GenomeNet

Database: UniProt
Entry: Q95ND4
LinkDB: Q95ND4
Original site: Q95ND4 
ID   EGF_FELCA               Reviewed;        1210 AA.
AC   Q95ND4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-FEB-2019, entry version 102.
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   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
OC   Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ohashi K., Takahashi N., Sugimoto C., Onuma M.;
RT   "Felis catus epidermal growth factor (EGF) cDNA.";
RL   Submitted (NOV-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; AB050947; BAB47391.1; -; mRNA.
DR   RefSeq; NP_001009381.1; NM_001009381.1.
DR   ProteinModelPortal; Q95ND4; -.
DR   SMR; Q95ND4; -.
DR   STRING; 9685.ENSFCAP00000000470; -.
DR   PRIDE; Q95ND4; -.
DR   GeneID; 493978; -.
DR   KEGG; fca:493978; -.
DR   CTD; 1950; -.
DR   eggNOG; ENOG410IPSY; Eukaryota.
DR   eggNOG; ENOG410ZVIM; LUCA.
DR   HOVERGEN; HBG003858; -.
DR   InParanoid; Q95ND4; -.
DR   KO; K04357; -.
DR   OrthoDB; 1174178at2759; -.
DR   Proteomes; UP000011712; 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; 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; 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; 5.
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     21       {ECO:0000255}.
FT   CHAIN        22   1210       Pro-epidermal growth factor.
FT                                /FTId=PRO_0000007538.
FT   CHAIN       969   1020       Epidermal growth factor. {ECO:0000250}.
FT                                /FTId=PRO_0000007539.
FT   TOPO_DOM     23   1029       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1030   1050       Helical. {ECO:0000255}.
FT   TOPO_DOM   1051   1210       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       86    127       LDL-receptor class B 1.
FT   REPEAT      128    169       LDL-receptor class B 2.
FT   REPEAT      170    211       LDL-receptor class B 3.
FT   REPEAT      212    258       LDL-receptor class B 4.
FT   DOMAIN      312    352       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      353    393       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      394    434       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      432    474       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      480    520       LDL-receptor class B 5.
FT   REPEAT      521    563       LDL-receptor class B 6.
FT   REPEAT      564    606       LDL-receptor class B 7.
FT   REPEAT      607    650       LDL-receptor class B 8.
FT   REPEAT      651    693       LDL-receptor class B 9.
FT   DOMAIN      738    778       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      830    868       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      869    910       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      911    951       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      970   1011       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
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    321    321       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    814    814       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    851    851       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    925    925       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    934    934       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    316    327       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    322    336       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    338    351       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    357    368       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    364    377       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    379    392       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    398    409       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    405    418       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    420    433       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    436    448       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    444    458       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    460    473       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    742    753       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    749    762       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    764    777       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    834    845       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    839    854       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    856    867       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    873    887       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    880    896       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    898    909       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    915    928       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    922    937       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    939    950       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    974    988       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    982    999       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1001   1010       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   1210 AA;  133640 MW;  46EABA4C49886003 CRC64;
     MLLFLIILLP VVFKFSFVSL SVLQGWDCSE GSSSGKGNST CVGPEPFLIF SHGGSIFRID
     LDGTNYEQLV ADAGVSVIMD FHYYKERLYW VDLERQLLQR VFLNGTRQET VCNIEKNVSG
     MAINWINEEL IWSNQQEGII TVTDMKGNNS RVLLSALKYP ANVAIDPVER FIFWSSEVAG
     SLHRADLNGV EVKILLETSE RITAVSLDVL DKRLFWIQNN RDGSNSYICS CNYDGGSVHF
     NKHLTQHSLF AMSLFGDRIF YSTWKKKTIW IANKRKDMVR INLNPSFVPP GGTKVVHPLL
     QPKAESDAWA PGQKLCLRKG NCTGSVCEQD SKSHLCTCAE GYTLSPDGKH CEDVNECAFW
     NHGCTLGCEN IPGSYYCTCP VGFILLPDGK RCHQLISCPS NTSKCSHDCV LTSDGPICFC
     PEGSVLETDG KTCSGCSSPD NGGCSQLCLP LSPVSWECGC FPGYDLQLDK KSCAASGPQP
     FLLFANSQDI RHVRFDGTDY GSLLSQQMGM VFALDHDPVE NKIYFAHTAL KWIERANMDG
     SQRERLIEEA VDVPEGLAID WIDRKFYWTD RGKALIEGSD LNGKHREIII KEEVSQPRGI
     AVHPMAKRLF WTDMGINPRI ESSSLQGIGR RVIASSDLVW PSGITIDYLT DKLYWCDAKQ
     SVIEMANLDG SKRQRLAQND VGHPFAIAVF EDHVWFSDWT MPSVIRVNKR TGKNRVRLRG
     SMLKPSSLVV VHPLAKPGSD PCLHQNGGCE HICKERFGSA QCLCREGFVK APDGKMCLAL
     NGHQIPPAVG SEADLSNQVT PLDVLSRNRG SEDNSTESQH MLVAEIMVSD NDDCGPIRCG
     TWGQCVSEGE NATCQCLKGF TGDGKLCSDI NECGTSTTVC PPTSSKCINT EGGYVCQCSE
     GYRGDGIHCL DIDECQLGIH TCGENATCTN TEGNYTCMCA GTLSEPGQMC PDSTPPSVLM
     EDGRYSVRNS YQECPPSYDG YCLYNGVCMY IEAVDRYACN CVFGYVGERC QHRDLKWELR
     HAGQGRQRQV TVVAVCVVAL VLLLLLGLWG AHCYRTKKLP SKNLKNPYEE SSREVSRPTD
     SEAGMASCPQ PWFVVIKEHQ NLRNGSQSMA LKDSEAADVS QFSSRETGSV QLPSRRNEPQ
     VYMGAEQGCC IPPSSDKGPG PHGMQWGFHL PSCEAQPIAL GVEKSQSLLS ANPILQQRAS
     DLPHQKKLTQ
//
DBGET integrated database retrieval system