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Database: UniProt
Entry: A0A3B4FI24_9CICH
LinkDB: A0A3B4FI24_9CICH
Original site: A0A3B4FI24_9CICH 
ID   A0A3B4FI24_9CICH        Unreviewed;       395 AA.
AC   A0A3B4FI24;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
GN   Name=TGFB3 {ECO:0000313|Ensembl:ENSPNYP00000010172.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000010172.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000010172.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Transforming growth factor beta-3 proprotein: Precursor of
CC       the Latency-associated peptide (LAP) and Transforming growth factor
CC       beta-3 (TGF-beta-3) chains, which constitute the regulatory and active
CC       subunit of TGF-beta-3, respectively. {ECO:0000256|ARBA:ARBA00003972}.
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; A0A3B4FI24; -.
DR   STRING; 303518.ENSPNYP00000010172; -.
DR   Ensembl; ENSPNYT00000010422.1; ENSPNYP00000010172.1; ENSPNYG00000007736.1.
DR   GeneTree; ENSGT00940000155747; -.
DR   Proteomes; UP000261460; 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:0051781; P:positive regulation of cell division; IEA:UniProtKB-UniRule.
DR   CDD; cd19386; TGF_beta_TGFB3; 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; IPR015618; TGFB3.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR   PANTHER; PTHR11848:SF34; TRANSFORMING GROWTH FACTOR BETA-3 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; PR01426; TGFBETA3.
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   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR001787};
KW   Signal {ECO:0000256|PIRNR:PIRNR001787}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT   CHAIN           22..395
FT                   /note="Transforming growth factor beta"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT                   /id="PRO_5017107211"
FT   DOMAIN          280..395
FT                   /note="TGF-beta family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51362"
FT   DISULFID        290..299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT   DISULFID        298..361
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT   DISULFID        327..392
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT   DISULFID        331..394
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT   DISULFID        360
FT                   /note="Interchain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ   SEQUENCE   395 AA;  45609 MW;  55491957E985AB03 CRC64;
     MHLGKALLFV ILLNCATLSS SLSTCATVDI DHVKRKRVEA IRGQILSKLR LTSPPQSLGP
     SKIPYQIQAL YNSTKELLEE LGRDRQQSCG QDNSETEYYA KEIYKFNMDN GPPENNDLSY
     CPKGITSKVF RFNISAMERN ATNLFRAEFR ALRVPNSTAK RNEQRIELYQ IVRRNEHIRK
     QRFIGAKNVL TKGTAEWISF DVTETVREWL MKRGSNMGLE ISVHCPFVHL DHVYNQGIDE
     EEEHSRLDLD HLKRKMEQNL PHLILMMIPP HRLDTQSTRR RKRALDTNYC FSNTEESCCV
     RRLHIDFRRD LDWKWIHEPS GYDANYCSGP CPYLRSSDTT HSSLLSLYNT LNPEASASPC
     CVPQDLEPLT ILYYSGRTPK VEQLSNMIVK SCKCS
//
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