ID C0HB75_SALSA Unreviewed; 381 AA.
AC C0HB75;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
GN Name=TGFB1 {ECO:0000313|EMBL:ACN11294.1};
GN Synonyms=LOC100136559 {ECO:0000313|RefSeq:XP_014051977.1,
GN ECO:0000313|RefSeq:XP_014051978.1, ECO:0000313|RefSeq:XP_014051979.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACN11294.1};
RN [1] {ECO:0000313|EMBL:ACN11294.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN11294.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACN11294.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN11294.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACN11294.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN11294.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:XP_014051977.1, ECO:0000313|RefSeq:XP_014051978.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014051977.1,
RC ECO:0000313|RefSeq:XP_014051978.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of
CC the Latency-associated peptide (LAP) and Transforming growth factor
CC beta-1 (TGF-beta-1) chains, which constitute the regulatory and active
CC subunit of TGF-beta-1, respectively. {ECO:0000256|ARBA:ARBA00002007}.
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; BT059581; ACN11294.1; -; mRNA.
DR RefSeq; XP_014051977.1; XM_014196502.1.
DR RefSeq; XP_014051978.1; XM_014196503.1.
DR RefSeq; XP_014051979.1; XM_014196504.1.
DR STRING; 8030.ENSSSAP00000004983; -.
DR PaxDb; 8030-ENSSSAP00000004983; -.
DR Ensembl; ENSSSAT00000005337; ENSSSAP00000004983; ENSSSAG00000002509.
DR GeneID; 100136559; -.
DR KEGG; sasa:100136559; -.
DR OMA; LALEYMC; -.
DR OrthoDB; 5390486at2759; -.
DR Proteomes; UP000087266; Chromosome ssa04.
DR Bgee; ENSSSAG00000002509; Expressed in head kidney and 7 other cell types or tissues.
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:0051781; P:positive regulation of cell division; IEA:UniProtKB-UniRule.
DR CDD; cd19384; TGF_beta_TGFB1; 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; IPR003939; TGFb1.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR PANTHER; PTHR11848:SF125; TRANSFORMING GROWTH FACTOR BETA-1 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; PR01424; TGFBETA1.
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 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:UP000087266};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR001787};
KW Signal {ECO:0000256|PIRNR:PIRNR001787}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT CHAIN 23..381
FT /note="Transforming growth factor beta"
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT /id="PRO_5010827500"
FT DOMAIN 266..381
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT DISULFID 284..347
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 313..378
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 317..380
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 346
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ SEQUENCE 381 AA; 44322 MW; C91BF8CEA319FF56 CRC64;
MRAECLTLVV LLALEYMCRS EAMSTCKSLD LELMKRKRIE AIRGQILSKL RLPKEPEIDQ
EGDFEKVPTS LISIYNSTVE LSEEQVHTCI PPTQDTEEEA YFAKEVHKFN MKQSENNIKH
QMLFNMSEMR SVLGTDRLLS QAELRLLIKN RGMQDSSEQR LELYRGVGDK ARYMKSHFIS
KEWANRWISF DVTQTLREWL QGAGKEQGFQ LKLPCDCGKT MEEFRFEIAG MNKPRGDKET
LFMNMPKPHI LLMSLPVERH SQLSSRKKRQ TTTEEICSDK SESCCVRKLY IDFRKDLGWK
WIHEPTGYFA NYCMGPCTYI WNTENKYSQV LALYKHHNPG ASAQPCCVPQ VLEPLPILYY
VGRQHKVEQL SNMIVKSCKC S
//
