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Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]

 TGFB1_CHICK             Reviewed;         391 AA.
P09531; A0A1D5PM67;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
10-OCT-2018, sequence version 3.
26-FEB-2020, entry version 121.
RecName: Full=Transforming growth factor beta-1 proprotein;
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-1;
Short=TGF-beta-1;
Flags: Precursor;
Name=TGFB1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl;
PubMed=15592404; DOI=10.1038/nature03154;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide unique
perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-391.
STRAIN=White leghorn;
PubMed=2464131; DOI=10.1210/mend-2-12-1186;
Jakowlew S.B., Dillard P.J., Sporn M.B., Roberts A.B.;
"Complementary deoxyribonucleic acid cloning of a messenger ribonucleic
acid encoding transforming growth factor beta 4 from chicken embryo
chondrocytes.";
Mol. Endocrinol. 2:1186-1195(1988).
[3]
SEQUENCE REVISION.
PubMed=1353860; DOI=10.1210/mend.6.6.1353860;
Burt D.W., Jakowlew S.B.;
"Correction: a new interpretation of a chicken transforming growth factor-
beta 4 complementary DNA.";
Mol. Endocrinol. 6:989-992(1992).
-!- FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of
the Latency-associated peptide (LAP) and Transforming growth factor
beta-1 (TGF-beta-1) chains, which constitute the regulatory and active
subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.
-!- FUNCTION: [Latency-associated peptide]: Required to maintain the
Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state
during storage in extracellular matrix. Associates non-covalently with
TGF-beta-1 and regulates its activation via interaction with 'milieu
molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control
activation of TGF-beta-1. Interaction with integrins (ITGAV:ITGB6 or
ITGAV:ITGB8) results in distortion of the Latency-associated peptide
chain and subsequent release of the active TGF-beta-1.
{ECO:0000250|UniProtKB:P01137}.
-!- FUNCTION: Transforming growth factor beta-1: Multifunctional protein
that regulates the growth and differentiation of various cell types and
is involved in various processes, such as normal development, immune
function, microglia function and responses to neurodegeneration (By
similarity). Activation into mature form follows different steps:
following cleavage of the proprotein in the Golgi apparatus, Latency-
associated peptide (LAP) and Transforming growth factor beta-1 (TGF-
beta-1) chains remain non-covalently linked rendering TGF-beta-1
inactive during storage in extracellular matrix. At the same time, LAP
chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and
LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a
latent state during storage in extracellular milieus. TGF-beta-1 is
released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-
binding to LAP stabilizes an alternative conformation of the LAP bowtie
tail and results in distortion of the LAP chain and subsequent release
of the active TGF-beta-1. Once activated following release of LAP, TGF-
beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which
transduce signal (By similarity). While expressed by many cells types,
TGF-beta-1 only has a very localized range of action within cell
environment thanks to fine regulation of its activation by Latency-
associated peptide chain (LAP) and 'milieu molecules'. Plays an
important role in bone remodeling: acts as a potent stimulator of
osteoblastic bone formation. Can promote either T-helper 17 cells
(Th17) or regulatory T-cells (Treg) lineage differentiation in a
concentration-dependent manner (By similarity). Can induce epithelial-
to-mesenchymal transition (EMT) and cell migration in various cell
types (By similarity). {ECO:0000250|UniProtKB:P01137,
ECO:0000250|UniProtKB:P04202}.
-!- SUBUNIT: Latency-associated peptide: Homodimer; disulfide-linked.
Latency-associated peptide: Interacts with Transforming growth factor
beta-1 (TGF-beta-1) chain; interaction is non-covalent and maintains
(TGF-beta-1) in a latent state; each Latency-associated peptide (LAP)
monomer interacts with TGF-beta-1 in the other monomer. Transforming
growth factor beta-1: Homodimer; disulfide-linked. Transforming growth
factor beta-1: Interacts with TGF-beta receptors (TGFBR1 and TGFBR2),
leading to signal transduction. {ECO:0000250|UniProtKB:P01137}.
-!- SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted,
extracellular space, extracellular matrix
{ECO:0000250|UniProtKB:P01137}.
-!- SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted
{ECO:0000250|UniProtKB:P01137}.
-!- DOMAIN: [Latency-associated peptide]: The 'straitjacket' and 'arm'
domains encircle the Transforming growth factor beta-1 (TGF-beta-1)
monomers and are fastened together by strong bonding between Lys-45 and
Tyr-93/Trp-94. {ECO:0000250|UniProtKB:P07200}.
-!- DOMAIN: [Latency-associated peptide]: The cell attachment site motif
mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8). The motif
