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Database: UniProt
Entry: A0A3Q4ADQ2_MOLML
LinkDB: A0A3Q4ADQ2_MOLML
Original site: A0A3Q4ADQ2_MOLML 
ID   A0A3Q4ADQ2_MOLML        Unreviewed;       953 AA.
AC   A0A3Q4ADQ2;
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   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000002110.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000002110.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A3Q4ADQ2; -.
DR   Ensembl; ENSMMOT00000002147.1; ENSMMOP00000002110.1; ENSMMOG00000001729.1.
DR   OMA; SHTCRDL; -.
DR   Proteomes; UP000261620; 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; 2.
DR   CDD; cd00112; LDLa; 6.
DR   Gene3D; 2.40.128.620; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
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; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24270:SF3; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 8; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 2.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00058; Ldl_recept_b; 4.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 8.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 5.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS51120; LDLRB; 4.
PE   4: Predicted;
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, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..953
FT                   /note="EGF-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018571931"
FT   TRANSMEM        876..897
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          349..388
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          474..517
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          518..560
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          561..604
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          605..649
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          747..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        21..33
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        40..55
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        60..72
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        67..85
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        122..137
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        144..156
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        151..169
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        163..178
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        185..197
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        192..210
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        232..244
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        239..257
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        251..266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        271..283
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        319..337
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   953 AA;  105379 MW;  330A036796BEA5B0 CRC64;
     MWTDVGKLLM LHLLLAELHC CVSGQFQCKN GRCVPTLWRC DDDDDCSDNS DEENCPKKTC
     ATTEFACKNG QCLPARWRCD GEPECPDGSD EADAICSRQT CPPEKFDCGG ATSKCVSLSW
     RCDGEQDCEN GADEEQCAAD AKACPSNDFQ CHNGKCVAPI FVCDGDDDCR DGSDEEKCSA
     PAPTCGQHEF RCNDSECIPA LWSCDGDPDC KDKSDESMER CSRRTEPQKP RCPVGEFQCG
     SGECVHMNWK CDGDADCKDK SDEANCPLMT CRPDEFQCGD GSCIHGTRQC NKVRDCPDYS
     DEAGCVNVTK CDGPGKFHCK NGECIDRSKV CDKVYDCKDG SDEPLNECDL NECADNNGGC
     SHICRDQKIG YDCDCPPGYK LLDKKTCGDI DECENPDACS QICINYKGDY KCECYEGYEM
     DPSTKTCKAV GKSPYLMFTN RHEIRRIDLL KSEYGQVVPT LKNAVALDVD VSTNKMFWSD
     LYHRKIYSAY INKATESQVE LIDSLHSPEG LAVDWVHKNI YWTDSGNKSI SVATGDGRKR
     KVLIATELSE PRAIAVDPHQ GFMYWSDWGD RAKIEKSGLN GVDRQVLVSE HIEWPNGITL
     DLSNRRLYWV DSKLHLLSSV DLNGDNRKVL LSSHQQLGHP FALTVFEDHI YWTDLEDEAI
     YSVNRLTGHD IAKVAEHLNN PLDLVVFHEQ RQPKAPDTCN MGSLPNGGCE YLCLKAPQIT
     EHSPKYTCAC PDGMELGPDM RRCATVRPRT TTAPTTTTPA TVTTTSATPT STPATTTTTP
     ATTTTLSTTT TSAATTLRPM TRRPTTPAPR QTPRSTSTKQ PRTPAAKSTE TSSLSSTHQT
     STSTHTPLLA PMAPNSIQRE SNGNLSHRGK NLIHTVVFPI LATVVIGLLC TGGYLVWRNW
     RSKNTKSMNF DNPVYRKTTE DDEDEIHIGR HSESIGHVYP AHVALSLEDD GYP
//
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