ID A0A3B4T931_SERDU Unreviewed; 864 AA.
AC A0A3B4T931;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Very low density lipoprotein receptor {ECO:0000313|Ensembl:ENSSDUP00000002614.1};
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:ENSSDUP00000002614.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000002614.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A3B4T931; -.
DR STRING; 41447.ENSSDUP00000002614; -.
DR Ensembl; ENSSDUT00000002687.1; ENSSDUP00000002614.1; ENSSDUG00000001965.1.
DR GeneTree; ENSGT00940000155460; -.
DR OrthoDB; 3918101at2759; -.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
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; 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; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
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; 8.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 3.
PE 4: Predicted;
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, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..864
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017251780"
FT TRANSMEM 788..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..65
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 68..106
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 353..392
FT /note="EGF-like calcium-binding"
FT /evidence="ECO:0000259|SMART:SM00179"
FT DOMAIN 356..392
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 393..432
FT /note="EGF-like calcium-binding"
FT /evidence="ECO:0000259|SMART:SM00179"
FT DOMAIN 396..432
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 524..566
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 567..610
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 611..655
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 704..749
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 746..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 131..146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 151..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 158..176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 170..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 190..202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 197..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 236..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 243..261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 255..270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 275..287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 282..300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 294..309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 323..341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 864 AA; 94997 MW; E8718C1DF8612893 CRC64;
MVTSTPGILL LPMLICLQHC INVHGTKTEC EASQFQCGNG RCIPSVWQCD GDEDCTDGSD
ENSCVKKTCA EVDFVCQNGQ CVPKRWHCDG EPDCEDGSDE SLEICHMRTC RVNEFSCGAG
STQCIPIFWK CDGEKDCDNG EDEVNCGNIT CAPNEFTCAS GRCISRNFVC NSEDDCGDGS
DEVECAPSSC GPSEFQCGNS SCIPASWVCD DDVDCQDQSD ESPSRCGRHP TPPAKCSSSE
MQCRSGECIH KKWRCDGDPD CKDGSDEANC PVRTCGPDQF KCDDGNCILG SRQCNGVRDC
TDGSDEVNCK NMTQCHGPEK FKCRSGECIE MSKVCNKARD CPDWSDEPIK ECNLNECLLN
NGGCSHICKD MVIGFECDCT PGLQLIDHKT CGDINECLNP GICSQICINL KGGYKCECHN
GYQMDPTTGV CKAVGKEPCL IFTNRRDIRR LGLERKEYTQ IVEQQRNTVA LDADFDQQMI
FWADLGQKAI YSTVLDKRGD VGTHNKVIDN VQTPVGIAVD WIYKNMYWSD LSTKTISVAN
FNGTKQKVLF SRGLKEPASI AVDPLSGFLY WSDWGEPAKI EKSGMNGVDR QVLVATDIQW
PNGITLDLIK GRLYWVDSKL HMLCSVDLNG DNRKKVLQSS DYLAHPFALT VFEDRVFWTD
GENEAIYGAN KFTGSDVVTL ASNLNDPQDI IVYHELIQLS GTNWCTEKGE NGGCSYMCLP
APQINKHSPK YTCVCPEGQE LAADGLRCRP DPSTKGPSKD DGNVLIQPPP EANVSTSIQV
NSTARGSAAA WAILPVLLLA MAAAGGYLMW RNWQLKNQKS MNFDNPVYLK TTEEDLNIDI
TRHSANVGHT YPAISIVSTD DDLS
//
