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Protransforming growth factor alpha [Cleaved into: Transforming growth factor alpha (TGF-alpha) (EGF-like TGF) (ETGF) (TGF type 1)]

 TGFA_HUMAN              Reviewed;         160 AA.
P01135; A8K286; Q15577; Q53SK7; Q9BS56; Q9UEI3; Q9UKM1; Q9UKM2;
Q9UKM3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 188.
RecName: Full=Protransforming growth factor alpha;
Contains:
RecName: Full=Transforming growth factor alpha;
Short=TGF-alpha;
AltName: Full=EGF-like TGF;
Short=ETGF;
AltName: Full=TGF type 1;
Flags: Precursor;
Name=TGFA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=6088071; DOI=10.1016/0092-8674(84)90550-6;
Derynck R., Roberts A.B., Winkler M.E., Chen E.Y., Goeddel D.V.;
"Human transforming growth factor-alpha: precursor structure and
expression in E. coli.";
Cell 38:287-297(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2464748; DOI=10.1210/mend-2-11-1056;
Jakowlew S.B., Kondaiah P., Dillard P.J., Sporn M.B., Roberts A.B.;
"A novel low molecular weight ribonucleic acid (RNA) related to
transforming growth factor alpha messenger RNA.";
Mol. Endocrinol. 2:1056-1063(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=8224876; DOI=10.1016/0378-1119(93)90210-T;
Qian J.F., Lazar-Wesley E., Breugnot C., May E.;
"Human transforming growth factor alpha: sequence analysis of the 4.5-
kb and 1.6-kb mRNA species.";
Gene 132:291-296(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8100397;
Qian J.F., Feingold J., Stoll C., May E.;
"Transforming growth factor-alpha: characterization of the BamHI,
RsaI, and TaqI polymorphic regions.";
Am. J. Hum. Genet. 53:168-175(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10552925; DOI=10.1006/geno.1999.5962;
Machida J., Yoshiura K., Funkhauser C.D., Natsume N., Kawai T.,
Murray J.C.;
"Transforming growth factor-alpha (TGFA): genomic structure, boundary
sequences, and mutation analysis in nonsyndromic cleft lip/palate and
cleft palate only.";
Genomics 61:237-242(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), AND TISSUE
SPECIFICITY.
PubMed=10523832; DOI=10.1038/sj.onc.1203091;
Xu X., Liao J., Creek K.E., Pirisi L.;
"Human keratinocytes and tumor-derived cell lines express
alternatively spliced forms of transforming growth factor-alpha mRNA,
encoding precursors lacking carboxyl-terminal valine residues.";
Oncogene 18:5554-5562(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) System Donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
PubMed=2907605; DOI=10.1128/MCB.8.12.5549;
Jakobovits E.B., Schlokat U., Vannice J.L., Derynck R., Levinson A.D.;
"The human transforming growth factor alpha promoter directs
transcription initiation from a single site in the absence of a TATA
sequence.";
Mol. Cell. Biol. 8:5549-5554(1988).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
PubMed=10066034; DOI=10.1034/j.1399-0004.1999.550111.x;
Collin G.B., Marshall J.D., Naggert J.K., Nishina P.M.;
"TGFA: exon-intron structure and evaluation as a candidate gene for
Alstrom syndrome.";
Clin. Genet. 55:61-62(1999).
[14]
DISULFIDE BONDS.
PubMed=1632509; DOI=10.1016/0003-2697(92)90331-Z;
Bean M.F., Carr S.A.;
"Characterization of disulfide bond position in proteins and sequence
analysis of cystine-bridged peptides by tandem mass spectrometry.";
Anal. Biochem. 201:216-226(1992).
[15]
PALMITOYLATION AT CYS-153 AND CYS-154.
PubMed=8910478; DOI=10.1074/jbc.271.45.28502;
Shum L., Turck C.W., Derynck R.;
"Cysteines 153 and 154 of transmembrane transforming growth factor-
alpha are palmitoylated and mediate cytoplasmic protein association.";
J. Biol. Chem. 271:28502-28508(1996).
[16]
INTERACTION WITH SNTA1 AND SDCBP.
PubMed=10230395; DOI=10.1016/S1097-2765(00)80470-0;
Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J.,
Arribas J.;
"A role for a PDZ protein in the early secretory pathway for the
targeting of proTGF-alpha to the cell surface.";
Mol. Cell 3:423-433(1999).
