ID Q3UNK5_MOUSE Unreviewed; 390 AA.
AC Q3UNK5;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
GN Name=Tgfb1 {ECO:0000313|MGI:MGI:98725};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE25742.1};
RN [1] {ECO:0000313|EMBL:BAE25742.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAE25742.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAE25742.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:BAE25742.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [5] {ECO:0000313|EMBL:BAE25742.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [6] {ECO:0000313|EMBL:BAE25742.1}
RP NUCLEOTIDE SEQUENCE.
RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:BAE25742.1}
RP NUCLEOTIDE SEQUENCE.
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [8] {ECO:0000313|EMBL:BAE25742.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
RN [9] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of
CC the Latency-associated peptide (LAP) and Transforming growth factor
CC beta-1 (TGF-beta-1) chains, which constitute the regulatory and active
CC subunit of TGF-beta-1, respectively. {ECO:0000256|ARBA:ARBA00002007}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|PIRNR:PIRNR001787}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the TGF-beta family.
CC {ECO:0000256|ARBA:ARBA00006656, ECO:0000256|PIRNR:PIRNR001787,
CC ECO:0000256|RuleBase:RU000354}.
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DR EMBL; AK144163; BAE25742.1; -; mRNA.
DR RefSeq; NP_035707.1; NM_011577.2.
DR AlphaFoldDB; Q3UNK5; -.
DR SMR; Q3UNK5; -.
DR SwissPalm; Q3UNK5; -.
DR EPD; Q3UNK5; -.
DR MaxQB; Q3UNK5; -.
DR Antibodypedia; 4372; 1931 antibodies from 44 providers.
DR DNASU; 21803; -.
DR GeneID; 21803; -.
DR KEGG; mmu:21803; -.
DR AGR; MGI:98725; -.
DR CTD; 7040; -.
DR MGI; MGI:98725; Tgfb1.
DR VEuPathDB; HostDB:ENSMUSG00000002603; -.
DR HOGENOM; CLU_039840_0_0_1; -.
DR OMA; FSAHCSC; -.
DR OrthoDB; 5390486at2759; -.
DR PhylomeDB; Q3UNK5; -.
DR BioGRID-ORCS; 21803; 2 hits in 119 CRISPR screens.
DR ExpressionAtlas; Q3UNK5; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0072562; C:blood microparticle; ISS:AgBase.
DR GO; GO:0009986; C:cell surface; ISS:AgBase.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0003823; F:antigen binding; ISS:AgBase.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0006754; P:ATP biosynthetic process; ISS:AgBase.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:AgBase.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:AgBase.
DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0085029; P:extracellular matrix assembly; ISS:AgBase.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:AgBase.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0060364; P:frontal suture morphogenesis; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISS:AgBase.
DR GO; GO:0030214; P:hyaluronan catabolic process; ISS:AgBase.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISS:AgBase.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:AgBase.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:AgBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:AgBase.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:AgBase.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:AgBase.
DR GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; ISS:AgBase.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:AgBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:AgBase.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISS:AgBase.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS:AgBase.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:AgBase.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:AgBase.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:AgBase.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISS:AgBase.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; IEA:Ensembl.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISS:AgBase.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:AgBase.
DR GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; ISS:AgBase.
DR GO; GO:0071677; P:positive regulation of mononuclear cell migration; IEA:Ensembl.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:AgBase.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:AgBase.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:AgBase.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:AgBase.
DR GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:AgBase.
DR GO; GO:0032801; P:receptor catabolic process; ISS:AgBase.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:AgBase.
DR GO; GO:0070723; P:response to cholesterol; ISS:AgBase.
DR GO; GO:0032355; P:response to estradiol; ISS:AgBase.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; ISS:AgBase.
DR GO; GO:1902074; P:response to salt; IEA:Ensembl.
DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; ISS:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR CDD; cd19384; TGF_beta_TGFB1; 1.
DR Gene3D; 2.60.120.970; -; 1.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR016319; TGF-beta.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR003939; TGFb1.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR PANTHER; PTHR11848:SF125; TRANSFORMING GROWTH FACTOR BETA-1 PROPROTEIN; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR PIRSF; PIRSF001787; TGF-beta; 1.
DR PRINTS; PR01423; TGFBETA.
DR PRINTS; PR01424; TGFBETA1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001787-1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW ECO:0000256|PIRNR:PIRNR001787};
KW Mitogen {ECO:0000256|ARBA:ARBA00023246, ECO:0000256|PIRNR:PIRNR001787};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR001787};
KW Signal {ECO:0000256|PIRNR:PIRNR001787}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT CHAIN 30..390
FT /note="Transforming growth factor beta"
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT /id="PRO_5014309152"
FT DOMAIN 275..390
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT COILED 150..177
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 285..294
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 293..356
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 322..387
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 326..389
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 355
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ SEQUENCE 390 AA; 44310 MW; 4381A51B711D689E CRC64;
MPPSGLRLLP LLLPLPWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA
SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESADPEPEPE ADYYAKEVTR VLMVDRNNAI
YEKTKDISHS IYMFFNTSDI REAVPEPPLL SRAELRLQRL KSSVEQHVEL YQKYSNNSWR
YLGNRLLTPT DTPEWLSFDV TGVVRQWLNQ GDGIQGFRFS AHCSCDSKDN KLHVEINGIS
PKRRGDLGTI HDMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SASPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS
//
