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Database: UniProt
Entry: A0A2K5IW34_COLAP
LinkDB: A0A2K5IW34_COLAP
Original site: A0A2K5IW34_COLAP 
ID   A0A2K5IW34_COLAP        Unreviewed;       442 AA.
AC   A0A2K5IW34;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000020707.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000020707.1}
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   RefSeq; XP_011784831.1; XM_011929441.1.
DR   RefSeq; XP_011784832.1; XM_011929442.1.
DR   SMR; A0A2K5IW34; -.
DR   STRING; 336983.ENSCANP00000020677; -.
DR   Ensembl; ENSCANT00000043649.1; ENSCANP00000020677.1; ENSCANG00000033744.1.
DR   Ensembl; ENSCANT00000043679.1; ENSCANP00000020707.1; ENSCANG00000033744.1.
DR   GeneID; 105502787; -.
DR   KEGG; cang:105502787; -.
DR   CTD; 7042; -.
DR   OrthoDB; 5390486at2759; -.
DR   Proteomes; UP000233080; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR001787-1};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000233080};
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..442
FT                   /note="Transforming growth factor beta"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT                   /id="PRO_5014295117"
FT   DOMAIN          327..442
FT                   /note="TGF-beta family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51362"
FT   DISULFID        337..346
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT   DISULFID        345..408
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT   DISULFID        374..439
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT   DISULFID        378..441
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT   DISULFID        407
FT                   /note="Interchain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ   SEQUENCE   442 AA;  50573 MW;  5D7A3C2ED51753D5 CRC64;
     MHYCVLSAFL ILHLVTVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP
     EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPP FFPSETVCPV
     VTTPSGSVGS LCSRQSQVLC GYLDAIPPTF YRPYFRIVRF DVSAMEKNAS NLVKAEFRVF
     RLQNPKARVP EQRIELYQIL KSKDLTSPTQ RYIDSKVVKT RAEGEWLSFD VTDAVHEWLH
     HKDRNLGFKI SLHCPCCTFV PSNNYIIPNK SEELEARFAG IDGTSTYTSG DQKTIKSTRK
     KNSGKTPHLL LMLLPSYRLE SQQTNRRKKR ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW
     KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY
     YIGKTPKIEQ LSNMIVKSCK CS
//
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