[17]
INTERACTION WITH CNIH AND GORASP2.
PubMed=17607000; DOI=10.1242/jcs.004200;
Perez Castro C., Piscopo D., Nakagawa T., Derynck R.;
"Cornichon regulates transport and secretion of TGFalpha-related
proteins in metazoan cells.";
J. Cell Sci. 120:2454-2466(2007).
[18]
INTERACTION WITH NKD2.
PubMed=18757723; DOI=10.1073/pnas.0806298105;
Ding W., Li C., Hu T., Graves-Deal R., Fotia A.B., Weissman A.M.,
Coffey R.J.;
"EGF receptor-independent action of TGF-alpha protects Naked2 from
AO7-mediated ubiquitylation and proteasomal degradation.";
Proc. Natl. Acad. Sci. U.S.A. 105:13433-13438(2008).
[19]
STRUCTURE BY NMR OF TGF-ALPHA.
PubMed=2261437; DOI=10.1021/bi00486a005;
Kline T.P., Brown F.K., Brown S.C., Jeffs P.W., Kopple K.D.,
Mueller L.;
"Solution structures of human transforming growth factor alpha derived
from 1H NMR data.";
Biochemistry 29:7805-7813(1990).
[20]
STRUCTURE BY NMR OF TGF-ALPHA.
PubMed=2050136; DOI=10.1111/j.1432-1033.1991.tb16050.x;
Harvey T.S., Wilkinson A.J., Tappin M.J., Cooke R.M., Campbell I.D.;
"The solution structure of human transforming growth factor alpha.";
Eur. J. Biochem. 198:555-562(1991).
[21]
STRUCTURE BY NMR OF TGF-ALPHA.
PubMed=8338831; DOI=10.1021/bi00080a003;
Moy F.J., Li Y.C., Rauenbuehler P., Winkler M.E., Scheraga H.A.,
Montelione G.T.;
"Solution structure of human type-alpha transforming growth factor
determined by heteronuclear NMR spectroscopy and refined by energy
minimization with restraints.";
Biochemistry 32:7334-7353(1993).
-!- FUNCTION: TGF alpha is a mitogenic polypeptide that is able to
bind to the EGF receptor/EGFR and to act synergistically with TGF
beta to promote anchorage-independent cell proliferation in soft
agar.
-!- SUBUNIT: Interacts with the PDZ domains of MAGI3, SDCBP and SNTA1.
The interaction with SDCBP, is required for the targeting to the
cell surface. In the endoplasmic reticulum, in its immature form
(i.e. with a prosegment and lacking full N-glycosylation),
interacts with CNIH. In the Golgi apparatus, may form a complex
with CNIH and GORASP2. Interacts (via cytoplasmic C-terminal
domain) with NKD2. {ECO:0000269|PubMed:10230395,
ECO:0000269|PubMed:17607000, ECO:0000269|PubMed:18757723}.
-!- INTERACTION:
P00533:EGFR; NbExp=2; IntAct=EBI-1034374, EBI-297353;
Q9EQJ9:Magi3 (xeno); NbExp=4; IntAct=EBI-1034374, EBI-7455245;
Q969F2:NKD2; NbExp=3; IntAct=EBI-1034374, EBI-1538629;
O43765:SGTA; NbExp=3; IntAct=EBI-1034374, EBI-347996;
-!- SUBCELLULAR LOCATION: Transforming growth factor alpha: Secreted,
extracellular space.
-!- SUBCELLULAR LOCATION: Protransforming growth factor alpha: Cell
membrane; Single-pass type I membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P01135-1; Sequence=Displayed;
Name=2;
IsoId=P01135-2; Sequence=VSP_038369;
Name=3; Synonyms=VaII;
IsoId=P01135-3; Sequence=VSP_038369, VSP_038370;
Name=4; Synonyms=VaI;
IsoId=P01135-4; Sequence=VSP_038371;
Name=5; Synonyms=VaIM;
IsoId=P01135-5; Sequence=VSP_038369, VSP_038371;
-!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are
expressed in keratinocytes and tumor-derived cell lines.
{ECO:0000269|PubMed:10523832}.
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EMBL; K03222; AAA61159.1; -; mRNA.
EMBL; M31172; AAA61157.1; -; mRNA.
EMBL; X70340; CAA49806.1; -; mRNA.
EMBL; AF123243; AAF13491.1; -; Genomic_DNA.
