GenomeNet

Database: UniProt
Entry: P01135
LinkDB: P01135
Original site: P01135 
ID   TGFA_HUMAN              Reviewed;         160 AA.
AC   P01135; A8K286; Q15577; Q53SK7; Q9BS56; Q9UEI3; Q9UKM1; Q9UKM2;
AC   Q9UKM3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   13-FEB-2019, entry version 198.
DE   RecName: Full=Protransforming growth factor alpha;
DE   Contains:
DE     RecName: Full=Transforming growth factor alpha;
DE              Short=TGF-alpha;
DE     AltName: Full=EGF-like TGF;
DE              Short=ETGF;
DE     AltName: Full=TGF type 1;
DE   Flags: Precursor;
GN   Name=TGFA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=6088071; DOI=10.1016/0092-8674(84)90550-6;
RA   Derynck R., Roberts A.B., Winkler M.E., Chen E.Y., Goeddel D.V.;
RT   "Human transforming growth factor-alpha: precursor structure and
RT   expression in E. coli.";
RL   Cell 38:287-297(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2464748; DOI=10.1210/mend-2-11-1056;
RA   Jakowlew S.B., Kondaiah P., Dillard P.J., Sporn M.B., Roberts A.B.;
RT   "A novel low molecular weight ribonucleic acid (RNA) related to
RT   transforming growth factor alpha messenger RNA.";
RL   Mol. Endocrinol. 2:1056-1063(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=8224876; DOI=10.1016/0378-1119(93)90210-T;
RA   Qian J.F., Lazar-Wesley E., Breugnot C., May E.;
RT   "Human transforming growth factor alpha: sequence analysis of the 4.5-
RT   kb and 1.6-kb mRNA species.";
RL   Gene 132:291-296(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8100397;
RA   Qian J.F., Feingold J., Stoll C., May E.;
RT   "Transforming growth factor-alpha: characterization of the BamHI,
RT   RsaI, and TaqI polymorphic regions.";
RL   Am. J. Hum. Genet. 53:168-175(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10552925; DOI=10.1006/geno.1999.5962;
RA   Machida J., Yoshiura K., Funkhauser C.D., Natsume N., Kawai T.,
RA   Murray J.C.;
RT   "Transforming growth factor-alpha (TGFA): genomic structure, boundary
RT   sequences, and mutation analysis in nonsyndromic cleft lip/palate and
RT   cleft palate only.";
RL   Genomics 61:237-242(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10523832; DOI=10.1038/sj.onc.1203091;
RA   Xu X., Liao J., Creek K.E., Pirisi L.;
RT   "Human keratinocytes and tumor-derived cell lines express
RT   alternatively spliced forms of transforming growth factor-alpha mRNA,
RT   encoding precursors lacking carboxyl-terminal valine residues.";
RL   Oncogene 18:5554-5562(1999).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) System Donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RX   PubMed=2907605; DOI=10.1128/MCB.8.12.5549;
RA   Jakobovits E.B., Schlokat U., Vannice J.L., Derynck R., Levinson A.D.;
RT   "The human transforming growth factor alpha promoter directs
RT   transcription initiation from a single site in the absence of a TATA
RT   sequence.";
RL   Mol. Cell. Biol. 8:5549-5554(1988).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX   PubMed=10066034; DOI=10.1034/j.1399-0004.1999.550111.x;
RA   Collin G.B., Marshall J.D., Naggert J.K., Nishina P.M.;
RT   "TGFA: exon-intron structure and evaluation as a candidate gene for
RT   Alstrom syndrome.";
RL   Clin. Genet. 55:61-62(1999).
RN   [14]
RP   DISULFIDE BONDS.
RX   PubMed=1632509; DOI=10.1016/0003-2697(92)90331-Z;
RA   Bean M.F., Carr S.A.;
RT   "Characterization of disulfide bond position in proteins and sequence
RT   analysis of cystine-bridged peptides by tandem mass spectrometry.";
RL   Anal. Biochem. 201:216-226(1992).
RN   [15]
RP   PALMITOYLATION AT CYS-153 AND CYS-154.
RX   PubMed=8910478; DOI=10.1074/jbc.271.45.28502;
RA   Shum L., Turck C.W., Derynck R.;
RT   "Cysteines 153 and 154 of transmembrane transforming growth factor-
RT   alpha are palmitoylated and mediate cytoplasmic protein association.";
RL   J. Biol. Chem. 271:28502-28508(1996).
RN   [16]
RP   INTERACTION WITH SNTA1 AND SDCBP.
RX   PubMed=10230395; DOI=10.1016/S1097-2765(00)80470-0;
RA   Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J.,
RA   Arribas J.;
RT   "A role for a PDZ protein in the early secretory pathway for the
RT   targeting of proTGF-alpha to the cell surface.";
RL   Mol. Cell 3:423-433(1999).
