ID A0A3L8SPT2_CHLGU Unreviewed; 903 AA.
AC A0A3L8SPT2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=DV515_00004719 {ECO:0000313|EMBL:RLW05919.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW05919.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW05919.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW05919.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW05919.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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:RLW05919.1}.
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DR EMBL; QUSF01000010; RLW05919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SPT2; -.
DR STRING; 44316.ENSEGOP00005020408; -.
DR Proteomes; UP000276834; 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; 2.
DR CDD; cd00112; LDLa; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
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; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 6.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 6.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 6.
DR PROSITE; PS51120; LDLRB; 4.
PE 4: Predicted;
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:UP000276834};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 822..847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..341
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 342..381
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 427..473
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 474..516
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 517..560
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 561..605
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 737..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 14..26
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 21..39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 122..137
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 141..153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 148..166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 160..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 180..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 187..205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 226..238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 233..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 245..260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 265..277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 272..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 284..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 346..356
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 903 AA; 99708 MW; 5A99D8C65E87B4CE CRC64;
MPQICCTTSA KKTCAESDFT CDNGHCIPAR WKCDGEEECP DGSDESEAAC ITVHWAKAAC
EGGFEEEHAQ ETGEDALCKG QGEQQFRLEP MVFSAYAKQV CPSEKISCGD LSNKCIPLSW
RCDGQKDCES GIDEAGCTPA CSPNEFQCSN KSCISIIFVC DGDNDCGDGS DERKCSPLTC
NPSEFQCNNS VCIPELWVCD HQPDCEDQSD ESVEKCGHDA KALNTCAAHE FRCGNGECIH
LNWKCDGDED CKDKSDEQDC PLVTCQPDEF QCGDGACIHG AKQCDKVRDC PDNSDEAGCV
QGVNECSMNN GGCSHICKDL KIGYECECPP GYKLLDKKTC GDIDECENPD ACSQICINYK
GDYKCECYEG YEMDTLSKNC KAVGKSPYLI FTNRHEVRKI DLVKRDYSRI IPMLKNVVAL
DVEVSTNRIY WCDLFYRKIY SAYIDKASDT AEQVILIDSQ LNSPEGLAID WVHKNIYWTD
SGNKTISVAT ADGSRRRTLF NSDLSEPRAI AVDPTQRFMY WSDWGDKAKI EKAGLNGVGR
QVLVTDNIEW PNGITLDLLN QRLYWVDSKL HSLSCIDFNG SNRKVLISSV DDLSHPFGLA
VFEDRVFWTD LENEAIFSAN RLNGLDISIL AENLNNPHDI VVFHELKQPK GERCPQDVMA
LNQICLSWQM KCSLMVLDER ECTAPDSCEL SPQPNGGCDY LCLPAPQISP HSPKYTCACP
DNMWLGPDMK KCYKDPPTTA TPAVVSTTTT SRAEGTTTTA GPGSANDTTE VVPKAVPEAT
ITTPSLHLHS TTSILIDSEM TTGNSNLSQH YANDDEGFGS TVTAAVIGIV IPVVVIGLLC
MGGYLIWRNW KRKNTKSMNF DNPVYRKTTE EEDEDEIHIG RTAQIGHVYP ARVALSLEDD
GLP
//
