ID G1SNK8_RABIT Unreviewed; 442 AA.
AC G1SNK8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
GN Name=TGFB2 {ECO:0000313|Ensembl:ENSOCUP00000004578.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000004578.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000004578.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000004578.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000004578.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004578.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Precursor of the Latency-associated peptide (LAP) and
CC Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute
CC the regulatory and active subunit of TGF-beta-2, respectively.
CC {ECO:0000256|ARBA:ARBA00034081}.
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; AAGW02025670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02025671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SNK8; -.
DR SMR; G1SNK8; -.
DR STRING; 9986.ENSOCUP00000004578; -.
DR PaxDb; 9986-ENSOCUP00000004578; -.
DR Ensembl; ENSOCUT00000005281.4; ENSOCUP00000004578.3; ENSOCUG00000005279.4.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000157390; -.
DR HOGENOM; CLU_039840_0_0_1; -.
DR InParanoid; G1SNK8; -.
DR OMA; FYIDFKR; -.
DR Proteomes; UP000001811; Chromosome 16.
DR Bgee; ENSOCUG00000005279; Expressed in lung and 17 other cell types or tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; ISS:AgBase.
DR GO; GO:0005576; C:extracellular region; ISS:AgBase.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:AgBase.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR GO; GO:0005102; F:signaling receptor binding; ISS:AgBase.
DR GO; GO:0005160; F: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:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:AgBase.
DR GO; GO:0010002; P:cardioblast differentiation; ISS:AgBase.
DR GO; GO:0016477; P:cell migration; ISS:AgBase.
DR GO; GO:0000902; P:cell morphogenesis; ISS:AgBase.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:AgBase.
DR GO; GO:0030199; P:collagen fibril organization; ISS:AgBase.
DR GO; GO:0048566; P:embryonic digestive tract development; ISS:AgBase.
DR GO; GO:0030855; P:epithelial cell differentiation; ISS:AgBase.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:AgBase.
DR GO; GO:0001654; P:eye development; ISS:AgBase.
DR GO; GO:0008347; P:glial cell migration; ISS:AgBase.
DR GO; GO:0001942; P:hair follicle development; ISS:AgBase.
DR GO; GO:0007507; P:heart development; ISS:AgBase.
DR GO; GO:0003007; P:heart morphogenesis; ISS:AgBase.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
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:0050680; P:negative regulation of epithelial cell proliferation; ISS:AgBase.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:AgBase.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:AgBase.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:AgBase.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0045823; P:positive regulation of heart contraction; ISS:AgBase.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISS:AgBase.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:AgBase.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:AgBase.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:AgBase.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:AgBase.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:AgBase.
DR GO; GO:0051795; P:positive regulation of timing of catagen; ISS:AgBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISS:AgBase.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; ISS:AgBase.
DR GO; GO:0009611; P:response to wounding; ISS:AgBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
DR GO; GO:0007165; P:signal transduction; ISS:AgBase.
DR GO; GO:0023052; P:signaling; ISS:AgBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
DR CDD; cd19385; TGF_beta_TGFB2; 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; IPR003940; TGFb2.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR PANTHER; PTHR11848:SF141; TRANSFORMING GROWTH FACTOR BETA-2 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; PR01425; TGFBETA2.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR001787};
KW Signal {ECO:0000256|PIRNR:PIRNR001787}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT CHAIN 21..442
FT /note="Transforming growth factor beta"
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT /id="PRO_5016196531"
FT DOMAIN 327..442
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT DISULFID 337..346
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 345..408
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 374..439
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 378..441
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 407
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ SEQUENCE 442 AA; 50553 MW; AFB0B348E89C293E CRC64;
MHYCVLSAFL ILHLVTVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP
EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPS YFPSETVCPV
VTTPSGSVGS LCARQSQVLC GYLDAIPPTF YRPYFRIVRF DVSTMEKNAS NLVKAEFRVF
RLQNPKARVA EQRIELYQIL KSKDLTSPTQ RYIDSKVVKT RAEGEWLSFD VTDAVHEWLH
HKDRNLGFKI SLHCPCCTFV PSNNYIIPNK SEELEARFAG IDGTSTYTSG DQKTIKSTRK
KNSGKTPHLL LMLLPSYRLE SQQSNRRKKR ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW
KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY
YIGKTPKIEQ LSNMIVKSCK CS
//
