ID A0A091EHU9_CORBR Unreviewed; 412 AA.
AC A0A091EHU9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
GN ORFNames=N302_00733 {ECO:0000313|EMBL:KFO56646.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO56646.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO56646.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO56646.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK718445; KFO56646.1; -; Genomic_DNA.
DR RefSeq; XP_008628563.1; XM_008630341.2.
DR AlphaFoldDB; A0A091EHU9; -.
DR STRING; 85066.A0A091EHU9; -.
DR GeneID; 103612645; -.
DR KEGG; cbrc:103612645; -.
DR CTD; 7042; -.
DR OrthoDB; 5390486at2759; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; IEA:InterPro.
DR GO; GO:0009790; P:embryo development; IEA:UniProt.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0009888; P:tissue development; IEA:UniProt.
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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001787-1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
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:UP000052976};
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..412
FT /note="Transforming growth factor beta"
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT /id="PRO_5016196257"
FT DOMAIN 297..412
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT DISULFID 307..316
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 315..378
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 344..409
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 348..411
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 377
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ SEQUENCE 412 AA; 47604 MW; 8CA3940F7CBE2DFD CRC64;
MHCYLLSVLL TVDLATVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPDEYPEP
EEVPPEVISI YNSTRDLLQE KANHRAATCE RERSDEEYYA KEVYKIDMQP FYPENAIPPS
YYSLYFRIVR FDVSAMEKNA SNLVKAEFRV FRLQNSKARV SEQRIELYQV LKSKELSSPG
QRYIDSKVVK TRAEGEWLSF DVTEAVHEWL HHRDRNLGFK ISLHCPCCTF VPSNNYIIPN
KSEELEARFA GIDDYTYSSG DVKALKSNRK KYSGKTPHLL LMLLPSYRLE SQQPSRRKKR
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYH ANFCAGACPY LWSSDTQHSR
VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS
//
