GenomeNet

Database: UniProt
Entry: A0A2U9C3S0_SCOMX
LinkDB: A0A2U9C3S0_SCOMX
Original site: A0A2U9C3S0_SCOMX 
ID   A0A2U9C3S0_SCOMX        Unreviewed;      3283 AA.
AC   A0A2U9C3S0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN   ORFNames=SMAX5B_014637 {ECO:0000313|EMBL:AWP09692.1};
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:AWP09692.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP09692.1, 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; CP026253; AWP09692.1; -; Genomic_DNA.
DR   Proteomes; UP000246464; Chromosome 11.
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; 19.
DR   Gene3D; 2.10.25.10; Laminin; 12.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 19.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 6.
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   InterPro; IPR032485; LRP1-like_beta_prop.
DR   PANTHER; PTHR22722:SF5; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 1B; 1.
DR   PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF16472; DUF5050; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 2.
DR   Pfam; PF00057; Ldl_recept_a; 18.
DR   Pfam; PF00058; Ldl_recept_b; 9.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 19.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00192; LDLa; 19.
DR   SMART; SM00135; LY; 29.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF57424; LDL receptor-like module; 18.
DR   SUPFAM; SSF63825; YWTD domain; 6.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS01209; LDLRA_1; 7.
DR   PROSITE; PS50068; LDLRA_2; 19.
DR   PROSITE; PS51120; LDLRB; 16.
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   Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        3163..3184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          158..204
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          205..247
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          248..294
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          476..518
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          563..602
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          781..823
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          824..866
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          867..910
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1189..1233
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1234..1276
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          1828..1868
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          1915..1959
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1960..2002
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          2003..2046
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          2047..2089
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          2706..2748
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          2749..2792
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          2933..2966
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2969..3005
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3041..3077
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3114..3145
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          2659..2685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3262..3283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2659..2676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        16..31
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1377..1395
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1411..1423
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1418..1436
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1430..1445
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1450..1462
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1457..1475
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1469..1484
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1518..1533
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1541..1553
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1548..1566
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1560..1575
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1579..1591
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1586..1604
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1672..1690
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1705..1717
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1751..1763
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1758..1776
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1770..1785
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1832..1842
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2180..2192
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2187..2205
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2220..2232
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2227..2245
