GenomeNet

Database: UniProt
Entry: Q9BEA0
LinkDB: Q9BEA0
Original site: Q9BEA0 
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   10-APR-2019, entry version 113.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   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
CC       epithelial tissues in vivo and in vitro and of some fibroblasts in
CC       cell culture. Magnesiotropic hormone that stimulates magnesium
CC       reabsorption in the renal distal convoluted tubule via engagement
CC       of EGFR and activation of the magnesium channel TRPM6 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with EGFR and promotes EGFR dimerization.
CC       Interacts with RHBDF1; may retain EGF in the endoplasmic reticulum
CC       and regulates its degradation through the endoplasmic reticulum-
CC       associated degradation (ERAD) (By similarity). Interacts with
CC       RHBDF2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
DR   EMBL; AB049597; BAB40599.1; -; mRNA.
DR   RefSeq; NP_001003094.1; NM_001003094.1.
DR   UniGene; Cfa.3524; -.
DR   ProteinModelPortal; 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; ENOG410IPSY; Eukaryota.
DR   eggNOG; ENOG410ZVIM; LUCA.
DR   HOGENOM; HOG000112345; -.
DR   HOVERGEN; HBG003858; -.
DR   InParanoid; Q9BEA0; -.
DR   KO; K04357; -.
DR   OrthoDB; 1174178at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042813; F:Wnt-activated receptor activity; IBA:GO_Central.
DR   GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0043388; P:positive regulation of DNA binding; 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; IPR013032; EGF-like_CS.
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   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Growth factor; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   1216       Pro-epidermal growth factor.
FT                                /FTId=PRO_0000007536.
FT   CHAIN       973   1024       Epidermal growth factor. {ECO:0000250}.
FT                                /FTId=PRO_0000007537.
FT   TOPO_DOM     19   1033       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1034   1054       Helical. {ECO:0000255}.
FT   TOPO_DOM   1055   1216       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       86    127       LDL-receptor class B 1.
FT   REPEAT      128    169       LDL-receptor class B 2.
FT   REPEAT      170    213       LDL-receptor class B 3.
FT   REPEAT      214    260       LDL-receptor class B 4.
FT   DOMAIN      316    357       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      358    398       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      399    439       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      437    479       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      485    525       LDL-receptor class B 5.
FT   REPEAT      526    568       LDL-receptor class B 6.
FT   REPEAT      569    611       LDL-receptor class B 7.
FT   REPEAT      612    655       LDL-receptor class B 8.
FT   REPEAT      656    698       LDL-receptor class B 9.
FT   DOMAIN      743    783       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      834    872       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      873    914       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      915    955       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      974   1015       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    117    117       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    148    148       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    818    818       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    855    855       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    929    929       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    938    938       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    320    332       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    327    341       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    343    356       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    362    373       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    369    382       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    384    397       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    403    414       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    410    423       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    425    438       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    441    453       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    449    463       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    465    478       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    747    758       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    754    767       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    769    782       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    838    849       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    843    858       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    860    871       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    877    891       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    884    900       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    902    913       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    919    932       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    926    941       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    943    954       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    978    992       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    986   1003       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1005   1014       {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
//
DBGET integrated database retrieval system