ID A0A3Q1IBV5_ANATE Unreviewed; 414 AA.
AC A0A3Q1IBV5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000001906.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000001906.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q1IBV5; -.
DR STRING; 64144.ENSATEP00000001906; -.
DR Ensembl; ENSATET00000001929.2; ENSATEP00000001906.1; ENSATEG00000001337.2.
DR GeneTree; ENSGT00940000157390; -.
DR InParanoid; A0A3Q1IBV5; -.
DR OMA; FYIDFKR; -.
DR OrthoDB; 5390486at2759; -.
DR Proteomes; UP000265040; Unplaced.
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:0042221; P:response to chemical; IEA:UniProt.
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 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:UP000265040};
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..414
FT /note="Transforming growth factor beta"
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT /id="PRO_5018384190"
FT DOMAIN 299..414
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT DISULFID 309..318
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 317..380
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 346..411
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 350..413
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 379
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ SEQUENCE 414 AA; 47557 MW; EBF23B3B3CA9B382 CRC64;
MNLCIVSLLL TLDLATVALS LSTCSTLDMD QFKKKRIEAI RGQILSKLKL TNPPTDFPQP
EEVSRDIVAI YNSTRDLLQE KANERAATCE RQRSEEEYYA KEVHKIDMQP LYPSENVISP
THFNPYFRRL TFDVSSMEKN ASNLVKAELR IFRLQNPVAR VSEQRIELYQ ILGHKDLTSP
TQRYIDSKVV RTQTEGEWLS FDVTEAVSEW LNHRERNSGF KISLHCPCCT FVPSNNYIIP
NKSEELEARF AGIDDSIHDS DLKLFKKRRH GVRAPHLLLM LLPSYRLQSQ SQLQHINHRS
KRALDAAFCS KNVQDNCCLR SLYIDFKKDL GWRWIHEPKG YEANFCAGAC PYLWSADTQH
SKVLGLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI EQLSNMKVKS CKCS
//