ID A0A6P8GWA1_CLUHA Unreviewed; 542 AA.
AC A0A6P8GWA1;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Suppressor of cytokine signaling 5-like {ECO:0000313|RefSeq:XP_031439040.1};
GN Name=LOC105896939 {ECO:0000313|RefSeq:XP_031439040.1};
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_031439040.1};
RN [1] {ECO:0000313|RefSeq:XP_031439040.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR RefSeq; XP_031439040.1; XM_031583180.2.
DR AlphaFoldDB; A0A6P8GWA1; -.
DR GeneID; 105896939; -.
DR KEGG; char:105896939; -.
DR OrthoDB; 8820570at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000515152; Chromosome 16.
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 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 387..482
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 477..527
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 15..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..75
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..325
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 58762 MW; A7A525221C1514D3 CRC64;
MERVGKVWSN LKRGCQSLLH PDGGARDQAP HQEASPSSRP LPTSLPRYAG RANNNNNTGS
SSSAPSGGSS VPRPGQNCVV DMAQVLEITL EQEGDGRPGQ LGSRRDSYSR HAPWSGKKRH
SCSTRAQGSL EGRDRGGRGR CRRRGEDLEP GGGGRSLRQQ LQDTMGLCLP LRCSASRAPP
KRKIHLTELM METCPFPPGS DLARKWHLIK QHTVPVPAAS AAPAPLPPSA SGQQDWSRGA
APSAEDEEER LRERRRLSIE EGVDPPPNAQ IHTVEALACL HKLGPKLAPG LTEGSGEAGA
GAGAGGGGGG GGGGGGGGGG GGGGAAPDCD SEEEDGTTLC MQTRRMRQRQ PQPPPPPAPE
GPWRVHTQID YIHCLVPDLQ QITALPCYWG VMDRYQAEAL LDGRPEGSFL LRDSAQEDYL
FSVSFRRYGR SLHARIEQWN HNFSFDAHDP CVFHAATVTA LLEHYKDPSA CMFFEPLLTS
PVPRSFPFAL QGLARAAICR RVSYDGIGAL QLLPPPLQDY LREYHYKQRV RVRWLERELK
AK
//
