ID A0A3Q3VS47_MOLML Unreviewed; 1016 AA.
AC A0A3Q3VS47;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSMMOP00000005216.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000005216.1}
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; A0A3Q3VS47; -.
DR STRING; 94237.ENSMMOP00000005216; -.
DR Ensembl; ENSMMOT00000005310.1; ENSMMOP00000005216.1; ENSMMOG00000004149.1.
DR OMA; SDQNDCY; -.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00053; EGF; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
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; IPR024731; EGF_dom.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR PANTHER; PTHR46513:SF5; PRO-EPIDERMAL GROWTH FACTOR; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00058; Ldl_recept_b; 3.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00135; LY; 7.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF63825; YWTD domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1016
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018533634"
FT TRANSMEM 866..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 123..164
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 490..532
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 557..600
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 601..643
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 735..773
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 805..846
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 817..834
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 836..845
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1016 AA; 112597 MW; AAA9235E8B99B0BF CRC64;
MLASTITAVL IYLVVKNSGT LALSTACWDE QLSGAGRNSS CIGKYPFLIF GHGKAIHRMD
LDGKNQRRLV AGVGSSILID FHFKEERVYW ADKHTGVIFK APVRKLYSSD KHISGLAVDW
IWNSVYWTSG EKGKIKKMDI NGKNARTILR HLTHPSSITI DPINRFLFWL SGETSSSIQR
SDVTGQRKTT LIKIATKQLK TLSIDREEKR LFWVQFGPQG ESAVSSSCSL LIFYLFLPGI
FQYSDQDKSL FTVLSHWGYH VNLKPMAKPP IDIKVVHFLS QPMADTPSSI PACDKQSGNC
ANVCSSLAEE GTCECSEGFA LDRQGTHCED VNECALWNHG CSLGCENIPG SYFCTCPKGY
ALLPDRKTCQ EIIPCKGNIT KCSHGCLKTD EGDVCVCPEG SLLQEDGKAC SGCSSTDKGG
CSQLCTPVTP TRWQCGCLPG YELHHDGKRC IAPGESYPNI HLFLCLPMFI VSFVCLLIKE
FLSIFSVRIL KVYYASTSHK TIERVNINGG SREVLVSVGL DSPEGLAIDW VHRKMYWADK
SKGLEKPRGI AVHPLKKLLF WTDIGAKPVV ERASLEGKNL AVIASTNLVS PTGLAIDFTE
DRLFWCDQRR GTVETAALDG SDRQVLLENQ VGRPFDLAVF EDRLWISDQE HQQLSSVHKR
TGRRLQHIHG NMLQPASIVV VHPLAKPGAD ICLHMNGGCA QVCESELGFA HCSCLPRYIL
SADRKSCLLA DALNRTQECY SLHCDINAQC LLNAGSPTCL CLEGFTGDGL LCAGEYFCSC
LETSLPSVPT TSPADDTSKY HNINSVERCP SSHESYCLYQ GVCLYFPEME SYACNCVSGY
MGERCQFSDL EWWELQQSEE EKRRNVVIAA CMLVVISLLS IAACVTYWFV FQTQSMHLCN
VIFLELKNYF GHSLPISLLQ SSCPRSIDDA FLLSTESNAL VMLAPIQPTT ISTNPSVHFY
FCVCLKVDWE FLIEEAIASL FQGAGRKQST LTQRPSGATS ILIFQAGHTY LYIGLY
//
