EGF_CANLF
ID EGF_CANLF Reviewed; 1216 AA.
AC Q9BEA0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Pro-epidermal growth factor;
DE Short=EGF;
DE Contains:
DE RecName: Full=Epidermal growth factor;
DE Flags: Precursor;
GN Name=EGF;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ohashi K., Takahashi N., Sugimoto C., Onuma M.;
RT "Canis familiaris epidermal growth factor (EGF) cDNA.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: EGF stimulates the growth of various epidermal and epithelial
CC tissues in vivo and in vitro and of some fibroblasts in cell culture.
CC Magnesiotropic hormone that stimulates magnesium reabsorption in the
CC renal distal convoluted tubule via engagement of EGFR and activation of
CC the magnesium channel TRPM6 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EGFR and promotes EGFR dimerization. Interacts
CC with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates
CC its degradation through the endoplasmic reticulum-associated
CC degradation (ERAD) (By similarity). Interacts with RHBDF2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; AB049597; BAB40599.1; -; mRNA.
DR RefSeq; NP_001003094.1; NM_001003094.1.
DR AlphaFoldDB; Q9BEA0; -.
DR SMR; Q9BEA0; -.
DR STRING; 9612.ENSCAFP00000016954; -.
DR PaxDb; Q9BEA0; -.
DR PRIDE; Q9BEA0; -.
DR GeneID; 403657; -.
DR KEGG; cfa:403657; -.
DR CTD; 1950; -.
DR eggNOG; KOG1215; Eukaryota.
DR InParanoid; Q9BEA0; -.
DR OrthoDB; 1174178at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0038029; P:epidermal growth factor receptor signaling pathway via MAPK cascade; ISS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR032485; DUF5050.
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; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR016317; Pro-epidermal_GF.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF16472; DUF5050; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR PIRSF; PIRSF001778; Pro-epidermal_growth_factor; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00135; LY; 9.
DR SUPFAM; SSF57184; SSF57184; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS51120; LDLRB; 9.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Growth factor; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1216
FT /note="Pro-epidermal growth factor"
FT /id="PRO_0000007536"
FT CHAIN 973..1024
FT /note="Epidermal growth factor"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007537"
FT TOPO_DOM 19..1033
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1034..1054
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1055..1216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 86..127
FT /note="LDL-receptor class B 1"
FT REPEAT 128..169
FT /note="LDL-receptor class B 2"
FT REPEAT 170..213
FT /note="LDL-receptor class B 3"
FT REPEAT 214..260
FT /note="LDL-receptor class B 4"
FT DOMAIN 316..357
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 358..398
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 399..439
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 437..479
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 485..525
FT /note="LDL-receptor class B 5"
FT REPEAT 526..568
FT /note="LDL-receptor class B 6"
FT REPEAT 569..611
FT /note="LDL-receptor class B 7"
FT REPEAT 612..655
FT /note="LDL-receptor class B 8"
FT REPEAT 656..698
FT /note="LDL-receptor class B 9"
FT DOMAIN 743..783
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 834..872
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 873..914
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 915..955
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 974..1015
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1068..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 320..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 327..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 343..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 362..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 369..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 384..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 403..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 410..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 425..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 441..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 449..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 465..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 747..758
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 754..767
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 769..782
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 838..849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 843..858
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 860..871
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 877..891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 884..900
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 902..913
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 919..932
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 926..941
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 943..954
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 978..992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 986..1003
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1005..1014
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1216 AA; 134414 MW; 72536D89D3310638 CRC64;
MLLPLIILWP VVFKCSFASL SDPENWNCPE VSPSGKGSPA CVGPAPFLIF SHGISIFRID
LEGTNHEQLV ADAGVSVIMD FHYNKERIYW VDPERQLLQR VFLNGTRQER VCNIEKNVSG
MAINWINEEL IWSNQQEGII TVTDMKGNNS RVLLRALNYP ANVAIDPIER FIFWSSEVAV
AGSLHRADLN GVEEKILLQT SERITAVSLD VLDKQLFWIQ YSRDGSNSHI YSCNYDGGSV
HLSKHLTQHN FFAMSLFGNQ IFYSTWKKKT IWIANKHSGK DMVRINLDSS FVPPGGIKVV
HPLLQPKAES GTWAPDQKLC KWKQGNCRGS TCGQDSKSYS CTCAEGYTLS QDGKYCEDVN
ECAFWNHGCT LGCENIPGSY YCTCPVGFIL LPDGKRCHQL IACPSNTSKC SHDCVLTSDG
PICFCPEGSV LEADGKTCSG CSSPDNGGCS QLCLPLSPVS WECGCFPGYD LQLDKQSCAA
SGPQPFLLFA NSQDIRHMHF DGTDYGTLLS QQMGMVFALD HDPVENKIYF AHTALKWIER
ANMDGSQRER LIEEGVDVPE GLAIDWIDRK FYWTDSGKSL IEGSDLNGKH REIIIKEDIS
QPRGIAVHPM AKRLFWTDMG INPRIESSSL QGIGRLVIAS SDLVWPSGIT IDYVTDKLYW
CDTKLSVIEM ANLDGSKRQR LAQNDVGHPF AMAVFEDHVW FSDWTMPSII RVDKRTGKNR
VRLRGSMLKP SSLVVVHPLA KPGAQPCLYQ NGGCEHICKE RFGTAQCLCR EGFVKAPDGK
MCLALNGHQI PAVGSEADLS NHVTPGDVLP RSEGFEDNIT ESQHMLVAEI MVSDADDCAP
VGCSTWAECV SEGENATCQC LKGFTGDGKL CFDIDECEMG ITICPPTSSK CVNTEGGYVC
QCSEGYRGDG IHCLDINECQ LGMHTCGENA TCTNMEGNYT CMCAGSLSEP GQICADSTPP
SHPMEDSHYS VRNGYRECPS SYDGYCLYNG VCMYIEAVDR YACNCVFGYV GERCQHRDLK
WELRHAGQGR QRQVAAVAVG VVVLVLLLLL GLGGAHCYRT KKLSSKNLKN PYEEPSREGS
SSRPSDSEAR MASFPQPWFV VIKEHQNLRN GSQPMALKDG ESADVSQFSS PEPGSVKRTS
WRNEHQLYKD TEQGCCTPPS SNRGTGSQSM EQSFSVPSYE AQPIALGVEK PQSLLSAKPL
LQQRAPDPPH QMKLIQ
