ID A0A493TDP5_ANAPP Unreviewed; 1138 AA.
AC A0A493TDP5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Pro-epidermal growth factor {ECO:0000256|ARBA:ARBA00017466, ECO:0000256|PIRNR:PIRNR001778};
GN Name=EGF {ECO:0000313|Ensembl:ENSAPLP00000023780.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000023780.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000023780.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000023780.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR001778}.
CC -!- SUBUNIT: Interacts with EGFR and promotes EGFR dimerization.
CC {ECO:0000256|PIRNR:PIRNR001778}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A493TDP5; -.
DR Ensembl; ENSAPLT00000038561.1; ENSAPLP00000023780.1; ENSAPLG00000011867.2.
DR GeneTree; ENSGT00940000158366; -.
DR Proteomes; UP000016666; Chromosome 4.
DR GO; GO:0016020; C: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 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; 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; PF00008; EGF; 2.
DR Pfam; PF07645; EGF_CA; 3.
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; 1.
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; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51120; LDLRB; 5.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW ECO:0000256|PIRNR:PIRNR001778}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1044..1066
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 128..169
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 525..567
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 568..610
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 611..654
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 655..697
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 842..880
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 881..922
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 923..963
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 983..1024
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 995..1012
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1014..1023
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1138 AA; 126608 MW; 2E2F2EADA033FDE9 CRC64;
MFLFLVAFLP VVFKIGFVSL SALQHWNCPN GYRLKTENSA CIDPVPFLLF SHGSAIFRID
TEGTNHERLV ADAGPSTLMD FHYTEEKVYW VDSERRLLQR IHLTGAKQER LCYIDKGISG
FAIDWINQDI LWANRQKSTI EATDMNGKKR RVILRNVGRP TKITIDAEQR LLFWSSDGTV
SSIYRASLNG SDVRNILRTT EKIKTISLDL VNIRLYWIQH DHGKEISHIG SCDYDGGAVH
LLQSSGRHQL LGMSLFADHL YYSELKSGMI WRANKYTGKV VVTISLKPSF FPPVEIKVVH
PFQQPGARTD LQDFERGVCD MTKEKCRRRT CRPDLRTHRC KCSSGFILSR NKQYCEDINE
CGFWNHGCTL GCVNIPGSYY CTCPRGFVLL PDRKTCHELI SCVSNDTECS HGCLQTSKGP
VCFCPEGSIL KVDGKTCTGC TSPDNGGCSQ ICSSLSPSSW ECACFPGYKL QGDRKHCTAI
GPRPFLLFAN GQDIRRISFD GTDYTSLLDW QMGIVLALDS DPVENKIYFA HTALKWIERA
DLDGSNREKV IQEAVDIPEG LAVDWINRKL YWTDRGKACI ERSNLNGMQR KMIIWEDISQ
PRGIAIHPFV KRLFWTEMGV RPRIDSSSLE GSDRQVIAST GLASPSGITL DYLANKLYWC
DAKLSVVESA NLDGSDRRIL AQNDVGRPFD VAVFEDHLWF SDWARPSLMR VDKKTGQNRV
RLRGSMLRPS SMVVVHPLAK PGTNPCLYQN GGCDQICENN FGVVHCMCHP GFVKTQDGKT
CRALDASNTT AGSISVQKEA GPVPTPETLL QNTQGNAIFK DIDSGEKKKT NILLMAEIMI
SDQDDCTALE CDVNAQCVLL EDGAVCQCLK GFTRKGKSCY DIDECAANTD RCNRNVSGCI
NTEGGYVCKC LEGYTGDGLH CYDIDECKMG THTCGENRTC TNTEGNFTCS CANGASGTTM
GCESTLSPTA VSNEYSTHPV QGDSMGCPPS YDSYCLHGGV CNYVSDLQDY ACNCVTGYVG
ERCQFSDLEW WEQQHAERVK VRNITIAVCV AVLVLLLLLG TLAAYCSRSQ NLYKKNLYAE
AIRDASSHTD NENVTLTCNK SRFAVVKECN SPPETKAVDL IECETADPHP ACPSEYGE
//
