ID A0A2U9BQX5_SCOMX Unreviewed; 1357 AA.
AC A0A2U9BQX5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Putative very low-density lipoprotein receptor-like {ECO:0000313|EMBL:AWP06598.1};
GN ORFNames=SMAX5B_018830 {ECO:0000313|EMBL:AWP06598.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP06598.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP06598.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:PRU00076}.
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DR EMBL; CP026251; AWP06598.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000000178; -.
DR Proteomes; UP000246464; Chromosome 9.
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; 1.
DR CDD; cd00112; LDLa; 10.
DR Gene3D; 4.10.1220.10; EGF-type module; 3.
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; 2.
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 PANTHER; PTHR22722:SF12; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 4 ISOFORM X1; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00057; Ldl_recept_a; 10.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00192; LDLa; 11.
DR SMART; SM00135; LY; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 11.
DR SUPFAM; SSF63825; YWTD domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 11.
DR PROSITE; PS51120; LDLRB; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Lipoprotein {ECO:0000313|EMBL:AWP06598.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:AWP06598.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1357
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016003635"
FT TRANSMEM 1286..1307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 488..525
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 664..707
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1239..1275
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1315..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 47..62
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 86..101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 125..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 192..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 231..246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 270..285
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 290..302
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 297..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 309..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 330..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 349..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 391..406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 411..423
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 418..436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1265..1274
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1357 AA; 147619 MW; 249819475FA851F4 CRC64;
MGGCLLLGAV LLLLMGSLQA GSSRLKCSLS SKLCKDGSEC VLYSNVCDGE PDCKDGSDED
DCASECHRDQ FQCAHGKKCI QKDQICDGVP QCQDRSDELQ CMKHTDDCVH HCDNRNRCLP
ASFLCDGEKD CLDGTDEASC GNLEEDWYEK EEKNSTTPDL PVSGGPSTNI KCNLGAIPCK
DNTKCVLYNH VCDGEVDCSD GSDEGDCALA CGTDQFQCAH GKKCIEQSQV CDGVPQCQDR
SDELACAKHM EGCAHHCDDK SRCIPNSFLC DGERDCLDGS DEANCAEESC SATEFKCTSG
QCVSAIMRCD GSLDCWDRSD EEGCPKAPVC TTKHRCPVSR ECLLPEWICD GDRDCKDGTD
EKDCPVVPLN CGEFQWSCKS KTKCIPTAWR CDGMKDCDDG SDETECGVVP CLPHQFQCGS
QECLDPSLVC SGMTNCADGS DEGGSCQINC AEADDSRCSQ SCYSTPQGTR CHCKAGFRLT
EDGLTCADID ECEGPSPGVC SQLCVNTPGS YRCDCHPGFI MEAGEHHCKI PGEPYLLSSV
KTDLFVFGLR SGSLDVLPSS AKNAILSLDY DWRDQRVFWA SLDTESIRWS SLDQKTMGTL
IKEVRADSVA VDWLGRNMYW IDGMNSQIFA IRLGTGTVKS QDQSVILDED LDQPRSLALL
PQKGLMFWTE IGNVVKIERA GMDGSERMAV VNSSLGWPGG VAVDTDRVYW TDERLGAIGS
ATLDGDDIRI LQMKETTNPF ALAVFNDMLY WSDAKKRVVQ AAHKISGKKH QILMKRHKQP
FGVKIIHPWL QMGSQSPCEK RECSHMCVLA PGPKAVCKCP SGLLLAEDGL TCSSLVNSAF
LLMLSPSTVT QIYLQSRNRA AELKGWPEHL ALQLPSVNEA AIMDYNLHDH TLFLTDDGTN
SLSSFKLKES NLASQGQLLK LLGDTITAMA LDWVTLNVYW SSNKQPRLLV TSIKGAHTAV
LLKEGIGRIG SIAIHPPSGR LCFTNLGLQG TGTVATVECA NMDGAEQRVV WKDAVQPTSV
VFSSNGDAIY WADTALGAIG SVQLDGSRYR EMKVGDGLTA VALSDDTLLW MTVNDKTRLW
YRDEQQQSKL WFEVGTQVVS MKAFSKSSQS GSNQCTENNG NCQHFCLATS GGRTCRCSHD
HILMNATHCS LDQGCPVGSR PCLDQLSCQP VEKFCNGHVD CSDHSDENCV NLKQWSGVKV
FAPIQPRSSS LSPSPFPPLF KTTDLKTTLN VSSRLLNLDA QQCSQRHCSS NGHCVKINGD
TTCACSLGYS GDSCQDNILK TMQGPIIYGT AGLCVGMLVI AVMAVVVKRK KRTNMRSATP
AAVKGTSMTD LENRAETTPS TKTADTEKQE DVVLSVD
//
