ID A0A401NXX0_SCYTO Unreviewed; 414 AA.
AC A0A401NXX0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
GN ORFNames=scyTo_0000455 {ECO:0000313|EMBL:GCB65713.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB65713.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB65713.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB65713.1}.
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DR EMBL; BFAA01000088; GCB65713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401NXX0; -.
DR STRING; 75743.A0A401NXX0; -.
DR OMA; FRIYQVE; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
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 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:UP000288216};
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_5018825373"
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; 48263 MW; 4F4682FB90859EC4 CRC64;
MHYSIFTVFL TLDFAMIAAC LSTCNTLDME QFMKKRIEAI RGQILSKLKL TNPPEHYPEP
EEVTTEVLAI YNSTRDLLLE KANERAATCE RERSEEEYYA KEVYKIDTNP PNHPENVILP
QQYNPYFRRV YLDVTSMEKN VSNLVKAEFR VFRLQNPKAK VEEQRIELYQ ILKSKEPSSP
SQRYIDSKVV RTRTEGEWLS FDVTETVNEW LLHRDRNLGF KISLHCPCCT FVPSNNYIIP
NKSEELEARF AGIYDNHLRD YSSGDMRKLK SNHYNGKTAH LILMLLPTYR LESQQSSRRK
KRALDAAFCF RNVQDNCCLR PLYIDFRRDL GWKWIHEPKG YQANFCAGAC PYLWSSDTQH
SRILSLYNNI NPEASASPCC VSQDLEPLTI LYFVGKVPKI EHLSNMVVKS CKCS
//
