ID A0A5C6PDH6_9TELE Unreviewed; 541 AA.
AC A0A5C6PDH6;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 17.
DE SubName: Full=Suppressor of cytokine signaling 5 {ECO:0000313|EMBL:TWW77049.1};
GN ORFNames=D4764_12G0004390 {ECO:0000313|EMBL:TWW77049.1};
OS Takifugu flavidus (sansaifugu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=433684 {ECO:0000313|EMBL:TWW77049.1, ECO:0000313|Proteomes:UP000324091};
RN [1] {ECO:0000313|EMBL:TWW77049.1, ECO:0000313|Proteomes:UP000324091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTHZ2018 {ECO:0000313|EMBL:TWW77049.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TWW77049.1};
RA Xiao S.;
RT "Chromosome genome assembly for Takifugu flavidus.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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:TWW77049.1}.
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DR EMBL; RHFK02000004; TWW77049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6PDH6; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000324091; Chromosome 12.
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:UP000324091};
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 392..487
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 482..531
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..46
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..56
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 60210 MW; F3089EE15179905F CRC64;
MSLPKETGNR DEVPDRGARP KVRQSRSEER RDAGRGRKSS RGKKKGSASN AAAAERPASD
GFEYGELLGD LHTRDQSSSS PLKENWRGFD AATSLPGPEQ VTSRLGLGPF SSSMEPSAPS
ERESRGSNSN RTLRQKIQDA MGQCFPIKTH AAAAPATPQA LAPSAASASS RRKIHLSELM
LDDCPFPAGS ELAQKWYLIK QHTAPITQPP VLDSPAGPST PVSSLPTAVD DVDDRLRERR
RISIEQGVEP PPNAEIHTFE VTAQINPLYK HGPKLAHGMN ELAGPDAAPL PLPLPLPQQQ
ELLLQRQQQH QLLLQRCLDT LDEVVASASF HACSANSDAQ PDAELAASGT PPRADPLQAE
HLKPQHGYRV HTQIDYIHCL VPDLLQISSL PYYWGVMDRY EAETLLEGKP EGTFLLRDSA
QEDYLFSVSF RRYGRSLHAR IEQWNHNFSF DVHDPSVFHA PTVTGLLEHY KDPNSCMFFE
PLLSNPIHRK QPFQLQHICR AVISSRTTYD GINVLPIPNV LKKHLKEYHY KQRVRVRRMD
A
//