ID EGF_PIG Reviewed; 1214 AA.
AC Q00968; O62759; Q9BDQ0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 24-JAN-2024, entry version 140.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Uterus;
RX PubMed=11518619; DOI=10.1016/s0739-7240(01)00097-2;
RA Kim J.G., Vallet J.L., Christenson R.K.;
RT "Characterization of uterine epidermal growth factor during early pregnancy
RT in pigs.";
RL Domest. Anim. Endocrinol. 20:253-265(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 389-962.
RC STRAIN=Danish Landrace;
RX PubMed=9741816; DOI=10.1080/00365519850186463;
RA Jorgensen P.E., Jensen L.G., Sorensen B.S., Poulsen S.S., Nexo E.;
RT "Pig epidermal growth factor precursor contains segments that are highly
RT conserved among species.";
RL Scand. J. Clin. Lab. Invest. 58:287-298(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 970-1022, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=2015058; DOI=10.1677/jme.0.0060063;
RA Pascall J.C., Jones D.S.C., Doel S.M., Clements J.M., Hunter M., Fallon T.,
RA Edwards M., Brown K.D.;
RT "Cloning and characterization of a gene encoding pig epidermal growth
RT factor.";
RL J. Mol. Endocrinol. 6:63-70(1991).
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; Single-pass type I membrane protein.
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DR EMBL; AF336151; AAK18830.1; -; mRNA.
DR EMBL; AF053364; AAC14024.1; -; mRNA.
DR EMBL; X59516; CAA42102.1; -; mRNA.
DR PIR; S17294; S17294.
DR RefSeq; NP_999185.1; NM_214020.1.
DR AlphaFoldDB; Q00968; -.
DR SMR; Q00968; -.
DR STRING; 9823.ENSSSCP00000028117; -.
DR GlyCosmos; Q00968; 7 sites, No reported glycans.
DR PaxDb; 9823-ENSSSCP00000028117; -.
DR PeptideAtlas; Q00968; -.
DR GeneID; 397083; -.
DR KEGG; ssc:397083; -.
DR CTD; 1950; -.
DR eggNOG; KOG1215; Eukaryota.
DR InParanoid; Q00968; -.
DR OrthoDB; 5351433at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; 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; IPR032485; LRP1-like_beta_prop.
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; PF16472; DUF5050; 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; 7.
DR SMART; SM00135; LY; 10.
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; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51120; LDLRB; 9.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Growth factor; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1214
FT /note="Pro-epidermal growth factor"
FT /id="PRO_0000007544"
FT CHAIN 970..1022
FT /note="Epidermal growth factor"
FT /id="PRO_0000007545"
FT TOPO_DOM 23..1031
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1032..1051
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1052..1214
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 314..355
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 356..396
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 397..437
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 435..477
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 483..523
FT /note="LDL-receptor class B 5"
FT REPEAT 524..566
FT /note="LDL-receptor class B 6"
FT REPEAT 567..609
FT /note="LDL-receptor class B 7"
FT REPEAT 610..653
FT /note="LDL-receptor class B 8"
FT REPEAT 654..696
FT /note="LDL-receptor class B 9"
FT DOMAIN 741..781
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 832..869
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 870..911
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 912..952
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 971..1012
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1193..1214
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 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 360..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 367..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 382..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 401..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 408..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 423..436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 439..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 447..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 463..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 745..756
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 752..765
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 767..780
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 835..846
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 840..855
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 857..868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 874..888
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 881..897
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 899..910
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 916..929
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 923..938
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 940..951
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 975..989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 983..1000
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1002..1011
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 634
FT /note="Q -> R (in Ref. 2; AAC14024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1214 AA; 133506 MW; 83D10409057458CF CRC64;
MLLFLILLLP VVLKFSFVSL SAPARWNCPE GSPSGNGNAT CVGPAPFLIF SHGNSIFRID
LEGTNHEQLV ADAGISVLMD FHYNEERIYW VDLERQLLQR VFLNGTRQEK VCNLEKNVSG
MAINWINEEL IWSNQQEGTI TVTDMKGNNS RVLLSALKYP ANVAVDPVER LMFWSSVVAG
SLHRADVTGV EVRLLLETSE EIAAVSLDVL DKRLFWIQYN REGGSSRICS CDYDGGSVHF
SKHLTQHNVF AMSLFGDHIF YSTWKKKTIW VANKHTGKDM VKMNLNPAFV PPGGIKVVHP
LVQPKAEGDA WASDQKLCKL RKGNCRGSMC GQEPKSHVCT CAEGYTLSQD GRKCEDVNEC
AFWNHGCTLG CENTPGSYYC TCPAGFVLLP DGKRCHQLIS CPSNVSECSH DCVLTSDGPI
CFCPEDSVLE ADGKTCSGCS SPDNGGCSQL CLPLSPVTWE CGCFPGYDLQ LDKKSCRASG
PPPFLLFANS QDIRHMHFDG TDYETLLNQQ IGMVLALDHD PVENKVYFAH TALKWIERAN
MDGSQRERLF EEAVDVPEGL AIDWIGRKFY WTDRGRSLIE GSDLNGKYRE IIIKEDISQP
RGIAVHPVAK RLFWTDMGTN PRIESSSLQG IGRQVIASSD LVWPSGITID YLTDKLYWCD
AKQSVIEMSN LDGSRRQRLA QNDVGHPFAV AVFEDHVWFS DWTMPSVIRV NKRTGKNRVR
LRGSMLKPSS LVVVHPLAKP GTNPCLHQNG GCEHICKESF GTAQCLCHEG FLKAPDGKMC
LALNGQEILA GRGKDLSDGV MPVDTLPRSR ELEDNLTESQ HILVAEIMVS DDEDCGAAGC
SAQARCVTEG EDATCQCLKG FAGDGNLCSD IDECELGTSV CPPTSSECIN TEGGHVCRCS
EGYQGDGIHC LDIDECQLGV HTCGENATCT NTEGNYTCTC AGRPSEPGRI CPDPTPPSHL
GEDGRYSVRN SYSECPPSHD GYCLHGGVCM YIEAVDSYAC NCVFGYVGER CQHRDLKWWE
LRHAGLGRQW NVTVVAVCVV VLVLLLLLGL WGAHYYRTQK LLSKNPKNPY EESGRDVSGI
RPADGEAGMS SCPQPWFVVI KEHQNLRNGS QPGAPKDGLG ADVGQFSSLE PGSLQPTSWR
KEPQMYMDTE QGCCIPSSSD KGSGPQGIGY SFHLPSYGAR SIAVGVEKSH SLLSANPLRQ
QRAPDPPHQM ELTQ
//
