GDF11_RAT
ID GDF11_RAT Reviewed; 405 AA.
AC Q9Z217; G3V6Y2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Growth/differentiation factor 11;
DE Short=GDF-11;
DE AltName: Full=Bone morphogenetic protein 11;
DE Short=BMP-11;
DE Flags: Precursor;
GN Name=Gdf11; Synonyms=Bmp11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-399.
RC TISSUE=Dental pulp;
RX PubMed=10072786; DOI=10.1016/s0925-4773(98)00205-6;
RA Nakashima M., Toyono T., Akamine A., Joyner A.;
RT "Expression of growth/differentiation factor 11, a new member of the
RT BMP/TGFbeta superfamily during mouse embryogenesis.";
RL Mech. Dev. 80:185-189(1999).
CC -!- FUNCTION: Secreted signal that acts globally to regulate
CC anterior/posterior axial patterning during development. May play
CC critical roles in patterning both mesodermal and neural tissues. It is
CC required for proper vertebral patterning and orofacial development.
CC Signals through activin receptors type-2, ACVR2A and ACVR2B, and
CC activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the
CC phosphorylation of SMAD2 and SMAD3. {ECO:0000250|UniProtKB:O95390,
CC ECO:0000250|UniProtKB:Q9Z1W4}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts
CC directly with ACVR2B. Interacts directly with ACVR2A. Interacts with
CC ACVR1B, TGFBR1 and ACVR1C in an ACVR2B-dependent manner (By
CC similarity). Interacts with FST isoform 2/FS288 (By similarity).
CC {ECO:0000250|UniProtKB:O95390, ECO:0000250|UniProtKB:Q9Z1W4}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: Synthesized as large precursor molecule that undergoes proteolytic
CC cleavage by furin-like proteases. This produces an inactive form
CC consisting of the mature C-terminal portion non-covalently bound to its
CC cleaved N-terminal propeptide. Activation of the mature form requires
CC additional cleavage of the propeptide by a tolloid-like
CC metalloproteinase. {ECO:0000250|UniProtKB:Q9Z1W4}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AC141508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474104; EDL84790.1; -; Genomic_DNA.
DR EMBL; AF092733; AAD05266.1; -; mRNA.
DR RefSeq; NP_058899.1; NM_017203.1.
DR AlphaFoldDB; Q9Z217; -.
DR SMR; Q9Z217; -.
DR STRING; 10116.ENSRNOP00000010035; -.
DR GlyGen; Q9Z217; 1 site.
DR PaxDb; Q9Z217; -.
DR Ensembl; ENSRNOT00000010035; ENSRNOP00000010035; ENSRNOG00000007610.
DR GeneID; 29454; -.
DR KEGG; rno:29454; -.
DR UCSC; RGD:2673; rat.
DR CTD; 10220; -.
DR RGD; 2673; Gdf11.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000161052; -.
DR InParanoid; Q9Z217; -.
DR OMA; NSRAGHW; -.
DR OrthoDB; 892873at2759; -.
DR PhylomeDB; Q9Z217; -.
DR TreeFam; TF318514; -.
DR PRO; PR:Q9Z217; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000007610; Expressed in cerebellum and 20 other tissues.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0035881; P:amacrine cell differentiation; IEA:Ensembl.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISO:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0001656; P:metanephros development; ISO:RGD.
DR GO; GO:1902870; P:negative regulation of amacrine cell differentiation; IEA:Ensembl.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0031016; P:pancreas development; ISO:RGD.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0021512; P:spinal cord anterior/posterior patterning; ISO:RGD.
DR GO; GO:0072560; P:type B pancreatic cell maturation; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW Growth factor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..296
FT /evidence="ECO:0000250"
FT /id="PRO_0000033990"
FT CHAIN 297..405
FT /note="Growth/differentiation factor 11"
FT /id="PRO_0000033991"
FT SITE 119..120
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W4"
FT SITE 296
FT /note="Cleavage; by FURIN"
FT /evidence="ECO:0000250|UniProtKB:O95390"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 302..312
FT /evidence="ECO:0000250|UniProtKB:O95390"
FT DISULFID 311..370
FT /evidence="ECO:0000250|UniProtKB:O95390"
FT DISULFID 339..402
FT /evidence="ECO:0000250|UniProtKB:O95390"
FT DISULFID 343..404
FT /evidence="ECO:0000250|UniProtKB:O95390"
FT DISULFID 369
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:O95390"
FT CONFLICT 71..75
FT /note="ELRLE -> RVRGL (in Ref. 3; AAD05266)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="L -> C (in Ref. 3; AAD05266)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="F -> S (in Ref. 3; AAD05266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 44921 MW; 47B467845D9C7350 CRC64;
MVLAAPLLLG FLLLALELRP RGEAAEGPAA AAAAAAAAAG VGGERSSRPA PSAAPEPDGC
PVCVWRQHSR ELRLESIKSQ ILSKLRLKEA PNISREVVKQ LLPKAPPLQQ ILDLHDFQGD
ALQPEDFLEE DEYHATTETV ISMAQETDPA VQTDGSPLCC HFHFSPKVMF TKVLKAQLWV
YLRPVPRPAT VYLQILRLKP LTGEGTAGGG GGGRRHIRIR SLKIELHSRS GHWQSIDFKQ
VLHSWFRQPQ SNWGIEINAF DPSGTDLAVT SLGPGAEGLH PFMELRVLEN TKRSRRNLGL
DCDEHSSESR CCRYPLTVDF EAFGWDWIIA PKRYKANYCS GQCEYMFMQK YPHTHLVQQA
NPRGSAGPCC TPTKMSPINM LYFNDKQQII YGKIPGMVVD RCGCS
