ID A0A226N5Z5_CALSU Unreviewed; 1864 AA.
AC A0A226N5Z5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=ASZ78_003101 {ECO:0000313|EMBL:OXB63006.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB63006.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB63006.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB63006.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB63006.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXB63006.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFN01000187; OXB63006.1; -; Genomic_DNA.
DR STRING; 9009.A0A226N5Z5; -.
DR Proteomes; UP000198323; 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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 16.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 17.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
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; 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; PF00057; Ldl_recept_a; 16.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 17.
DR SMART; SM00135; LY; 11.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 17.
DR SUPFAM; SSF63825; YWTD domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 17.
DR PROSITE; PS51120; LDLRB; 4.
PE 3: Inferred from homology;
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};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REPEAT 17..61
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 702..744
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 745..788
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1524..1567
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1804..1840
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 205..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 246..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 258..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 278..296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 290..305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 339..354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 362..374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 369..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 381..396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 400..412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 407..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 442..454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 449..467
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 494..506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 501..519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 513..528
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 889..907
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 922..934
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 929..947
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 941..956
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 981..996
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1124..1136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1131..1149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1143..1158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1165..1177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1172..1190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1184..1199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1223..1238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1245..1257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1252..1270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1307..1322
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1332..1344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1339..1357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1351..1366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1808..1818
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1830..1839
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1864 AA; 209276 MW; 9D41AF57D1ACD1DA CRC64;
MSEDDHPHVL ALDECQNLMF WTNWNEQLPS IMRSTLSGKN AQVIISTDIL TPNGLTIDHR
AEKLYFSDGS LGKIERCEYD GSQRYVIVKS GPGTFLSLAV YDDYIFWSDG VRRAILRSSK
YTGGDTKVLR SDIPHQPMGI IAVANDTNSC ELSPCAQMNG GCHDLCLLTP DGRVNCSCRG
DRILIDDNRC VTKNSTCNIY SEFECGNGEC IDYQLTCDGT AHCKDKSDEK LFYCENRGCR
KGFKPCSNRR CVSRNRVCDG TNDCGDNSDE FDCKEFRCAD GTCIGKSAQC NQIIDCADAS
DEKNCNNTNC AYFYKLGIKS TGFISCNSTS LCILPEWICD GSNDCGDYTD ELKCPVQNKP
TCEENYFGCP SGRCILNTWL CDGQKDCEDG VDELHCDSSC PWNQFACSAN KCISKQWICD
GEDDCGDGLD ESDAICAPNN TCDENAFMCH NNICIPKQFV CDHDDDCGDG SDESLECGKY
NKIVSSFSFP EQSCNSSFFL CKNGKCIPQS NVCNNKEDCS DGSDEKSCHI NECLSKKVSG
CSQDCQDLPV GYKCKCWPGF QLKDDGKTCT DIDECSTGFP CSQQCINTYG TYKCLCADGY
EIQPDNPNGC KSLSDEEPFL ILADHHEIRK ISTDGSNYTL LKQGLNNVIA IDFDYREEFI
YWIDSSRPNG SRINRMRLNG SDIKVVHNTA VPNALAVDWI GKNLYWSDTE KRIIEVSKVN
GLYPTVLVSK RVKFPRDLSL DPQAGYLYWI DCCEYPHIGR VGMDGSNQTV VIETRISRPM
ALTIDYVNHR LYWADENHIE FSDMDGSQRH KVPNQDIPGV IALTLFEDYI YWTDGKTKSL
NRAHKTSGLG RLSLINSWHT ITDIQVYHSY RQPDGNYPIF FVQHIDFRCK TDKCIPFWWK
CDTVDDCGDG SDEPEECPEF RCQPGRFQCG TGLCALPAFI CDGENDCGDN SDELNCDTHV
CLSGQFKCTK NQKCIPINLR CNGQNDCGDE EDERDCRKLC LENFVLMYVT DFKQDDEIKY
LKTVVLQTIS SVKQQNTAFL NCGYVMKTQI VLMDRMKLTV TKKLVGLMNS SAKTTTVFQI
IGDVTAKMTV VIILMKRIVV STFYLSACFK EHSVLQHRYC ETGCSRDQFQ CSNGQCISAK
WKCDGHEDCK LGDDEKNCEP ASPTCSGSEY ICASGGCVSA SLKCNGEYDC ADGSDEMDCV
TECKEDQFRC KNKAYCIPVR WLCDGIHDCV DGSDEEDCVQ GGSICRADEF LCNNSLCKLH
FWVCDGEDDC GDNSDEVAEM CVKFPCPPTR PYRCRNNRVC LRPEQICNEV DDCGDNSDED
HCDKISYKAR PCKKDEFTCN DKKCIPMELQ CDWFDDCGDG SDEQDCKIRS EEQVLYVAND
TDILGFAYPF NYSDGHQQIS HIEHNSRITG MDAYFQGNMI VWSTQFNPGG IFYKKLHDEE
KRQSNSGLIC PEFKRPRGIA VDWIAGNIYW TDHSRMHWFS YYTTHWTSLR YSINVGQLNG
PNCTRLLTSI AGEPYAIAVN PKKGMMYWTV IGDRSHIEES SMDGTLRRIL VQKNLQRPTG
LVVDQFSQRL FWADFELSVI GSVLFDGSDS VVSVSTKQGL LHPHRIDVFE DYIYGAGPKN
GAFRVHKFGR SFVEYLSVDV DKAKSALIFH RYKQMDLPNP CLDLTCEFIC LLNPSGASCA
CPEGKSLVNG TCVDQSLLGR YLKLCLFQML PPTRLTCPLA KVVFFFEQGG PPAIVHWVLQ
DQTAIRQSAI IFAKMEEPAV SLLEISPFAA AYLSIQGTDV STFPVKPPVF IHHFVSTIPL
SKGQKNVCHH YCVNSESCTI SDDGSVECVC PVRFEGLKCE VDKCVRCHGG HCIINKDTND
IVCK
//
