ID A0A3B4TFC0_SERDU Unreviewed; 1365 AA.
AC A0A3B4TFC0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Very low-density lipoprotein receptor-like {ECO:0000313|Ensembl:ENSSDUP00000004871.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000004871.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000004871.1}
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:PRU00076}.
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DR STRING; 41447.ENSSDUP00000004871; -.
DR Ensembl; ENSSDUT00000004972.1; ENSSDUP00000004871.1; ENSSDUG00000003580.1.
DR GeneTree; ENSGT00940000162544; -.
DR OMA; SHCLPAN; -.
DR OrthoDB; 2876426at2759; -.
DR Proteomes; UP000261420; Unplaced.
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; 11.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 9.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
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; 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; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 10.
DR Pfam; PF00058; Ldl_recept_b; 1.
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; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 9.
DR SUPFAM; SSF63825; YWTD domain; 2.
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; 4.
DR PROSITE; PS50068; LDLRA_2; 11.
DR PROSITE; PS51120; LDLRB; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1365
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017411606"
FT TRANSMEM 1293..1314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 493..534
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 669..712
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 713..755
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1246..1282
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 144..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 52..67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 91..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 130..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 197..212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 236..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 275..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 295..307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 302..320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 314..329
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 335..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 354..369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 396..411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 416..428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 423..441
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1272..1281
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1365 AA; 147960 MW; A9FBF03D84BF35BF CRC64;
MGGWLFLFVL LQLSEFLQAE PVVSAGSSPL NCGLGSKRCK DGSECVLYSH VCDGEPDCRD
GSDEEDCASG CNGDQFQCAH GKKCIDKDQV CDGVPQCQDR SDELHCMKQT EGCVHHCDSK
SRCLPASFLC DGERDCLDGT DEANCEDQED SGYEKEEKTS TTPEPAVSDG PSTIIKCPLG
AIPCMNKVEC ILYNHVCDGE ADCRDGSDEE ECSSACEADQ FQCAHGKKCI EQGQVCDGVA
QCQDRSDELG CAKHMEDCAH QCDDKSRCIP NSFLCDGEMD CWDGSDEANC ADEDCSATEF
KCTSGQCVSA TMRCDGHPDC WDHSDEESCT KPPVCTTKHR CLQSKECLVQ EWICDGDQDC
KDGTDEKDCP VAPLTCGEFQ WSCKSKTKCI PSAWRCDGVK DCNDGSDETE CGVVACLPHQ
FQCGSQECLD PVLVCNNITN CADGSDEGGS CQINCAEADN SRCSQSCYST PQGTRCHCTA
GFSLMEDGLT CADIDECDGQ SPAVCSQLCI NTPGSYRCDC HPGYIMEAGG HNCKITGEPL
LLSSVQTDLF LVGLRSGSVD VLSSSAKKAI LSVDYDWREQ RVYWVSLDSE NIRWSSLDQK
TTGTLIKGIR ADSVAVDWLG RNLYWIDGVN SQIVAIRLAT GTLESLDHSV ILDEDLDQPR
SLALLPQKGL MFWTEIGNVV KIERAGMDGS ERRAVVNSSL GWPGGVAVDT ISDRVYWTDE
RLGAIGSATL DGDDIQILQM KETTNPFSLA VFNNMLYWTD AKKRVVQAAH KISGKNRQVL
LKRPRQPFAV KIIHSLLQMG NQSPCEKMDC SHMCVLAPGP KAVCKCPSGL SLAEDGLTCS
SLVNSAFLLI LSPSTVTQIY LQSRHTAAEL KGWPEHLALQ VPSVNEAAIM DYNLRYHTLF
LTDDGTTSLS SFKLKDSDLT SQGQLLKLLG DAISAMALDW VTLSVYWSSN KQRRLQVTSI
TGAYTAVLIK EGIGRVESIA LHPPSGRVCF TNLARQDIGT VATVECANMD GAERRVMWKD
AVQPTSLVFS SNGDTIYWAD SGLGTIGYVQ LDGSGYRELK AGDGLAAVAL SDDTLLWMTV
NDKTRLWYRD EQQQNKLWFE VGTEVVSLKA FSKSSQTGSN QCTENNGNCQ HLCLATPGGR
TCKCGHDHVL VNATHCSPEQ GCPAGTRPCL DQVSCQPVEK FCNGRVDCSD HSDENCVSLK
QWSGIKVLAP TQPRSSSPPP PPLPPLSETN DLNTTLNVSS LLMNLDAQQC SQRHCSGNGR
CVDNSGDTVC VCSLGYSGDS CTDHLLQTVQ RPLVYGAAVL GAGVLVISVL AVVIKRKKNA
NMRRASPAAM KDTSMTDLEK KAETAPPTTA PVDTEKPEEA VSSVD
//