EMBL; AF123238; AAF13491.1; JOINED; Genomic_DNA.
EMBL; AF123239; AAF13491.1; JOINED; Genomic_DNA.
EMBL; AF123240; AAF13491.1; JOINED; Genomic_DNA.
EMBL; AF123241; AAF13491.1; JOINED; Genomic_DNA.
EMBL; AF123242; AAF13491.1; JOINED; Genomic_DNA.
EMBL; AY325886; AAP97822.2; -; Genomic_DNA.
EMBL; AY325885; AAP97822.2; JOINED; Genomic_DNA.
EMBL; AY326405; AAP97822.2; JOINED; Genomic_DNA.
EMBL; AY327131; AAP97822.2; JOINED; Genomic_DNA.
EMBL; AY327132; AAP97822.2; JOINED; Genomic_DNA.
EMBL; AY329368; AAP97822.2; JOINED; Genomic_DNA.
EMBL; AF149096; AAF05089.1; -; mRNA.
EMBL; AF149097; AAF05090.1; -; mRNA.
EMBL; AF149098; AAF05091.1; -; mRNA.
EMBL; BT006833; AAP35479.1; -; mRNA.
EMBL; AK290151; BAF82840.1; -; mRNA.
EMBL; AC005234; AAY14793.1; -; Genomic_DNA.
EMBL; AC017084; AAY14705.1; -; Genomic_DNA.
EMBL; CH471053; EAW99810.1; -; Genomic_DNA.
EMBL; CH471053; EAW99812.1; -; Genomic_DNA.
EMBL; BC005308; AAH05308.1; -; mRNA.
EMBL; M22440; AAA52530.1; -; Genomic_DNA.
EMBL; AF075584; AAD12238.1; -; Genomic_DNA.
EMBL; AF075583; AAD12238.1; JOINED; Genomic_DNA.
CCDS; CCDS1905.1; -. [P01135-1]
CCDS; CCDS46316.1; -. [P01135-2]
PIR; JN0876; WFHU1.
RefSeq; NP_001093161.1; NM_001099691.2. [P01135-2]
RefSeq; NP_001295087.1; NM_001308158.1.
RefSeq; NP_001295088.1; NM_001308159.1.
RefSeq; NP_003227.1; NM_003236.3. [P01135-1]
UniGene; Hs.170009; -.
UniGene; Hs.628298; -.
PDB; 1GK5; NMR; -; A=83-89.
PDB; 1MOX; X-ray; 2.50 A; C/D=40-89.
PDB; 1YUF; NMR; -; A=40-89.
PDB; 1YUG; NMR; -; A=40-89.
PDB; 2TGF; NMR; -; A=40-89.
PDB; 3E50; X-ray; 2.30 A; C/D=40-89.
PDB; 3TGF; NMR; -; A=40-89.
PDB; 4TGF; NMR; -; A=40-89.
PDB; 5KN5; X-ray; 2.80 A; C/F=49-88.
PDBsum; 1GK5; -.
PDBsum; 1MOX; -.
PDBsum; 1YUF; -.
PDBsum; 1YUG; -.
PDBsum; 2TGF; -.
PDBsum; 3E50; -.
PDBsum; 3TGF; -.
PDBsum; 4TGF; -.
PDBsum; 5KN5; -.
ProteinModelPortal; P01135; -.
SMR; P01135; -.
BioGrid; 112897; 68.
DIP; DIP-5765N; -.
IntAct; P01135; 9.
MINT; MINT-121235; -.
STRING; 9606.ENSP00000295400; -.
SwissPalm; P01135; -.
BioMuta; TGFA; -.
DMDM; 135689; -.
PaxDb; P01135; -.
PeptideAtlas; P01135; -.
PRIDE; P01135; -.
DNASU; 7039; -.
Ensembl; ENST00000295400; ENSP00000295400; ENSG00000163235. [P01135-1]
Ensembl; ENST00000418333; ENSP00000404099; ENSG00000163235. [P01135-2]
Ensembl; ENST00000445399; ENSP00000387493; ENSG00000163235. [P01135-3]
GeneID; 7039; -.
KEGG; hsa:7039; -.
UCSC; uc002sgs.4; human. [P01135-1]
CTD; 7039; -.
DisGeNET; 7039; -.
EuPathDB; HostDB:ENSG00000163235.15; -.
GeneCards; TGFA; -.
