ID A0A060WB91_ONCMY Unreviewed; 674 AA.
AC A0A060WB91;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=GSONMT00071630001 {ECO:0000313|EMBL:CDQ64578.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ64578.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ64578.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ64578.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) 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; FR904477; CDQ64578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060WB91; -.
DR STRING; 8022.A0A060WB91; -.
DR PaxDb; 8022-A0A060WB91; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
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; cd00112; LDLa; 9.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 9.
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; 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; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 10.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00192; LDLa; 10.
DR SMART; SM00135; LY; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 9.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 9.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
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};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..674
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001589781"
FT DOMAIN 488..529
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 47..62
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 125..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 193..208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 232..247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 258..276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 270..285
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 290..302
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 297..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 309..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 330..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 349..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 391..406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 674 AA; 74038 MW; 87A1CE32F5564623 CRC64;
MAFCLLLCIA ILEITVLSAA AQTPLNCNLG TKPCKDGSEC VLHQHVCDGE ADCRDGSDEE
DCTVACNNGQ FLCAHGKKCI DQWQVCDGVA QCQDRSDELD CLNSMEGCVH HCDNKTRCLP
DTFLCDGERD CLDGTDEANC DSDSTDYLKS HHNVAEDGNN GNTTMSAPAP LKCPFGTKPC
WDRIECVLYN HVCDGEADCK DGSDEEECIL ECERGQFQCA HGKKCIDQRQ VCDGVAQCQD
RSDELDCLNS MEGCTHHCDK TRCLPDTFLC DGERDCLDGT DEANCADESC NSGEFRCTSG
QCLSVSMRCD GHPDCRDRSD EESCTEPPQC TTKLRCPQSQ ECLLEEWVCD REQDCKDGSD
EKNCKMVQLK CGNFQWACTS KSQCVPKAWR CDGTKDCADE SDEAGCGQVA TCPSHQFQCG
STWECLDTAL VCNTVRNCAN GSDEGGKCQA KCPDKTQCAH NCYSTPHGTR CGCKAGYRLQ
EDTVSCVDID ECEGGRPGVC SHLCVNTQGS FQCHCYPGYL LASDGRRCKI TGEPYLLASV
QTELFLFGLR SSSLDVLVSS AKKAILSLDY DWRDQKVYWV SLDSESIKWS SLDQKKRGTL
VKGIKSDCIA VDWVGRNLYW IDGIGGGRII AVGLNSTIIN SMDLTVILDE DFEQPRSLAL
LPQKGQDHVL VGDW
//