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 27-MAR-2024, entry version 123.
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; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; 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 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; AB050947; BAB47391.1; -; mRNA.
DR RefSeq; NP_001009381.1; NM_001009381.1.
DR AlphaFoldDB; Q95ND4; -.
DR SMR; Q95ND4; -.
DR STRING; 9685.ENSFCAP00000059920; -.
DR GlyCosmos; Q95ND4; 10 sites, No reported glycans.
DR PaxDb; 9685-ENSFCAP00000000470; -.
DR GeneID; 493978; -.
DR KEGG; fca:493978; -.
DR eggNOG; KOG1215; Eukaryota.
DR InParanoid; Q95ND4; -.
DR OrthoDB; 5351433at2759; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005886; C:plasma membrane; 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:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
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 PANTHER; PTHR46513:SF5; PRO-EPIDERMAL GROWTH FACTOR; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00058; Ldl_recept_b; 4.
DR PIRSF; PIRSF001778; Pro-epidermal_growth_factor; 1.
DR PRINTS; PR00009; EGFTGF.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00135; LY; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF63825; YWTD domain; 2.
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 Disulfide bond; EGF-like domain; Glycoprotein; Growth factor; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1210
FT /note="Pro-epidermal growth factor"
FT /id="PRO_0000007538"
FT CHAIN 969..1020
FT /note="Epidermal growth factor"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007539"
FT TOPO_DOM 23..1029
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1030..1050
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1051..1210
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..211
FT /note="LDL-receptor class B 3"
FT REPEAT 212..258
FT /note="LDL-receptor class B 4"
FT DOMAIN 312..352
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 353..393
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 394..434
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 432..474
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 480..520
FT /note="LDL-receptor class B 5"
FT REPEAT 521..563
FT /note="LDL-receptor class B 6"
FT REPEAT 564..606
FT /note="LDL-receptor class B 7"
FT REPEAT 607..650
FT /note="LDL-receptor class B 8"
FT REPEAT 651..693
FT /note="LDL-receptor class B 9"
FT DOMAIN 738..778
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 830..868
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 869..910
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 911..951
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 970..1011
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1065..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 316..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 322..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 338..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 357..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 364..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 379..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 398..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 405..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 420..433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 436..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 444..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 460..473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 742..753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 749..762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 764..777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 834..845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 839..854
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 856..867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 873..887
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 880..896
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 898..909
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 915..928
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 922..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 939..950
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 974..988
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 982..999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1001..1010
FT /evidence="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
//
