ID W5KRL5_ASTMX Unreviewed; 3131 AA.
AC W5KRL5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Low-density lipoprotein receptor-related protein 2-like {ECO:0000313|Ensembl:ENSAMXP00000010227.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000010227.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000010227.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 7994.ENSAMXP00000010227; -.
DR Ensembl; ENSAMXT00000010227.2; ENSAMXP00000010227.2; ENSAMXG00000009947.2.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000162544; -.
DR HOGENOM; CLU_242519_0_0_1; -.
DR InParanoid; W5KRL5; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000009947; Expressed in testis and 2 other cell types or tissues.
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; 39.
DR Gene3D; 4.10.1220.10; EGF-type module; 6.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 35.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR006150; Cys_repeat_1.
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 InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR24270:SF66; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 37.
DR Pfam; PF00058; Ldl_recept_b; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00192; LDLa; 43.
DR SMART; SM00135; LY; 8.
DR SMART; SM00289; WR1; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 41.
DR SUPFAM; SSF63825; YWTD domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 15.
DR PROSITE; PS50068; LDLRA_2; 43.
DR PROSITE; PS51120; LDLRB; 2.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT TRANSMEM 3054..3072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 3..48
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 2086..2115
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 2261..2302
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 2438..2481
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 3009..3045
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ZN_FING 2086..2115
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1795..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3090..3131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3117..3131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 457..472
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 497..512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 547..562
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 586..601
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 625..640
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 677..692
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 717..732
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 752..767
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 802..817
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 841..856
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 880..895
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 934..949
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 974..989
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1009..1024
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1059..1074
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1130..1145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1194..1209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1234..1249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1284..1299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1323..1338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1362..1377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1406..1421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1446..1461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1497..1512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1536..1551
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1575..1590
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1619..1634
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1659..1674
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1709..1724
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1748..1763
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1787..1802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1839..1854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1879..1894
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1914..1929
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1964..1979