RN   [17]
RP   INTERACTION WITH CNIH AND GORASP2.
RX   PubMed=17607000; DOI=10.1242/jcs.004200;
RA   Perez Castro C., Piscopo D., Nakagawa T., Derynck R.;
RT   "Cornichon regulates transport and secretion of TGFalpha-related
RT   proteins in metazoan cells.";
RL   J. Cell Sci. 120:2454-2466(2007).
RN   [18]
RP   INTERACTION WITH NKD2.
RX   PubMed=18757723; DOI=10.1073/pnas.0806298105;
RA   Ding W., Li C., Hu T., Graves-Deal R., Fotia A.B., Weissman A.M.,
RA   Coffey R.J.;
RT   "EGF receptor-independent action of TGF-alpha protects Naked2 from
RT   AO7-mediated ubiquitylation and proteasomal degradation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:13433-13438(2008).
RN   [19]
RP   STRUCTURE BY NMR OF TGF-ALPHA.
RX   PubMed=2261437; DOI=10.1021/bi00486a005;
RA   Kline T.P., Brown F.K., Brown S.C., Jeffs P.W., Kopple K.D.,
RA   Mueller L.;
RT   "Solution structures of human transforming growth factor alpha derived
RT   from 1H NMR data.";
RL   Biochemistry 29:7805-7813(1990).
RN   [20]
RP   STRUCTURE BY NMR OF TGF-ALPHA.
RX   PubMed=2050136; DOI=10.1111/j.1432-1033.1991.tb16050.x;
RA   Harvey T.S., Wilkinson A.J., Tappin M.J., Cooke R.M., Campbell I.D.;
RT   "The solution structure of human transforming growth factor alpha.";
RL   Eur. J. Biochem. 198:555-562(1991).
RN   [21]
RP   STRUCTURE BY NMR OF TGF-ALPHA.
RX   PubMed=8338831; DOI=10.1021/bi00080a003;
RA   Moy F.J., Li Y.C., Rauenbuehler P., Winkler M.E., Scheraga H.A.,
RA   Montelione G.T.;
RT   "Solution structure of human type-alpha transforming growth factor
RT   determined by heteronuclear NMR spectroscopy and refined by energy
RT   minimization with restraints.";
RL   Biochemistry 32:7334-7353(1993).
CC   -!- FUNCTION: TGF alpha is a mitogenic polypeptide that is able to
CC       bind to the EGF receptor/EGFR and to act synergistically with TGF
CC       beta to promote anchorage-independent cell proliferation in soft
CC       agar.
CC   -!- SUBUNIT: Interacts with the PDZ domains of MAGI3, SDCBP and SNTA1.
CC       The interaction with SDCBP, is required for the targeting to the
CC       cell surface. In the endoplasmic reticulum, in its immature form
CC       (i.e. with a prosegment and lacking full N-glycosylation),
CC       interacts with CNIH. In the Golgi apparatus, may form a complex
CC       with CNIH and GORASP2. Interacts (via cytoplasmic C-terminal
CC       domain) with NKD2. {ECO:0000269|PubMed:10230395,
CC       ECO:0000269|PubMed:17607000, ECO:0000269|PubMed:18757723}.
CC   -!- INTERACTION:
CC       P00533:EGFR; NbExp=2; IntAct=EBI-1034374, EBI-297353;
CC       Q9EQJ9:Magi3 (xeno); NbExp=4; IntAct=EBI-1034374, EBI-7455245;
CC       Q969F2:NKD2; NbExp=3; IntAct=EBI-1034374, EBI-1538629;
CC       O43765:SGTA; NbExp=4; IntAct=EBI-12367411, EBI-347996;
CC   -!- SUBCELLULAR LOCATION: Transforming growth factor alpha: Secreted,
CC       extracellular space.
CC   -!- SUBCELLULAR LOCATION: Protransforming growth factor alpha: Cell
CC       membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=P01135-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P01135-2; Sequence=VSP_038369;
CC       Name=3; Synonyms=VaII;
CC         IsoId=P01135-3; Sequence=VSP_038369, VSP_038370;
CC       Name=4; Synonyms=VaI;
CC         IsoId=P01135-4; Sequence=VSP_038371;
CC       Name=5; Synonyms=VaIM;
CC         IsoId=P01135-5; Sequence=VSP_038369, VSP_038371;
CC   -!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are
CC       expressed in keratinocytes and tumor-derived cell lines.
CC       {ECO:0000269|PubMed:10523832}.
DR   EMBL; K03222; AAA61159.1; -; mRNA.
DR   EMBL; M31172; AAA61157.1; -; mRNA.
DR   EMBL; X70340; CAA49806.1; -; mRNA.