HGNC; HGNC:11765; TGFA.
HPA; HPA042297; -.
MalaCards; TGFA; -.
MIM; 190170; gene.
neXtProt; NX_P01135; -.
OpenTargets; ENSG00000163235; -.
Orphanet; 1991; Cleft lip with or without cleft palate.
Orphanet; 2227; Hypodontia.
Orphanet; 99798; Oligodontia.
PharmGKB; PA36480; -.
eggNOG; ENOG410IVW5; Eukaryota.
eggNOG; ENOG4111Z4I; LUCA.
GeneTree; ENSGT00730000110951; -.
HOGENOM; HOG000013036; -.
HOVERGEN; HBG000330; -.
InParanoid; P01135; -.
KO; K08774; -.
OMA; LIHCCEV; -.
PhylomeDB; P01135; -.
TreeFam; TF332938; -.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLink; P01135; -.
SIGNOR; P01135; -.
ChiTaRS; TGFA; human.
EvolutionaryTrace; P01135; -.
GeneWiki; TGF_alpha; -.
GenomeRNAi; 7039; -.
PMAP-CutDB; P01135; -.
PRO; PR:P01135; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163235; -.
CleanEx; HS_TGFA; -.
ExpressionAtlas; P01135; baseline and differential.
Genevisible; P01135; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB.
GO; GO:0008083; F:growth factor activity; IDA:HGNC.
GO; GO:0000187; P:activation of MAPK activity; IDA:HGNC.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IDA:HGNC.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:HGNC.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:HGNC.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR015497; EGF_rcpt_ligand.
PANTHER; PTHR10740; PTHR10740; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Growth factor;
Lipoprotein; Membrane; Mitogen; Palmitate; Polymorphism;
Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 160 Protransforming growth factor alpha.
/FTId=PRO_0000302744.
PROPEP 24 39 Removed in mature form.
/FTId=PRO_0000007752.
CHAIN 40 89 Transforming growth factor alpha.
/FTId=PRO_0000007753.
PROPEP 90 160 Removed in mature form.
/FTId=PRO_0000007754.
TOPO_DOM 24 98 Extracellular. {ECO:0000255}.
TRANSMEM 99 124 Helical. {ECO:0000255}.
TOPO_DOM 125 160 Cytoplasmic. {ECO:0000255}.
DOMAIN 43 83 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
LIPID 153 153 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8910478}.
LIPID 154 154 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8910478}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 47 60 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:1632509}.
DISULFID 55 71 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:1632509}.
DISULFID 73 82 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:1632509}.
VAR_SEQ 32 32 Missing (in isoform 2, isoform 3 and
isoform 5). {ECO:0000303|PubMed:10523832,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.7}.
/FTId=VSP_038369.
VAR_SEQ 159 160 VV -> ATLG (in isoform 3).
{ECO:0000303|PubMed:10523832}.
/FTId=VSP_038370.
VAR_SEQ 159 160 VV -> GCRLY (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:10523832}.
/FTId=VSP_038371.
VARIANT 109 109 V -> M (in dbSNP:rs11466259).
/FTId=VAR_024271.
CONFLICT 58 58 G -> A (in Ref. 2; AAA61157).
{ECO:0000305}.
CONFLICT 65 65 Q -> H (in Ref. 2; AAA61157).
{ECO:0000305}.
CONFLICT 159 159 V -> L (in Ref. 2; AAA61157).
{ECO:0000305}.
STRAND 43 45 {ECO:0000244|PDB:1MOX}.
HELIX 51 54 {ECO:0000244|PDB:1YUF}.
STRAND 58 63 {ECO:0000244|PDB:1MOX}.
TURN 64 67 {ECO:0000244|PDB:1MOX}.
STRAND 68 73 {ECO:0000244|PDB:1MOX}.
STRAND 77 79 {ECO:0000244|PDB:1MOX}.
STRAND 84 86 {ECO:0000244|PDB:5KN5}.
SEQUENCE 160 AA; 17006 MW; D692184F9353DE47 CRC64;
MVPSAGQLAL FALGIVLAAC QALENSTSPL SADPPVAAAV VSHFNDCPDS HTQFCFHGTC
RFLVQEDKPA CVCHSGYVGA RCEHADLLAV VAASQKKQAI TALVVVSIVA LAVLIITCVL
IHCCQVRKHC EWCRALICRH EKPSALLKGR TACCHSETVV


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