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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.
16-OCT-2019, entry version 119.
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.
PRIDE; P09531; -.
InParanoid; P09531; -.
OrthoDB; 643840at2759; -.
PhylomeDB; P09531; -.
Proteomes; UP000000539; Unplaced.
ExpressionAtlas; P09531; baseline and differential.
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:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0048468; P:cell development; 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:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
GO; GO:0043408; P:regulation of MAPK cascade; 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; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Growth factor; Mitogen;
Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 277 Latency-associated peptide.
{ECO:0000250|UniProtKB:P01137}.
/FTId=PRO_0000033774.
CHAIN 278 391 Transforming growth factor beta-1.
{ECO:0000250|UniProtKB:P01137}.
/FTId=PRO_0000033775.
REGION 19 63 Straightjacket domain.
{ECO:0000250|UniProtKB:P07200}.
REGION 64 270 Arm domain.
{ECO:0000250|UniProtKB:P07200}.
REGION 221 249 Bowtie tail.
{ECO:0000250|UniProtKB:P01137}.
MOTIF 241 243 Cell attachment site. {ECO:0000255}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 22 22 Interchain (with C-? in LTBP1 TB3
domain); in inactive form.
{ECO:0000250|UniProtKB:P07200}.
DISULFID 218 218 Interchain (with C-220).
{ECO:0000250|UniProtKB:P01137}.
DISULFID 220 220 Interchain (with C-218).
{ECO:0000250|UniProtKB:P01137}.
DISULFID 284 295 {ECO:0000250|UniProtKB:P01137}.
DISULFID 294 357 {ECO:0000250|UniProtKB:P01137}.
DISULFID 323 388 {ECO:0000250|UniProtKB:P01137}.
DISULFID 327 390 {ECO:0000250|UniProtKB:P01137}.
DISULFID 356 356 Interchain.
{ECO:0000250|UniProtKB:P01137}.
CONFLICT 110 110 P -> A (in Ref. 2; AAB05637).
CONFLICT 130 138 VRAEVGGRA -> ARRGGRPT (in Ref. 2;
AAB05637).
CONFLICT 228 228 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) (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)
[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)
[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)
[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)]
[TGF beta TGFB1] Transforming growth factor beta

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