GDF6_BOVIN
ID GDF6_BOVIN Reviewed; 470 AA.
AC P55106; F1MD30;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Growth/differentiation factor 6;
DE Short=GDF-6;
DE AltName: Full=Bone morphogenetic protein 13;
DE Short=BMP-13;
DE AltName: Full=Cartilage-derived morphogenetic protein 2;
DE Short=CDMP-2;
DE Flags: Precursor;
GN Name=GDF6; Synonyms=BMP13, CDMP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-470.
RC TISSUE=Articular cartilage;
RX PubMed=7961761; DOI=10.1016/s0021-9258(18)46918-9;
RA Chang S., Hoang B., Thomas J.T., Vukicevic S., Luyten F.P., Ryba N.J.P.,
RA Kozak C.A., Reddi A.H., Moos M.;
RT "Cartilage-derived morphogenetic proteins. New members of the transforming
RT growth factor-beta superfamily predominantly expressed in long bones during
RT human embryonic development.";
RL J. Biol. Chem. 269:28227-28234(1994).
CC -!- FUNCTION: Growth factor that controls proliferation and cellular
CC differentiation in the retina and bone formation. Plays a key role in
CC regulating apoptosis during retinal development. Establishes dorsal-
CC ventral positional information in the retina and controls the formation
CC of the retinotectal map. Required for normal formation of bones and
CC joints in the limbs, skull, digits and axial skeleton. Plays a key role
CC in establishing boundaries between skeletal elements during
CC development. Regulation of GDF6 expression seems to be a mechanism for
CC evolving species-specific changes in skeletal structures. Seems to
CC positively regulate differentiation of chondrogenic tissue through the
CC growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A,
CC leading to the activation of SMAD1-SMAD5-SMAD8 complex. The regulation
CC of chondrogenic differentiation is inhibited by NOG. Also involved in
CC the induction of adipogenesis from mesenchymal stem cells. This
CC mechanism acts through the growth factor receptors subunits BMPR1A,
CC BMPR2 and ACVR2A and the activation of SMAD1-SMAD5-SMAD8 complex and
CC MAPK14/p38. {ECO:0000250|UniProtKB:P43028,
CC ECO:0000250|UniProtKB:Q6KF10}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P39905}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6KF10}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61416.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; DAAA02039445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U13661; AAA61416.1; ALT_SEQ; mRNA.
DR PIR; B55452; B55452.
DR AlphaFoldDB; P55106; -.
DR SMR; P55106; -.
DR STRING; 9913.ENSBTAP00000043329; -.
DR PaxDb; P55106; -.
DR PRIDE; P55106; -.
DR eggNOG; KOG3900; Eukaryota.
DR HOGENOM; CLU_020515_0_0_1; -.
DR InParanoid; P55106; -.
DR OrthoDB; 749511at2759; -.
DR TreeFam; TF316134; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
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 Apoptosis; Cleavage on pair of basic residues; Cytokine;
KW Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..350
FT /evidence="ECO:0000255"
FT /id="PRO_0000425155"
FT CHAIN 351..470
FT /note="Growth/differentiation factor 6"
FT /id="PRO_0000425156"
FT REGION 28..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 369..435
FT /evidence="ECO:0000250|UniProtKB:P39905"
FT DISULFID 398..467
FT /evidence="ECO:0000250|UniProtKB:P39905"
FT DISULFID 402..469
FT /evidence="ECO:0000250|UniProtKB:P39905"
FT DISULFID 434
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P39905"
SQ SEQUENCE 470 AA; 52112 MW; 6C40B980E8207A1F CRC64;
MDTSRVLLSA VFLISFLWDL PGFQQASISS SSSSAELGSA KGMRSRKEGR MPRAPRENAT
AREPLDRQEP PPRPQEEPQR RPPQQPEARE PPGRGPRVVP HEYMLSIYRT YSIAEKLGIN
ASFFQSSKSA NTITSFVDRG LDDLSHTPLR RQKYLFDVST LSDKEELVGA ELRLFRQAPA
APWGPPAGPL RLQLFACQSP LLLEARSLDP QGAPRPGWEV FDVWRGLRPQ PWKQLCLELR
AAWGGEPGAA EDEARAPGPQ QPPPPDLRSL GFGRRVRTPQ ERALLVVFSR SQRKTLFAEM
REQLGSATEV VGPGGGAEGS GPPPPPPPPP PSGTPDAGLW SPSPGRRRRR TAFASRHGKR
HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT
LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE EMVVESCGCR
