ID A0A3B4YGH8_SERLL Unreviewed; 809 AA.
AC A0A3B4YGH8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Low-density lipoprotein receptor-related protein 8-like {ECO:0000313|Ensembl:ENSSLDP00000028722.1};
GN Name=LRP8 {ECO:0000313|Ensembl:ENSSLDP00000028722.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000028722.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000028722.1}
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; A0A3B4YGH8; -.
DR Ensembl; ENSSLDT00000029569.1; ENSSLDP00000028722.1; ENSSLDG00000020700.1.
DR GeneTree; ENSGT00940000154819; -.
DR Proteomes; UP000261360; 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; 1.
DR CDD; cd00112; LDLa; 6.
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; 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; 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; 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; 6.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 6.
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};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 330..344
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT DOMAIN 369..384
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 471..513
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 514..557
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 558..602
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 81..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 98..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 105..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 117..132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 138..150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 145..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 189..201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 196..214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 208..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 228..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 235..253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 247..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 276..294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 809 AA; 89526 MW; A6CC6C7A3E8B11BE CRC64;
PGRWRCDGEP ECPDGSDEAE ETCMVSLFCF VFLLPPLRDH KTTAVISLSL LSLPTGKQTC
PPEKFDCGGS TNKCVSLSWR CDGEKDCENG ADEEDCACPS GEFMCANRKC LATVYVCDGD
DDCGDGSDEL KCTSPLTCGP NHLRCNTSEC VPLMWSCDGD PDCSDSSDEG PERCGRDGVP
YLPNRRANCT AGEFRCANGE CVRLTWKCDG DPDCKDKSDE SDCPLLTCRP DEFQCGDGSC
IHGTKQCNKV HDCPDHSDES GCVNATKCEG PLKFLCKNGE CIDSSKVCDS VKDCKDRSDE
PKKECGLNEC MINNGGCSHV CMDRPIGFEC QCPTGYQLLD KKTCGDIDEC ENPDACSQIC
INYKGDFKCE CYEGYEMDPV TKTCKAEGKS PYLLFTNRHE IRRIDLVKRD YSQVVSTQKN
AVALDLDVAN NRVFWCDRFH RKIYSDPSQQ VPLVDSSLQT PVGLALDWLQ HNLYWTDSGD
KSISVASVDG TKRRVLINTD LSEPRAIALD PHHGFMYWSD WGTRAKIEKA GMNGVDRQVL
VADNIEWPNG ITLDVANRRL YWVDSKLHLI ASVDLNGAHR RTHMSSAERL GHPYALAVFE
DRIYWTDRDR AAVFMANRLT GQEIHTLAEN LNDPHDIVVF HQLRQPQGNC NLGSVANGGC
EYLCLKAPQI TEHSPKYTCA CPDGQDLGPD MRGCVPGECL EVMVFGLVCA GVYLVWRNWR
RNSTKSMNFD NPVYRKTTGE GEEDEIHIGR TDGMGHHTHH HPYPQGVSMG VVGAGGGTCP
QFIALPLGGS MPDPGTHWYT EQPMLSTAK
//