DR   EMBL; AF123243; AAF13491.1; -; Genomic_DNA.
DR   EMBL; AF123238; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AF123239; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AF123240; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AF123241; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AF123242; AAF13491.1; JOINED; Genomic_DNA.
DR   EMBL; AY325886; AAP97822.2; -; Genomic_DNA.
DR   EMBL; AY325885; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AY326405; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AY327131; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AY327132; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AY329368; AAP97822.2; JOINED; Genomic_DNA.
DR   EMBL; AF149096; AAF05089.1; -; mRNA.
DR   EMBL; AF149097; AAF05090.1; -; mRNA.
DR   EMBL; AF149098; AAF05091.1; -; mRNA.
DR   EMBL; BT006833; AAP35479.1; -; mRNA.
DR   EMBL; AK290151; BAF82840.1; -; mRNA.
DR   EMBL; AC005234; AAY14793.1; -; Genomic_DNA.
DR   EMBL; AC017084; AAY14705.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99810.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99812.1; -; Genomic_DNA.
DR   EMBL; BC005308; AAH05308.1; -; mRNA.
DR   EMBL; M22440; AAA52530.1; -; Genomic_DNA.
DR   EMBL; AF075584; AAD12238.1; -; Genomic_DNA.
DR   EMBL; AF075583; AAD12238.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS1905.1; -. [P01135-1]
DR   CCDS; CCDS46316.1; -. [P01135-2]
DR   PIR; JN0876; WFHU1.
DR   RefSeq; NP_001093161.1; NM_001099691.2. [P01135-2]
DR   RefSeq; NP_001295087.1; NM_001308158.1.
DR   RefSeq; NP_001295088.1; NM_001308159.1.
DR   RefSeq; NP_003227.1; NM_003236.3. [P01135-1]
DR   UniGene; Hs.170009; -.
DR   UniGene; Hs.628298; -.
DR   PDB; 1GK5; NMR; -; A=83-89.
DR   PDB; 1MOX; X-ray; 2.50 A; C/D=40-89.
DR   PDB; 1YUF; NMR; -; A=40-89.
DR   PDB; 1YUG; NMR; -; A=40-89.
DR   PDB; 2TGF; NMR; -; A=40-89.
DR   PDB; 3E50; X-ray; 2.30 A; C/D=40-89.
DR   PDB; 3TGF; NMR; -; A=40-89.
DR   PDB; 4TGF; NMR; -; A=40-89.
DR   PDB; 5KN5; X-ray; 2.80 A; C/F=49-88.
DR   PDBsum; 1GK5; -.
DR   PDBsum; 1MOX; -.
DR   PDBsum; 1YUF; -.
DR   PDBsum; 1YUG; -.
DR   PDBsum; 2TGF; -.
DR   PDBsum; 3E50; -.
DR   PDBsum; 3TGF; -.
DR   PDBsum; 4TGF; -.
DR   PDBsum; 5KN5; -.
DR   ProteinModelPortal; P01135; -.
DR   SMR; P01135; -.
DR   BioGrid; 112897; 68.
DR   DIP; DIP-5765N; -.
DR   IntAct; P01135; 10.
DR   MINT; P01135; -.
DR   STRING; 9606.ENSP00000295400; -.
DR   SwissPalm; P01135; -.
DR   BioMuta; TGFA; -.
DR   DMDM; 135689; -.
DR   jPOST; P01135; -.
DR   PaxDb; P01135; -.
DR   PeptideAtlas; P01135; -.
DR   PRIDE; P01135; -.
DR   ProteomicsDB; 51332; -.
DR   ProteomicsDB; 51333; -. [P01135-2]
DR   ProteomicsDB; 51334; -. [P01135-3]
DR   ProteomicsDB; 51335; -. [P01135-4]
DR   ProteomicsDB; 51336; -. [P01135-5]
DR   DNASU; 7039; -.
DR   Ensembl; ENST00000295400; ENSP00000295400; ENSG00000163235. [P01135-1]
DR   Ensembl; ENST00000418333; ENSP00000404099; ENSG00000163235. [P01135-2]
DR   Ensembl; ENST00000445399; ENSP00000387493; ENSG00000163235. [P01135-3]
DR   GeneID; 7039; -.
DR   KEGG; hsa:7039; -.
DR   UCSC; uc002sgs.4; human. [P01135-1]
DR   CTD; 7039; -.
DR   DisGeNET; 7039; -.
DR   EuPathDB; HostDB:ENSG00000163235.15; -.
DR   GeneCards; TGFA; -.
DR   HGNC; HGNC:11765; TGFA.
DR   HPA; HPA042297; -.
DR   MalaCards; TGFA; -.
DR   MIM; 190170; gene.
DR   neXtProt; NX_P01135; -.
