ID   GRFA_MYXVL              Reviewed;          85 AA.
AC   P08072;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   02-DEC-2020, entry version 92.
DE   RecName: Full=Growth factor;
DE   AltName: Full=Secreted epidermal growth factor-like;
DE   Flags: Precursor;
GN   Name=MGF; OrderedLocusNames=m010L;
OS   Myxoma virus (strain Lausanne) (MYXV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX   NCBI_TaxID=31530;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3029424; DOI=10.1128/jvi.61.4.1271-1275.1987;
RA   Upton C., Macen J.L., McFadden G.;
RT   "Mapping and sequencing of a gene from myxoma virus that is related to
RT   those encoding epidermal growth factor and transforming growth factor
RT   alpha.";
RL   J. Virol. 61:1271-1275(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10562494; DOI=10.1006/viro.1999.0001;
RA   Cameron C., Hota-Mitchell S., Chen L., Barrett J.W., Cao J.-X.,
RA   Macaulay C., Willer D.O., Evans D.H., McFadden G.;
RT   "The complete DNA sequence of myxoma virus.";
RL   Virology 264:298-318(1999).
RN   [3]
RP   SYNTHESIS OF 30-83, DISULFIDE BONDS, AND FUNCTION.
RX   PubMed=2009268; DOI=10.1021/bi00227a020;
RA   Lin Y.-Z., Ke X.-H., Tam J.P.;
RT   "Synthesis and structure-activity study of myxoma virus growth factor.";
RL   Biochemistry 30:3310-3314(1991).
CC   -!- FUNCTION: Stimulates the growth of some tissues.
CC       {ECO:0000269|PubMed:2009268}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M15806; AAA46626.1; -; Genomic_DNA.
DR   EMBL; AF170726; AAF14898.1; -; Genomic_DNA.
DR   PIR; A26131; EGVZM1.
DR   RefSeq; NP_051724.1; NC_001132.2.
DR   SMR; P08072; -.
DR   GeneID; 932144; -.
DR   KEGG; vg:932144; -.
DR   Proteomes; UP000000867; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000742; EGF-like_dom.
DR   Pfam; PF00008; EGF; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Growth factor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..85
FT                   /note="Growth factor"
FT                   /id="PRO_0000007603"
FT   DOMAIN          33..77
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:2009268"
FT   DISULFID        45..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:2009268"
FT   DISULFID        67..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000269|PubMed:2009268"
SQ   SEQUENCE   85 AA;  9629 MW;  EDD4E94E41E9D4D6 CRC64;
     MVPRDLVATL LCAMCIVQAT MPSLDNYLYI IKRIKLCNDD YKNYCLNNGT CFTVALNNVS
     LNPFCACHIN YVGSRCQFIN LITIK