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2239..2254
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2279..2294
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2382..2394
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2389..2407
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2444..2459
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2468..2480
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2475..2493
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2937..2947
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2973..2983
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2995..3004
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3045..3055
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3067..3076
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3135..3144
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   3283 AA;  366719 MW;  A50083738C6CEAD9 CRC64;
     MCATNDSICL PAEKLCDGTD DCPDGSDEKL CDLCALDNGG CSHNCSIIPG EGFMCSCPLG
     MELGADNKTC HIQSFCAKHL KCSQKCEQEK SSVKCSCYEG WELESDMESC KSTDPFKPFI
     IFSNRHEIRR IELHKGEFSV LVPGLRNTIA LDFHLNESTL YWTDVVEDKI YRGKLSENGA
     LTSFEVVIQY GLATPEGLAV DWIAGNIYWV ESNLDQIEVA KLDGTMRTTL LAGEVEHPRA
     IALDPRDGIL FWTDWDASLP RIEAASMSGE GRRTIHRETG SGGWPNGLTV DYMERRIVWI
     DARSDAIYSA MYDGSGLIEV LRGHEYLSHP FAVTMYGGEV YWTDWRTNTL AKANKWTGHN
     VTVVQRTNTQ PFDLQVYHPS RQPQAPNPCA TSDGRGPCSH LCLINFNQTF SCACPHLMKL
     QPDRRTCKES RKFLLYARQI EIRGVDIDNP YYNYIISFTV PDIDNVTAVD YDAVEHRIYW
     SDVRTQTIKR AFINGTGVET VVSADLPNAH GLAVDWVSRN LFWTSYDANK KQINVARLDG
     SFKNAVIQGL DKPHCLVVHP LLGKLYWTDG DNISMANMDG SNRTTLFTNQ KGPVGLSIDY
     EKEQLYWISS VNSTINRCQM DGSKLEIMEG VKGKLTKATA LAIMGDKLWW ADQGSDQIGT
     CDKSDGGNWK VMRNNTSPMM HMRIYDEEVQ QAGINLCSNN NGDCSQLCLP TSHTTRACMC
     TAGYSLKTGQ QSCEGMGSFL LYSVHEGIRG IPLDPADKSD ALVPVSGTSL AVGIDFHAEN
     DTIYWVDMGL STISRAKRDQ TWREDVVTNG IGRVEGITVD WIAGNIYWTD QGFDVIEVAR
     LDGSFRYVVI SQGLDKPRAI TVHPVKGYLF WTEWGQYPRI ERSRLDGSQR LVLVNVSISW
     PNGISIDYEE SLLYWCDART DKIERINLET GENRELVLAN NNMDMFAVSV FEEYIYWSDR
     THANGSIKRG NKDNATDAVQ LRTGIGVQLK DIKVFNRARQ QGTNVCKNNG GCEQLCLYRG
     NGERTCACAH GMLAEDNRSC RDYDGYLLYS ERTILKSIHL SDETNLNAPI KPFEDPDHMK
     NVIALSFDYH GGGGKGANRV FFSDIHFGNI QQINDDGTDR KIVVDNVGSV EGLAYHRGWD
     TLYWTSYTTS TITRHTVDQS RSVAYNRNTV VTMSGDDHPR AFVLDECQDL MFWTNWNEQS
     PSIMRASLNG ANVLVIIGKD IKTPNGLAID HRAEKLYFSD ATLDKIERCE YDGSSRYVLL
     KNEPVHPFGL AVYGDYIFWT DWVRRAVLRA DKYTGGDMKV LRADIPQQPM GIVAVANDTN
     NCEFSPCRIN NGGCQDLCLP TSDGRVNCSC RGDRQLLDDN TCASLNISCG SVDDFECGNG
     DCINYSLTCD GMAHCKDKSD EKQSYCANRI CKKGYRRCMN GRCIGHQFWC DGTDDCGDHS
     DELPCNMTLC KVGEFQCKDG SCISNFSRCD QVVNCEDASD EMNCQATDCA RFFRLGVKGA
     SFQSCEKTTL CYLPSWVCDG NNDCGDYSDE RNCPDKRKPK CPVNFFACPS GRCIPMSWTC
     DKENDCENGA DETHCDKFCT STQFECGNHR CISSHWVCDG SDDCGDGSDE DQKCKSKTCS
     PEAFQCPGSH MCVPQRWKCD GDKDCPDGAD ESVKAGCMYT NNTCDAENEF MCQNRQCIPK
     HFVCDHDIDC SDGSDESPEC EYPTCGPDEF RCANGRCLNQ KKWECDGEFD CQDRSDEAPK
     NPRCTDTERT CNDSAFMCHN GKCLNETLLC DRNDDCGDGS DELNCFINEC LNSKLSGCSQ
     LCDDLKIGFK CRCHPGFQLK RDGKTCVDID ECTTTYPCSQ RCINTHGSFH CLCVDGFELN
     PNDPTICKST SEEEPYLIFA NRYYLRKLNL DGSNYTLIKQ GLNNAVALDF HYAEQMIYWT
     DVTTQGSMIR RMHMNGSNIE VLHRTSLSNP DGLAVDWVGG NLYWCDKGRD TIEVSKLNGA
     YRTVLVNNGL REPRAVAVDV RYGYLYWSDW GDNPHIGRIG MDGTNRSVIV EDKITWPNGL
     TLDFINDRIY WADAREDYIE FASLDGTNRH TVLSQDIPHI FAMTLFEEYI YWTDWETKSI
     NRAHKSLGTN KTTLISTLHR PMDIHIYHPY RQPEVLNHPC QTNNGGCSNL CLLSPGGGYK
     CACPTNFYLA NDQRTCMSNC TASQFVCKND KCIPFWWKCD TEDDCGDRSD EPAECPEFKC
     RPGQFQCGTG ICTNPAYICD GDNDCQDNSD EANCDIHVCL PSQFKCSHPS RCIPGIFRCN
     GQDNCGEGED EKDCPEVTCA PTQFQCAITK RCIPRVWVCD RDNDCVDGSD EPANCTQMTC
     GVDEFRCKDS GRCIPARWKC DGEDDCGDAS DEPKEECAGR HCPQDEFQCN NTLCKPLAWK
     CDGEDDCGDN SDENPEQCRR FQCPPTRAFR CHNDRVCLQV SKRCDGVNNC GDNSDELNCQ
     APPAVPTCEK DEFLCANSRC ISSTLRCNFF NDCEDYGSDE INCKTDTKLN DCRSNRTQCG
     DGDEAHCVTN GTDSFCACKP GFKKMGHQTC RDKNECLQFG VCSHMCNNTK GSYKCSCHKY
     FTRIHDTCKA DNMNSSRQVL YIADDNEIRS LDPGMPNWRY EQTFQGDASV RIDAMDLHVK
     SNRIFWTNWH TGRISSYELP GPSTSSSSSS SSNSHRNRRQ SEGRITNLQI KELKMPRGIA
     VDWVAGNLYW TDSGRDVIEV AQMSGQHCKT LISGMIDEPY AIVVDPQRGT MYWADWGNHP
     KIETAAMDGT LRQTLVHENI QWPTGLAVDY FNERLYWADA KLSVIGSVRL DGSDAVIAVS
     GIKNNLLHPF SIDVFEDYIY GVTYINNVVF RVNKFGKGPM ENLTTGINHA TDIVLYHRYK
     QPEMTNPCDR KKCEWLCLLS PSGPVCTCPN NYMADNGTCV ERPNPTQSPF SPPSGPCDIQ
     CQNGGSCFLN ARQVAKCRCQ PSYTGERCEI NQCRDYCKNG GTCTASHTGA ATCRCPKGFT
     GPTCNRHTCQ DYCVNGGNCS VNMGNQPTCS CPSEYLGDQC QYSQCEGYCH NGGTCLQTAN
     STKLCQCPTQ YIGYQCELDK CLFCGTGKCL TSSSGEVSCS CPNGQTQPSC YSCLDYCANG
     QCSVDTRTLL PQCKCPVGWT GYRCEVAAAS VDSSASSGST ASIVIPVLLL LLLALLVVGA
     ILWYKRRMRG AKGFQHHRMT NGAMNVEIGN PAYKIYEGDP DDDAGELLDS DFALDPDKPT
     NFTNPVYATL YMGAHNSRNS LASTDEKKEL LSQGDEDLSD PLA
//
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