ID A0A3B4VCH8_SERDU Unreviewed; 1647 AA.
AC A0A3B4VCH8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=LDL receptor related protein 5 {ECO:0000313|Ensembl:ENSSDUP00000028546.1};
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:ENSSDUP00000028546.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000028546.1}
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 STRING; 41447.ENSSDUP00000028546; -.
DR Ensembl; ENSSDUT00000029040.1; ENSSDUP00000028546.1; ENSSDUG00000020552.1.
DR GeneTree; ENSGT00940000156574; -.
DR OMA; HTPCEDN; -.
DR OrthoDB; 3107655at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035676; P:anterior lateral line neuromast hair cell development; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0031101; P:fin regeneration; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR GO; GO:0032474; P:otolith morphogenesis; IEA:Ensembl.
DR GO; GO:0035677; P:posterior lateral line neuromast hair cell development; IEA:Ensembl.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0045124; P:regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
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; PTHR46513:SF16; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 5; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF14670; FXa_inhibition; 4.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00058; Ldl_recept_b; 11.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00135; LY; 20.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS51120; LDLRB; 14.
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|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1647
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017310191"
FT TRANSMEM 1397..1417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 125..167
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 168..211
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 212..254
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 303..342
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 390..432
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 433..475
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 476..519
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 520..562
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 609..646
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 692..734
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 735..783
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 784..826
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 827..868
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 917..954
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 1045..1087
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1088..1132
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1133..1175
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1225..1263
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 1489..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1289..1304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1307..1319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1314..1332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1326..1341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1345..1357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1352..1370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1364..1379
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1647 AA; 183264 MW; 6C7246A682AB2D1F CRC64;
MGLKRRRLEM GGLLAVLLLR SCLLSVVHGS PLLLFANRRD VRLVDAEGVR GESAIVVSDL
EDAAAVDFLY AEGLIFWTDV SEEAIKQTHW NQSSNSLKEA LGTGQTVVVS GLDSPDGLAC
DWLGRKLYWT DSETNRIEVA NLDGTSRKVL FWMDLDQPRA VALNPAQRYM YWTDWGEEPR
IERAGMDGSN RKVIVNADIY WPNGLTIDLV EQKLYWADAK LSFIHKANLD GSARETVVEG
TLTHPFALTL SEETLYWTDW QTRSIHACNK HSGDKAREIL SGIYSPMDIQ VLEPYRQPYI
QTPCSDNNGG CSHLCLLSPV QPFYSCACPT GVQLKPDGKT CKPGAEQVLL LARRTDLRRI
SLDLPDFTDI VLQVDDIRHA IAIDYDPVEG YVYWTDDEVR AIRRSHIDGS NAMILVTTEI
NHPDGIAVDW VARNLYWTDT GTDRIEVTRL NGTSRKILIS ENLDEPRAIV LDPVNGYMYW
TDWGEHPKIE RANLDGTDRV VLLNSSLGWP NGLAIDYAAG KLYWGDAKTD KIEVINVDGS
NRQTLLEDKL PHIFGFTLLG DYIYWTDWQR RSIERVHKAT AVREIIIDQL PDLMGLKATK
VTEANGTNGC ALENGGCSHL CFWRRQAVSC ACPMGMELLS DLQTCVVPEA FLLFTNRDNI
RSISLGTNSN DVAIPLTGVK EASALDFDVS ERRIYWTDIQ AKTISRAYMN GSSVEHVIEF
GLDYPEGMAV DWMGRNIYWA DTGTNRIEVA RLDGQYRQVL VCKDLDNPRS LDNPRSLALD
PANGYMYWTE WGGRPRIARA YMDGSTIMTL VDKVGRANGL TIDYVDHRLY WTDLDTCMIE
STNMQGLQRE IIVDDLPHPF GLTQYRDFIY WTDFNLRSIE RADKRSGLNR TVVLQGQLEL
MLDILVFHSS RQDGTNECSH NNGNCAHLCL ATPAGAQCRC ASHYTLNPDG RNCSSPSSFL
LFSQKASISR MVLGEQSPDI ILPIHVLRNV RAVSYDPLDR LVYWLDGRQN IRRARDDGAM
SMIVSSTVQP VDNQLHDLSL DPYSRHIYWT CETTNTINVQ RMDGHTVGVV LKDDTDKPRA
IVVNAEKGYM YFTTVQERSA KIEGASLDGT ERESLFTTGL IRPVALALDN KLGKLFWVDA
DLKRIESSDL TGANRIVLQD SNILQPMGLT VLGDHLYWID RQQQMIERVD KLTGDGRTRI
QGRISYLTSI HAVEEMDPQE FASHPCSRDN GGCSHICIAK GDGTPRCSCP MHLVLLQDLL
RCGEPPTCST EQFTCSTGEI DCIPMAWRCD GFSECEDGSD EENCPVCSAF QFQCDKGGCI
DAQRRCNGEP DCADNSDEQD CETICPPNQF RCGDNQCITK KQQCDNYSDC PDGSDELACE
YVSPPSSGIP NTGPNTIGPV IAIILLVFVI GGAYFVCQRV VCRRYKGPSG TFPHEYISGT
PHVPLNFIAP SSSQHGTFQG ISCGKSIMSS VSLMGSSSSG APLYDRNHVT GASSSSSSST
KGAFYPQILN PPPSPATDRS LYNTEIFYSS NSPSTTRSYR PYHPVRGAAP PTTPCSTDVC
DSDYTPHHLP AGLASSAGRW KATGHGSHGK HNKYYMDLNS DSDPYPPPPT PRSQYLSAEE
SCPPSPSTER SYFHLCPPPP SPCTDSS
//
