ID A0A3B3SS34_9TELE Unreviewed; 1126 AA.
AC A0A3B3SS34;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS00022, ECO:0000259|PROSITE:PS01186};
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:ENSPKIP00000033522.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000033522.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B3SS34; -.
DR STRING; 1676925.ENSPKIP00000033522; -.
DR Ensembl; ENSPKIT00000014412.1; ENSPKIP00000033522.1; ENSPKIG00000013211.1.
DR GeneTree; ENSGT00940000155188; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR041161; EGF_Tenascin.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR PANTHER; PTHR46708:SF3; TENASCIN-X; 1.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF18720; EGF_Tenascin; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00181; EGF; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1126
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017252455"
FT DOMAIN 227..238
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS00022,
FT ECO:0000259|PROSITE:PS01186"
FT DOMAIN 290..301
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS00022"
FT REGION 189..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..981
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1126 AA; 122368 MW; E47A594D7636E9BC CRC64;
MDVRFPPRRF EMFFFMSFFC VLLPPSDLQS IASDKNPTSV PAQTSYSVKI IPSKPQTSSQ
NVVLTEQSPA ASAKVGQEQV LANHSQPTLA LPAQTSNQRT LGDASHTSPH SPVKLLILDT
CIEKDKQGDT ANQTRGLSQE VDLDPGSSLI LTHKISVVPA SCAGSCDSEF SALRKRLEKL
EMEVSTLRRK CGGPESSCPP PQRGGEENGD GCPDDCSDQG RCEKGKCVCF PGFIGPDCGT
AACPPGDCGS RGRCVRGKCE CDAGFSGVHC TTAPCPGNCS GKGRCVQGRC VCHPGYSGPD
CKCKDGHGGT DCERDSSGSV MTTMTIETVT MTLTPENDTI KEKIHGKLAK TILSKNEEKK
NPQRTLRRGE GREEMENISK TKVSSDLKPD TTESHSEVDL GLKSNTTKSY NKLDLDLKLN
TTKSQPKLDL GLKSNATKSQ PKLDLGVKSN TTKSQPKLDL GVKSNATKPH PKPDMFVKSN
ATKSQPKPDL GVKSNTTKSH AKADSDLKPG GAKDNEGFES KKNVMVKKLT IATTVHSNTS
RSGQMGHKVV QAILQQPKWN IEEHQTKTRK LDSKLQKKED DKRSKSDIKM SVDIKRDSAN
QTHIKSGKLI YHNVSRASAF VNHTNVELKG KGSSAKATDR TAPGKVTEKT ILAVKNASKI
LQKTNISQGK VNRTQTTDDH AKPKHNQGDN LRKSGVVPVS DTGSSTVALG NKTALSNANA
GSVKYAISSV KATVNQRMNT AASKGSEDER LKTENNINGT SAQTNSASAE SETLPRLASK
NIQTRNGTRP TLAGPHHLDR GPQHGRGFPK MQSQPLKEEI IMGPTGSQGS AARNASRSGQ
RTQEMQKDIT SIQTDVPNKT RIQAEIKRNN SSITKLKEAS TKISYNRTSS HTVNTGKVDI
HPDPRMETNR SSSSARKGEA AFISIRVKNV TSRGFTIVWE APQRSFKNFT LTRREYRTEM
EEEDEVEENK EEEEEEEEQS EGGALPDRMN IDQSALGKGV GHTKISNNSI TVHVSLKPHN
DSRAKTHLRR FTQVVAGSAR SLSFRNLHPQ SRYSVSLYGT SLGLRSKIHR ITVTTAPDSP
TDLLFSDVTH SSLSVSWTKP RLAVDGFKVT YTNTDNGKAD PCLCYL
//
