ID A0A8C5Q6P2_9ANUR Unreviewed; 428 AA.
AC A0A8C5Q6P2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=Suppressor of cytokine signaling 4 {ECO:0000313|Ensembl:ENSLLEP00000032554.1};
GN Name=SOCS4 {ECO:0000313|Ensembl:ENSLLEP00000032554.1};
OS Leptobrachium leishanense (Leishan spiny toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pelobatoidea; Megophryidae; Leptobrachium.
OX NCBI_TaxID=445787 {ECO:0000313|Ensembl:ENSLLEP00000032554.1, ECO:0000313|Proteomes:UP000694569};
RN [1] {ECO:0000313|Ensembl:ENSLLEP00000032554.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSLLEP00000032554.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR AlphaFoldDB; A0A8C5Q6P2; -.
DR Ensembl; ENSLLET00000033817.1; ENSLLEP00000032554.1; ENSLLEG00000020658.1.
DR GeneTree; ENSGT00940000161456; -.
DR OrthoDB; 8820570at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000694569; Unplaced.
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: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:UP000694569};
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 274..369
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 364..413
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..14
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..44
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 48423 MW; DE196A9D7F734801 CRC64;
MAENLEDKVD DLNVRPKSSR SRSADRKDGY VWSGKKLSWS SKGGRSLDGD GRASADRKDS
PTGSRERKHS CSSVELDMER SCGHKLLGRS LKQKLQDAVG QCFPIKTCSS RHSSALSSKR
KIHISELMLD KCPFPPKSDL AYRWHLIKRH TAPVNPGHEE SAVGDFPDGP GKDSRLEDET
SNGTEGVLSS SCEVNIDVVE SVTTKASRAD KEDSDVDSDD DVVTLCTSSR KRNKPKWEPD
DETFHAETPP KYHTQIDYVH CLVPDLLQVN NNPCYWGVMD RYAAEALLES KPEGTFLLRD
SAQEDYLFSV SFRRYSRSLH ARIEQWNHNF SFDAHDPCVF HAPNVTGLLE HYKDPSSCMF
FEPLLSSPLS RTFTFSLQHI CRTVICNCTS YDGIDALPVP SSMKLYLKEY HYKSKVRVRR
VDVPEQHK
//
