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Database: UniProt
Entry: A0A3Q0S5U2_AMPCI
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Original site: A0A3Q0S5U2_AMPCI 
ID   A0A3Q0S5U2_AMPCI        Unreviewed;      1191 AA.
AC   A0A3Q0S5U2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000018381.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000018381.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   STRING; 61819.ENSACIP00000018381; -.
DR   Ensembl; ENSACIT00000018875.1; ENSACIP00000018381.1; ENSACIG00000014322.1.
DR   GeneTree; ENSGT00940000162544; -.
DR   OMA; SHCLPAN; -.
DR   Proteomes; UP000261340; 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; 7.
DR   Gene3D; 4.10.1220.10; EGF-type module; 1.
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; 2.
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   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; PF12662; cEGF; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00057; Ldl_recept_a; 7.
DR   Pfam; PF00058; Ldl_recept_b; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 8.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 8.
DR   SUPFAM; SSF63825; YWTD domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 3.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS51120; LDLRB; 2.
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1191
FT                   /note="EGF-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018667743"
FT   TRANSMEM        1126..1146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1167..1188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          526..569
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          570..612
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          1079..1115
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          1042..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        54..69
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        93..108
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        132..147
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        152..164
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        159..177
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        171..186
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        192..204
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        211..226
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        253..268
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        273..285
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        280..298
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1105..1114
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1191 AA;  129016 MW;  C3F493B049C3FA22 CRC64;
     MGGCLFLCLA LLSGFLQVSV GPSKPSTSSN PIKCSLGFTP CSDNTECIQN NYFCDGETDC
     RDGSDEAKCS SSCERDQFQC AHGKMCIEKS QVCDGVAHCQ DRSDELECNK HMEGCSHQCD
     DKSSCIPSSF LCDGEKDCAD GSDESDCDKE DCSGTEFKCI SGQCVSATMR CDGHPDCRDR
     SDEEDCTKVS ACNTKLSCPQ SNECLVQEWI CDGDQDCKDG TDEKDCPVAP VNCGEFQWLC
     KSKTMCISTA WMCDGMKDCN DGSDETECQV ATCAPHQFQC GSQECLDPTL VCNGITNCAD
     GSDEGGSCQM NCAEADNTRC SQDCYKTPQG PRCHCAAGFR LMEDGLTCAD IDECDVQTPS
     VCSQLCINTP GSYKCDCQLG FIMEADGHHC KITGEPFLLS SVQTDIYMYG LRSGSLVMLP
     SSAKKAILSL DYDWKGQKVF WVSLDADAVM WSSLDQNMTG TLIKGVRADS IAVDWLGRNL
     YWINGVKSHI AAIKLATVSA RSLDQSIILD EDLDQPRSLA LLPHKGLMFW TEIGNVVKIE
     RAGMDGSERR AVVNSSLGWP GGVAVDAISE RVYWTDERLR AIGSAALDGD DIRILQMKET
     TNPFSVVVLN DMLYWSDPKK RVVQAAHKVS GKNHQVLLKR PRQPFAVTII HPTLQVGIEG
     PCKKMGCSHM CVLAPGPRAV CKCPSGLLLA EDGLTCSNLV NSAFLLLLSP STVTQIYLQS
     QHTAAEVKGW PEHLALQIPS VNKAIIMDYS LNEHTLFVTD DATTSLRSFK LKDSLLTSQG
     QLLELLDDTI TAMALDWITL NIYWSSDKQP RLXVTAATGT YTAILIKEGI RRVESIALHP
     PSGKVCFTNM DLQVSGKTAT IECASMDGAE RRAVWKDAVQ PTSLVFSNNG DKIFWADTSL
     GTIGSILIDG SGYTELKADD GLAAVALCDD LLLWMTVIDK TSLKAFSKSS QMGSNQCTEN
     NGNCEHLCLA TPGGHTCKCS HDHILLNDTH CSPEQHCPAG SRPCLDQLSC QPVEKFCNGQ
     ADCTDHSDEN CVGKKQRSGA EVFAPTQPHS SPPSSLPPLS EVTGQNTTLN VSTRLMNLDA
     QQCSQRLCSN NGHCVEMKGV TTCVCSLGYS GDSCQDHLLK TMQGSIVYAA VGLGAAVVII
     VAIVLVKRKK SANLRCLFVF SLKMTGHMGV SSLSFLSCGL FWACITSARG W
//
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