locates to a long loop in the arm domain called the bowtie tail.
Integrin-binding stabilizes an alternative conformation of the bowtie
tail. Activation by integrin requires force application by the actin
cytoskeleton, which is resisted by the 'milieu molecules' (such as
LTBP1, LRRC32/GARP and/or LRRC33/NRROS), resulting in distortion of the
prodomain and release of the active TGF-beta-1.
{ECO:0000250|UniProtKB:P01137}.
-!- PTM: Transforming growth factor beta-1 proprotein: The precursor
proprotein is cleaved in the Golgi apparatus to form Transforming
growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP)
chains, which remain non-covalently linked, rendering TGF-beta-1
inactive. {ECO:0000250|UniProtKB:P01137}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; M31160; AAB05637.1; -; mRNA.
PIR; A41918; A41918.
SMR; P09531; -.
PRIDE; P09531; -.
InParanoid; P09531; -.
OrthoDB; 643840at2759; -.
PhylomeDB; P09531; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IEP:AgBase.
GO; GO:0033686; P:positive regulation of luteinizing hormone secretion; IEP:AgBase.
GO; GO:0014008; P:positive regulation of microglia differentiation; ISS:UniProtKB.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
GO; GO:0042327; P:positive regulation of phosphorylation; IEP:AgBase.
GO; GO:0042701; P:progesterone secretion; IEP:AgBase.
GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
GO; GO:0050708; P:regulation of protein secretion; IEP:AgBase.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR016319; TGF-beta.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR003939; TGFb1.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PIRSF; PIRSF001787; TGF-beta; 1.
PRINTS; PR01423; TGFBETA.
PRINTS; PR01424; TGFBETA1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Disulfide bond; Extracellular matrix;
Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted; Signal.
SIGNAL 1..18
/evidence="ECO:0000255"
CHAIN 19..277
/note="Latency-associated peptide"
/evidence="ECO:0000250|UniProtKB:P01137"
/id="PRO_0000033774"
CHAIN 278..391
/note="Transforming growth factor beta-1"
/evidence="ECO:0000250|UniProtKB:P01137"
/id="PRO_0000033775"
REGION 19..63
/note="Straightjacket domain"
/evidence="ECO:0000250|UniProtKB:P07200"
REGION 64..270
/note="Arm domain"
/evidence="ECO:0000250|UniProtKB:P07200"
REGION 221..249
/note="Bowtie tail"
/evidence="ECO:0000250|UniProtKB:P01137"
MOTIF 241..243
/note="Cell attachment site"
/evidence="ECO:0000255"
CARBOHYD 71
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 126
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 171
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 22
/note="Interchain (with C-? in LTBP1 TB3 domain); in
inactive form"
/evidence="ECO:0000250|UniProtKB:P07200"
DISULFID 218
/note="Interchain (with C-220)"
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 220
/note="Interchain (with C-218)"
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 284..295
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 294..357
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 323..388
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 327..390
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 356
/note="Interchain"
/evidence="ECO:0000250|UniProtKB:P01137"
CONFLICT 110
/note="P -> A (in Ref. 2; AAB05637)"
CONFLICT 130..138
/note="VRAEVGGRA -> ARRGGRPT (in Ref. 2; AAB05637)"
CONFLICT 228
/note="D -> E (in Ref. 2; AAB05637)"
SEQUENCE 391 AA; 44437 MW; FB34D6A4BC4B0B93 CRC64;
MDPSPLLALL LLLGAARALS TCQRLDLEAA KKKRIEAVRG QILSKLRLTA PPPASETPPR
PLPDDVRALY NSTQELLKQR ARLRPPPDGP DEYWAKELRR IPMETTWDGP MEHWQPQSHS
IFFVFNVSRV RAEVGGRALL HRAELRMLRQ KAAADSAGTE QRLELYQGYG NASWRYLHGR
SVRATADDEW LSFDVTDAVH QWLSGSELLG VFKLSVHCPC EMGPGHADEM RISIEGFEQQ
RGDMQSIAKK HRRVPYVLAM ALPAERANEL HSARRRRDLD TDYCFGPGTD EKNCCVRPLY
IDFRKDLQWK WIHEPKGYMA NFCMGPCPYI WSADTQYTKV LALYNQHNPG ASAAPCCVPQ
TLDPLPIIYY VGRNVRVEQL SNMVVRACKC S


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Related Genes :
[TGFB1 TGFB] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
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[TGFB3] Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)]
[TGFB2] Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFBR1 ALK5 SKR4] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr3] Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Lefty1 Ebaf Lefty Stra3 Tgfb4] Left-right determination factor 1 (Protein lefty-1) (Lefty protein) (Stimulated by retinoic acid gene 3 protein) (Transforming growth factor beta-4) (TGF-beta-4)
[TGFBR2] TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[LEFTY2 EBAF LEFTA LEFTYA TGFB4 PSEC0024] Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4)
[Nrros Lrrc33] Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species)
[LTBP4] Latent-transforming growth factor beta-binding protein 4 (LTBP-4)
[tgfb1] Transforming growth factor beta-1 proprotein (TGF-beta-5) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]

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