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Database: UniProt
Entry: A0A6P8GHW8_CLUHA
LinkDB: A0A6P8GHW8_CLUHA
Original site: A0A6P8GHW8_CLUHA 
ID   A0A6P8GHW8_CLUHA        Unreviewed;       643 AA.
AC   A0A6P8GHW8;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   SubName: Full=Suppressor of cytokine signaling 5b {ECO:0000313|RefSeq:XP_031434494.1, ECO:0000313|RefSeq:XP_031434495.1};
GN   Name=socs5b {ECO:0000313|RefSeq:XP_031434494.1,
GN   ECO:0000313|RefSeq:XP_031434495.1};
OS   Clupea harengus (Atlantic herring).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes; Clupeoidei;
OC   Clupeidae; Clupea.
OX   NCBI_TaxID=7950 {ECO:0000313|Proteomes:UP000515152, ECO:0000313|RefSeq:XP_031434495.1};
RN   [1] {ECO:0000313|RefSeq:XP_031434494.1, ECO:0000313|RefSeq:XP_031434495.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (APR-2025) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   RefSeq; XP_031434494.1; XM_031578634.2.
DR   RefSeq; XP_031434495.1; XM_031578635.2.
DR   AlphaFoldDB; A0A6P8GHW8; -.
DR   GeneID; 105900024; -.
DR   KEGG; char:105900024; -.
DR   CTD; 559639; -.
DR   GeneTree; ENSGT00940000164285; -.
DR   OrthoDB; 8820570at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000515152; Chromosome 13.
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:SF15; SUPPRESSOR OF CYTOKINE SIGNALING 5; 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:UP000515152};
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          487..582
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          577..626
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          86..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..181
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..246
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..461
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  68553 MW;  DA7A0C6D44CD411A CRC64;
     MAKAGKMWSS LRSRCHTLLH LDGPCEVMDA ASCGVDLARG GCSGEPRASS PLRSLSPLTP
     MVVPRRGHNC VTDGPQILEI MLDRDGEDMR RGPGGVTLGR RDSYSRHAPW GGKKKHSCST
     KTQSSLEAER RGGRASRAAG RRERRYAVSS IQEIAEPGGG GGGGRGGGGG GGADRGGGGA
     AGRSLSARSL RQRLRDTVGL CLPLSPRRRS RSTSSKPASC SLTFSTVSSS SSSSSSSSAG
     SSCSSSSKRK IHLTELMLET CPFPPGSDLA NKWHLIKQHT APVSPQASSA LLTSDPAEAA
     TGHSHAAPED EEERMRERRR ISIEEGVDPP PNAQIHTLDA GLPPSSASSS SIYKLGPKMA
     PASSGPSDAM TSAEVGRVNL GGMVTSGSVL GGLVAQALSG LSASSSFSHP PPSEDCDSEE
     DSTTLCLQAR RPKQRHASGD GHASRQGGGG AGSSSSGGAG GPWKVHTQID YIHCLVPDLL
     RITALPCYWG VMDRYQAEAL LDGRPEGTFL LRDSAQEDYL FSVSFRRYNR SLHARIEQWN
     HNFSFDAHDP CVFHASTVTG LLEHYKDPSA CMFFEPLLTA PLHRTFPFGL QSLARAAICQ
     RVTYDGIAAL PLPPALQDFL KEYHYKQKVR VRWLERELPV RGK
//
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