ID H3BFI1_LATCH Unreviewed; 401 AA.
AC H3BFI1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
GN Name=TGFB1 {ECO:0000313|Ensembl:ENSLACP00000020652.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000020652.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000020652.1}
RP IDENTIFICATION.
RG Ensembl;
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; AFYH01010036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01010037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01010038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01010039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01010040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01010041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BFI1; -.
DR STRING; 7897.ENSLACP00000020652; -.
DR Ensembl; ENSLACT00000020792.1; ENSLACP00000020652.1; ENSLACG00000018146.2.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000155747; -.
DR InParanoid; H3BFI1; -.
DR OMA; LALEYMC; -.
DR TreeFam; TF351793; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000018146; Expressed in mesonephros and 5 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008672};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR001787};
KW Signal {ECO:0000256|PIRNR:PIRNR001787}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT CHAIN 24..401
FT /note="Transforming growth factor beta"
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT /id="PRO_5003580792"
FT DOMAIN 286..401
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT COILED 74..101
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 296..305
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 304..367
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 333..398
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 337..400
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 366
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ SEQUENCE 401 AA; 46246 MW; DC6AE61D31C96C60 CRC64;
FSMGIQRAFL VFLLLDSISW TLSLSTCKTF DMDMAKRKRI EAIRGQILSK LKLSKAPEEE
SDEVVVPEVV MSLYNSTRDM VEELTREQDQ IETAEEEYYA KEVTKFEIIP QNQYHHQSRK
TPRGITEKNF LFNVSQIRGN ISDEGLLHRA ELRILRESNP SASLTTQRVE LYQILTRFAE
LKDQRYLESR VVNPRDAAEW ISFDVTESVK QWINSKEASH GFQLKAHCPC GASVSFSDLS
VPIFLFQGLD TKRGDLELFS MKNQKLPHLL IMSTPAERAE HLHSSKRKRD VDTTYCFENV
EKNCCVRPLY IDFRKDLGWK WIHEPKGYSA NFCMGPCPYI WSMDTQYSKV LALYNQHNPD
ASAAPCCVPQ VLEPLPILYY VGRQAKVEQL SNMVVKSCKC S
//
