ID A0A1U7REV2_ALLSI Unreviewed; 413 AA.
AC A0A1U7REV2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
GN Name=TGFB2 {ECO:0000313|RefSeq:XP_006022407.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006022407.1};
RN [1] {ECO:0000313|RefSeq:XP_006022407.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006022407.1; XM_006022345.2.
DR AlphaFoldDB; A0A1U7REV2; -.
DR STRING; 38654.A0A1U7REV2; -.
DR GeneID; 102382227; -.
DR KEGG; asn:102382227; -.
DR CTD; 7042; -.
DR eggNOG; KOG3900; Eukaryota.
DR InParanoid; A0A1U7REV2; -.
DR OrthoDB; 5390486at2759; -.
DR Proteomes; UP000189705; 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: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:UP000189705};
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..413
FT /note="Transforming growth factor beta"
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT /id="PRO_5010538512"
FT DOMAIN 298..413
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT DISULFID 308..317
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 316..379
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 345..410
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 349..412
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 378
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ SEQUENCE 413 AA; 47605 MW; E0091F4E1E064915 CRC64;
MPCYLLSLLL SLDLAAVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPDEYPEP
EEVPPEVISI YNSTRDLLQE KANHRAATCE RERSEEEYYA KEVYKIDMLP FYPENAIPPS
YYSLYYRIVR FDVSAMEKNA SNLVKAEFRV FRLQNSKARV SEQRIELYQV VKSKELPSPG
QRYIDSKVVK TRAEGEWLSF DVTDAVHEWL HHRDRNLGFK ISLHCPCCTF VPSNNYIIPN
KSEELEARFA GIDDSYTYSS GDVKALKSNK KKYSGKTPHL LLMLLPSYRL ESQQPSRRKK
RALDAAYCFR NVQDNCCLRP LYIDFKRDLG WKWIHEPKGY HANFCAGACP YLWSSDTQHS
RVLSLYNTIN PEASASPCCV SQDLEPLTIL YYIGKTPKIE QLSNMIVKSC KCS
//