ID A0A3B3R4N2_9TELE Unreviewed; 1128 AA.
AC A0A3B3R4N2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Epidermal growth factor {ECO:0000313|Ensembl:ENSPKIP00000012880.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000012880.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000012880.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3R4N2; -.
DR STRING; 1676925.ENSPKIP00000012880; -.
DR Ensembl; ENSPKIT00000037285.1; ENSPKIP00000012880.1; ENSPKIG00000000516.1.
DR GeneTree; ENSGT00940000158366; -.
DR OrthoDB; 5351433at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00135; LY; 10.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF63825; YWTD domain; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51120; LDLRB; 6.
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 Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..1128
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017249850"
FT TRANSMEM 994..1017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 102..143
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 144..185
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 549..591
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 592..634
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 635..678
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 679..721
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 933..974
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1024..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 945..962
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 964..973
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1128 AA; 121685 MW; 149AB10F591F8C3A CRC64;
MLARPRRGMS NVGDLSFGTR RFGSMLLAAL ATLLVHLASG GDPCRPGGPS ATGNGTCPAP
EAYLIFSYGQ AVFRIGADGG AQRRLLRGAG AVALLDFHYT DGRLYWVDTE SGIIQRTLLN
GTRRQKVHSA GRGIAGFAVD WIRNQLLWAN RDKGTIEGID SNGKNLRTVL ANLSNPSSIA
VDPSNRFIFW VSDTLTSSIQ KSGLDSGPTI TILKTSSRLG TLSLDVADRR LFWVQSSLGG
RATIGSCDYN GNTINLMKQP PHSRPLGMSV FLDNVYYTDT KARSIIRVSK HTGDKAVKIT
PNYMPKPPVS VKVVHPFVQP LPKAPPTTLK ALPGGLSSDL DGGCDVLTGD CVSVCTAHAT
TAVCQCQDGF TLSGHGNYCE DINECALWTH GCTLGCENIP GSYVCTCPKG FVLLPDMKTC
RELTPCAKTT PTCKHGCIQT DDGDVCACLA GSVLQPDGTT CTGCSLQDNG GCSQECVPLG
PGGWDCQCRP GYSLQGDGRS CKATGPRPYL IFANAIDVRR MDWDGTGDRG LLQEPRGAIL
ALDYDPVERK VYYASSSLRR IERASLDGSD REVLVSEGLD TPEGLAVDWI HRKLYWTDRG
LSTIERSDLN GLEREIIIDR ELQKPRGIAV HPQAKRLFWT DMGETPAVGS ASLDGEDRAV
VVSTGLLEPS GVAVDYAEGR LYWCDSKMGV IEEAGLDGST RRVLVENQVG RPFDIAVFED
LLWVTDWDRY VVLRLNKRTG QNLERVSGDV VRPASLVVVH PLAKPGADAC LHNNGGCDQL
CESRFGLAQC SCHSDFIESP SGGTCLPSNS TGPSLVHFQS GESGDDETHK AVVLKNETLS
DEAPLVKESG PEPTMEDQAV VTLATEKMVS DQDCSSLLCP THARCLQGAG SSTCQCLEGF
ISVGKQCVES PRASWVTTDT PADVTTQGQN RDRVENCPLS HETFCLNDGV CLYFPEIQSY
ACNCVSGFMG ERCQFSDLEW WQLQQAEQQK RLNVTIGVCV LLLVTLLSVG VGAIYCYRSR
RLSQKCPPAD DMSDTSGAED SRSATLDRGP LELYVTLESG PCGNGEDIHS TGCRTGQRRS
SVSSGKGESI ISQPISSPRP EVPSTGVHLK SVDNLIFLDD PRLQCQML
//