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2003..2018
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2042..2057
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2062..2074
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2069..2087
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2081..2096
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2102..2114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2121..2136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2163..2178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2183..2195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2190..2208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2955..2970
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3035..3044
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3131 AA; 342863 MW; 633CB6773852AFC9 CRC64;
MKSSMFWINR GPNDEVTIEK AGMDGSMRTT LVIVTAQSPR SLTLDVAAQR LYWISDFKMS
IETIKVDGTG RYTFREFFKG RRAQNLAVFN GWIYWADEKR LWQAPQNQPD QKNFVLKAAL
PILTAYHQEQ QPQAPCPCRK AQCQLCLPSL GMPSGFMCSC PKDQLPVAEG SCQSLKLAYA
RSTNIYTLEY TEDGPVNSLL FSASEEVEAF DVDWKRGLVV WTNLTGQLKV GLLAEGRSEY
VATLKPACAI RIDQRTGNVY WVSCDALSIG ATHIILPDHS VSKQLHQAGG EIVDLFVDWQ
RGQLYWLEGL QIINMKLSLM GGNAKSIYSF EEKSVSQLVL DRKANSFLWS SENELQVLSL
LKKRAYSAGK EWTIPNRIVA AYEPYMVTMI NDVITPWRRQ DGMRLQSVPL GRGVVGVIVA
LRELNQGDAS SHSHGPCRSP SVVCKGTSVC LSQTQLCDGK KDCPDGSDEA SCGGVCPNQG
DFQCKDKTKC IGSYLVCDGH SHCADGSDEV GCPTVSAPTS TAAPLRCRFG SKLCTDGSEC
VLLSHVCDGE VDCKDGSDEE GCEQQCKAHQ FHCAHGRMCI DKNLVCDGTP QCQDRSDEMG
CFTKSEGCSH HCDDRTRCIP ESFLCDGERD CTDGSDEAGC PSAYVASSDK SSTGPTCYPP
SLTCERTSLC INQSQLCDEK FDCPDGFDEL FCLHSCSHPG QFLCKNKRKC IEEALVCDGR
SDCPDGSDEV SCPACPLHCD DWTVCLSSQQ FCDDRMDCRD GVDERNCNNN QPKPVGSSPL
KCSPGFKPCK DGSECVLYSH VCDGEKDCQD GSDEGDCESK CNKDQFQCAH GRKCIDKKLV
CDGTPQCQDR SDELSCITRS EHCHHHCDNN TRCIPDNFLC DGDVDCTDGS DEADCTSLTT
AVFPSYKPQA KPSCESPSIM CEGTSVCVSQ SQLCDGKFDC PDGFDEFFCL RACSHPGQFL
CKNKRKCIEE ALVCDGRSDC PDGSDEVSCP ACPLHCDDWS VCLSSQQFCD DRMDCRDGAD
ERNCDKGRKT ATGTSGLVCP LGLKPCLDAS ECILHRHVCD GEKDCRDGSD EENCDHRCNK
GQFQCTNGKL CIDRKQVCDG TAHCPDHSDE VDCCSLQCDK NRCIPEKLLC DGERDCVDGA
DEADCSRNNE SVESVKQSSN DVSTRLSAYQ SPACERPSVL CEGTRLCISQ TQLCDGKPDC
PDGSDEKSCI DTCTHIGNFR CKDSGRCIEG YLVCNGRSDC VDGSDEVGCP AVAPETANKT
PLWCRLGSRL CKDGSDCVLL SHVCDGERDC KDGSDEDGCD LQCSPGQFQC IRGKRCIDKK
QVCDGTPQCQ DGSDESGCWK PTRICALRCD QNSRCIPEVF ICNGKKDCWD GSDESDCGNS
AVHLPCKSPS VPCLGSTQCI SQLQLCDGRK DCADGSDERP CITKCPYNGD YLCKDRRKCV
DVKQVCDGNF HCTDGSDEVG CPTVAAETTT PAGPLKCRLG LKACKDGSQC ILYSHVCDGE
VDCKDGSDEE GCDVNCRTGQ FQCAHGKKCI DAKLVCDGKP QCQDRSDELG CFTRTKSCSH
HCDNRTRCIP ETFLCDGETD CADGSDEADC GYPTQVSSCA SPSVLCRGGK LCVSSSQVCD
GKRDCPDGFD EELCVKRCPK SGQFLCKDRR RCIDKYQVCD GHSHCADGSD EVGCPTVSAP
TSTAAPLRCR FGSKLCTDGS ECILLSHVCD GEVDCKDGSD EEGCERLCKA HQFRCAHGRM
CIDKNLVCDG TPQCQDRSDE MGCFTKSEGC SHHCDDRTRC IPESFLCDGE RDCTDGSDEA
GCSSDTKTSS YKPSPEVNCK YPSVKCEGTS LCISQSQMCD GKVDCPDQSD ERFCMQACSD
PGQFLCKNKR KCIEKMFVCN GHSDCTDGSD ELQCPPCPRH CDDRTMCLTN EQLCDGNVDC
KDGSDERNCA SGGGIAAGAS PLKCRVGFKA CLDGSECILY SHVCDGEKDC KDGSDEKDCE
QQCKKGSFQC AHGKMCIDMK QVCDGTPQCQ DRSDELNCYE RTEDCHHYCD NRTRCLPKTF
ICDGERDCFD GTDEVGCAPE PCSIGSFQCS SGQCVSTKLR CDGHADCRDH SDEKSCRRPP
HCPLGDRCPR SHECLLKEWR CDGHKDCANG SDEKNCKTRS VQCGELQWWC TSGTQCVPTS
WRCDGTKDCK DQSDEAGCGK AECPSHLFQC RSEGCVNPGL VCNGISDCVD GSDEGLGCLS
SNCSRSRMQQ CEHYCVNTPQ GERCVCRAGF RLQADGVSCV DVDECTEIKP SVCSHKCHNT
HGSYACQCSP GFLLEPDGST CKSPEEPHLL AAVQNELLFK DLRSGNLQLL LPPGQTPIFS
LDYDLMEQKL FWVSLEEKTI KYAVHGDKGN IKPLIKGVKS DSIAIDWIGR NLYWLDGAAK
QILAVRLGSS VVKPRNYIVI LDEDLEQPRS LLLLPQKGLM LWSEIGNESR IERAGMDGSQ
RKVVLNRNLR WPVSLAIDIV TDRLYWTDMK LQCIGSATLA GEDVRFLQLT ETSAPFSVAV
FNDMVYWSDN RRRIIYGAHK TTGKNRTVIL KRPGLPFGLK IVHPLMQPKI PNPCQALKCS
HMCLLTSGSQ AVCRCPDGLL LAEDRITCSS LEESASDSAF LLLLSPSVLT QIFTKNLPAK
VELNQWPEHR AMALPGISEA TGLDLVLRDG MLFLASQASV AQLQMDDSGL TRKGSPLQLS
DDSVTALAVD WITHNLYWSS LKKPQLYVSS PDWKYTAVVI KAKLKDTTSI TLHPPTGRLC
FTAIELGGAG SLPQIFCAFM NGENRKVLWK KAQMPMSLTF STQGSSLYWV DIAAAVIASV
DIDGSNYREY KTGPPLIVSF APSDNILFWV TLYNGTNTVW YSDGVQPKQM WFEVQTNIVA
LKAYSANSQK GSNLCAENNG GCSQLCLANP GGRTCRCTQG YLVVSKTQCV ATLECPAGSK
PCRNGHECLS SSKFCDHISD CPDGSDEEDC AYLNTYQGFK HRPPPPQPSS SGSQGVSVPQ
DDILVRTLSG QSCDSDLCNG RGQCVIQEGE QSCRCVQGYS GTFCEVGGSR SSSVVLSVLF
ILGIVIVAAV LLRMRREKAL RGLSIDKETL MKDMEDHEEP EEPEEQESSP QNFVNELYDP
DKEEQATELV D
//
