ID   A2AII0_MOUSE            Unreviewed;       454 AA.
AC   A2AII0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 142.
DE   RecName: Full=Growth/differentiation factor 6 {ECO:0000256|ARBA:ARBA00072965};
DE   AltName: Full=Bone morphogenetic protein 13 {ECO:0000256|ARBA:ARBA00083549};
DE   AltName: Full=Growth/differentiation factor 16 {ECO:0000256|ARBA:ARBA00081757};
GN   Name=Gdf6 {ECO:0000313|EMBL:AAI41341.1, ECO:0000313|MGI:MGI:95689};
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:AAI41341.1};
RN   [1] {ECO:0000313|EMBL:AAI41341.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI41341.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family.
CC       {ECO:0000256|ARBA:ARBA00006656, ECO:0000256|RuleBase:RU000354}.
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DR   EMBL; BC141339; AAI41340.1; -; mRNA.
DR   EMBL; BC141340; AAI41341.1; -; mRNA.
DR   RefSeq; NP_038554.1; NM_013526.1.
DR   AlphaFoldDB; A2AII0; -.
DR   SMR; A2AII0; -.
DR   Antibodypedia; 25942; 167 antibodies from 31 providers.
DR   DNASU; 242316; -.
DR   GeneID; 242316; -.
DR   KEGG; mmu:242316; -.
DR   AGR; MGI:95689; -.
DR   CTD; 392255; -.
DR   MGI; MGI:95689; Gdf6.
DR   VEuPathDB; HostDB:ENSMUSG00000051279; -.
DR   HOGENOM; CLU_020515_0_0_1; -.
DR   OMA; KKSKYRC; -.
DR   OrthoDB; 5987191at2759; -.
DR   BioGRID-ORCS; 242316; 1 hit in 76 CRISPR screens.
DR   ExpressionAtlas; A2AII0; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR   GO; GO:0032924; P:activin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0001656; P:metanephros development; IEA:UniProtKB-ARBA.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
DR   CDD; cd13766; TGF_beta_GDF5_6_7; 1.
DR   FunFam; 2.10.90.10:FF:000001; Bone morphogenetic protein 4; 1.
DR   FunFam; 2.60.120.970:FF:000026; Growth differentiation factor 6; 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; IPR015615; TGF-beta-like.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848:SF43; GROWTH_DIFFERENTIATION FACTOR 6; 1.
DR   PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 1.
DR   PRINTS; PR00669; INHIBINA.
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   2: Evidence at transcript level;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Cytokine {ECO:0000256|ARBA:ARBA00022514};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW   ECO:0000256|RuleBase:RU000354}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..454
FT                   /note="Growth/differentiation factor 6"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014296795"
FT   DOMAIN          331..454
FT                   /note="TGF-beta family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51362"
FT   REGION          28..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..92
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..319
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..350
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  50942 MW;  5A3FADDA539CCB38 CRC64;
     MDTPRVLLWA IFLISFLWDL PGFQQASISS SSSSSTELDS TKDVGNRKEG KMQRTPQESA
     EGRTPPEHGL RQKDLRRRPP GQHQGQEPPG RGLRVVPHEY MLSIYKTYSI AEKLGINASF
     FQSSKSANTI TSFVDRGLDD LSHTPLRRQK YLFDVSTLSD KEELVGAELR LYRQAPPTPW
     GLPARPLHLQ LFPCLSPLLL DARTLDPQGP TQAGWEVFDV WQGLRPQPWK QLCLELRAAW
     GELDAGDTGA RARGPQQPPP LDLRSLGFGR RVRPPQERAL LVVFTRSQRK NLFTEMHEQL
     GSAEAAGAEG SWPAPSGSPD AGSWLPSPGR RRRRTAFASR HGKRHGKKSR LRCSRKPLHV
     NFKELGWDDW IIAPLEYEAY HCEGVCDFPL RSHLEPTNHA IIQTLMNSMD PGSTPPSCCV
     PTKLTPISIL YIDAGNNVVY KQYEDMVVES CGCR
//