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Database: UniProt
Entry: A0A1U7REV2_ALLSI
LinkDB: A0A1U7REV2_ALLSI
Original site: A0A1U7REV2_ALLSI 
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}.
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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
//
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