DR   OpenTargets; ENSG00000163235; -.
DR   Orphanet; 2227; NON RARE IN EUROPE: Hypodontia.
DR   Orphanet; 99798; Oligodontia.
DR   PharmGKB; PA36480; -.
DR   eggNOG; ENOG410IVW5; Eukaryota.
DR   eggNOG; ENOG4111Z4I; LUCA.
DR   GeneTree; ENSGT00940000160058; -.
DR   HOGENOM; HOG000013036; -.
DR   HOVERGEN; HBG000330; -.
DR   InParanoid; P01135; -.
DR   KO; K08774; -.
DR   OMA; CQALICR; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P01135; -.
DR   TreeFam; TF332938; -.
DR   Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-HSA-177929; Signaling by EGFR.
DR   Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
DR   Reactome; R-HSA-180292; GAB1 signalosome.
DR   Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR   Reactome; R-HSA-182971; EGFR downregulation.
DR   Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR   Reactome; R-HSA-212718; EGFR interacts with phospholipase C-gamma.
DR   Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR   Reactome; R-HSA-5638303; Inhibition of Signaling by Overexpressed EGFR.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   SignaLink; P01135; -.
DR   SIGNOR; P01135; -.
DR   ChiTaRS; TGFA; human.
DR   EvolutionaryTrace; P01135; -.
DR   GeneWiki; TGF_alpha; -.
DR   GenomeRNAi; 7039; -.
DR   PMAP-CutDB; P01135; -.
DR   PRO; PR:P01135; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000163235; Expressed in 192 organ(s), highest expression level in pigmented layer of retina.
DR   ExpressionAtlas; P01135; baseline and differential.
DR   Genevisible; P01135; HS.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IDA:HGNC.
DR   GO; GO:0000187; P:activation of MAPK activity; IDA:HGNC.
DR   GO; GO:0008283; P:cell population proliferation; TAS:ProtInc.
DR   GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IDA:HGNC.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:HGNC.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:HGNC.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:Reactome.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR015497; EGF_rcpt_ligand.
DR   PANTHER; PTHR10740; PTHR10740; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Growth factor;
KW   Lipoprotein; Membrane; Mitogen; Palmitate; Polymorphism;
KW   Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    160       Protransforming growth factor alpha.
FT                                /FTId=PRO_0000302744.
FT   PROPEP       24     39       Removed in mature form.
FT                                /FTId=PRO_0000007752.
FT   CHAIN        40     89       Transforming growth factor alpha.
FT                                /FTId=PRO_0000007753.
FT   PROPEP       90    160       Removed in mature form.
FT                                /FTId=PRO_0000007754.
FT   TOPO_DOM     24     98       Extracellular. {ECO:0000255}.
FT   TRANSMEM     99    124       Helical. {ECO:0000255}.
FT   TOPO_DOM    125    160       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       43     83       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   LIPID       153    153       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:8910478}.
FT   LIPID       154    154       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:8910478}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     47     60       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:1632509}.
FT   DISULFID     55     71       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:1632509}.
FT   DISULFID     73     82       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:1632509}.
FT   VAR_SEQ      32     32       Missing (in isoform 2, isoform 3 and
FT                                isoform 5). {ECO:0000303|PubMed:10523832,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.7}.
FT                                /FTId=VSP_038369.
FT   VAR_SEQ     159    160       VV -> ATLG (in isoform 3).
FT                                {ECO:0000303|PubMed:10523832}.
FT                                /FTId=VSP_038370.
FT   VAR_SEQ     159    160       VV -> GCRLY (in isoform 4 and isoform 5).
FT                                {ECO:0000303|PubMed:10523832}.
FT                                /FTId=VSP_038371.
FT   VARIANT     109    109       V -> M (in dbSNP:rs11466259).
FT                                /FTId=VAR_024271.
FT   CONFLICT     58     58       G -> A (in Ref. 2; AAA61157).
FT                                {ECO:0000305}.
FT   CONFLICT     65     65       Q -> H (in Ref. 2; AAA61157).
FT                                {ECO:0000305}.
FT   CONFLICT    159    159       V -> L (in Ref. 2; AAA61157).
FT                                {ECO:0000305}.
FT   STRAND       43     45       {ECO:0000244|PDB:1MOX}.
FT   HELIX        51     54       {ECO:0000244|PDB:1YUF}.
FT   STRAND       58     63       {ECO:0000244|PDB:1MOX}.
FT   TURN         64     67       {ECO:0000244|PDB:1MOX}.
FT   STRAND       68     73       {ECO:0000244|PDB:1MOX}.
FT   STRAND       77     79       {ECO:0000244|PDB:1MOX}.
FT   STRAND       84     86       {ECO:0000244|PDB:5KN5}.
SQ   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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