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Database: UniProt
Entry: A0A3Q1IBV5_ANATE
LinkDB: A0A3Q1IBV5_ANATE
Original site: A0A3Q1IBV5_ANATE 
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
//
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