ID   A0A091K3K6_COLST        Unreviewed;       436 AA.
AC   A0A091K3K6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-JAN-2026, entry version 49.
DE   SubName: Full=Suppressor of cytokine signaling 4 {ECO:0000313|EMBL:KFP30788.1};
GN   ORFNames=N325_07624 {ECO:0000313|EMBL:KFP30788.1};
OS   Colius striatus (Speckled mousebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Coraciimorphae;
OC   Coliiformes; Coliidae; Colius.
OX   NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP30788.1, ECO:0000313|Proteomes:UP000053615};
RN   [1] {ECO:0000313|EMBL:KFP30788.1, ECO:0000313|Proteomes:UP000053615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP30788.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK540675; KFP30788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091K3K6; -.
DR   KEGG; csti:104555949; -.
DR   OrthoDB; 8820570at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053615; Unassembled WGS sequence.
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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd10385; SH2_SOCS4; 1.
DR   CDD; cd03738; SOCS_SOCS4; 1.
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; IPR035864; SOCS4_SH2.
DR   InterPro; IPR037342; SOCS4_SOCS.
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:SF21; SUPPRESSOR OF CYTOKINE SIGNALING 4; 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:UP000053615};
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          282..377
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          372..421
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  49582 MW;  B953F005FC2D5157 CRC64;
     MAENKDSNVK NADVRPKSSR SRSADRKDGY VWSGKKLSWS KKSEHCPDAE TASAAGRSGT
     NLKSQERKYS CSSVELDLDR SCGHRFLGRS LKQKLQDAVG QCFPIKNCSS RHASGPPSKR
     KIHISELMLD KCPFPPRSEL AFRWHLIKRH TAPVNPKAEE WIIADLSQRE ETEGQLRDGE
     IANGEADSPS QSCDLTDSGS SRGDSRSELV TGKVVRSGRD ESDMDSDDEV ITLCTSSRKR
     NKPKWETDDE LLRMETPPKY HTQIDYVHCL VPDLLQINNN PCYWGVMDKY AAEALLEGKP
     EGTFLLRDSA QEDYLFSVSF RRYSRSLHAR IEQWNHNFSF DAHDPCVFHS PDITGLLEHY
     KDPSSCMFFE PLLSTPLNRT FPFSLQHICR TVICNCTTYD GIDALPIPPS VKLYLKEYHY
     KSKVRVLRID VPEQQS
//