..527
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 528..570
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 571..614
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 615..659
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 30..42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 37..55
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 49..64
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 69..81
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 76..94
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 116..128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 123..141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 135..150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 155..167
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 162..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 174..189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 194..206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 201..219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 246..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 258..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 278..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 285..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 297..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 324..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 796 AA; 87903 MW; CE1C3272F5DFA547 CRC64;
MTQGVVIDII IDRFLTPILP SCFTTAAKYC DDHEFRCANG QCISKSFVCD SNETCSDGSD
EVSCSNTTCS PHSFQCNNSV CVPAVWRCDG DIDCPDGSDE WPQNCEGREP EKKTHCQTHE
FQCVNGSCIK DNWKCDGMFD CQDGSDETNC TAKQCDDREF RCANGQCISK SFVCDIDNDC
LDGSDEASCS KTNCNPHFFQ CNSSMCVPAV WRCNGDINCD DGSDEWPQNC EGRKPEKTCR
PHEFQCANGD CIPGNWKCDG GFDCLDHSDE ANCTHSTCRS DEFQCKDGTC INKNLQCNGR
ADCGDLTDEI ECDTVCEGPN KFQCRSGECI DTEKVCNKQN DCKDGSDEPA KECDNNECLT
GNGGCSHYCN DLKIGYNCSC PAGYRLKADN KTCEDIDECA EPDTCTQICI NLPGSYKCDC
EEGYMIDPAT KTCKAESGTV PTLYFTIKHE VRKLTVDRSE YVRVIPQLKN AVALDMDMPN
KMIFWSDLSL KKIYSSMIDV AGNSSHHNVV VESGIEAPEG IAVDWIHGNI YWTDSVLKTI
SVATTDGGMR KTLIATDLDK PRAITVDPVN NLMYWTDWGE EAKIEKSGLN GADRTTLVKD
NIVWPNGITL DMVNQRLYWV DAKLHSLSSI DVNGGARHSL IINEEKLFHP LSLTVFEVSD
EVFWTDMRKA AVFSANRLTG SDITELAKNL GQLKDIVLHH NLKQPASANW CTNGGCEFLC
LPAPQNDPQS PRYTCACPDG MVLRPDMKKC VAGKHLSSSS SGKVIHTNFG LLCHDKAVNI
HVTQTAHISG NMDICV
//