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Database: UniProt
Entry: A0A5A9MTG8_9TELE
LinkDB: A0A5A9MTG8_9TELE
Original site: A0A5A9MTG8_9TELE 
ID   A0A5A9MTG8_9TELE        Unreviewed;       508 AA.
AC   A0A5A9MTG8;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   05-FEB-2025, entry version 15.
DE   SubName: Full=Suppressor of cytokine signaling 5 {ECO:0000313|EMBL:KAA0701624.1};
GN   ORFNames=E1301_Tti020283 {ECO:0000313|EMBL:KAA0701624.1};
OS   Triplophysa tibetana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Nemacheilidae; Triplophysa.
OX   NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0701624.1, ECO:0000313|Proteomes:UP000324632};
RN   [1] {ECO:0000313|EMBL:KAA0701624.1, ECO:0000313|Proteomes:UP000324632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0701624.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAA0701624.1};
RX   PubMed=30977968;
RA   Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA   Wang W., Yang R.;
RT   "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT   to the harsh high-altitude environment of the Tibetan Plateau.";
RL   Mol. Ecol. Resour. 19:1027-1036(2019).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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:KAA0701624.1}.
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DR   EMBL; SOYY01000025; KAA0701624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5A9MTG8; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000324632; Chromosome 25.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:TreeGrafter.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IEA:TreeGrafter.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.30.505.10:FF:000028; Suppressor of cytokine signaling 5; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR022252; SOCS4/SOCS5_dom.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10155:SF18; SUPPRESSOR OF CYTOKINE SIGNALING 9 ISOFORM X1; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF12610; SOCS; 1.
DR   Pfam; PF07525; SOCS_box; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00253; SOCS; 1.
DR   SMART; SM00969; SOCS_box; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF158235; SOCS box-like; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50225; SOCS; 1.
PE   4: Predicted;
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324632};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          356..451
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          446..495
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..43
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  56442 MW;  4DAA400A30B58DA3 CRC64;
     MSLPEDRGKE RERGARPKVR QSRSEERRDG GRRKGVRGKK KNHPSHDLTS VRPVSDGFEY
     GDLLNGLQGS SEGGSSSPVT EHWRWQVLGS SGSLLSEKVS ARPSLSSPAS DPGCDADSKS
     SGASRTLRQK IQDAVGQCFP IKSHSQGLSQ PGPATALCSS RRKIHLSELM LDSCPFPPGS
     DLAQKWNLIK QHTAPLSLAP IPDSSATTAT FVATPVEDEE DRLRERRRIS IEQGVEPPPN
     ALIHTFEVTA QINPQYKLGP KLAHGMNELA GDERATLHQL LLQSCLDTLD EVAAASSVTA
     DVELSAASPT APSLTGATFV QTDSPKSLDG QHRVHTQIDY IHCLVPDLLQ ITNLPCYWGV
     MDRYQAETLL EGKPEGTFLL RDSAQEDYLF SVSFRRYGRS LHARIEQWNH NFSFDVHDPS
     VFHAPTVTGL LEHYKDPNSC MFFEPLLSTP THRTHPFSLQ HICRAVISGC TTYDGINTLP
     LPNSLKEHLK EYHYKQRVRI RRLDAWWE
//
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