ID A0A6I9X7K1_9SAUR Unreviewed; 435 AA.
AC A0A6I9X7K1;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Suppressor of cytokine signaling 4 {ECO:0000313|RefSeq:XP_013910236.1};
GN Name=SOCS4 {ECO:0000313|RefSeq:XP_013910236.1};
OS Thamnophis sirtalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Natricinae; Thamnophis.
OX NCBI_TaxID=35019 {ECO:0000313|Proteomes:UP000504617, ECO:0000313|RefSeq:XP_013910236.1};
RN [1] {ECO:0000313|RefSeq:XP_013910236.1}
RP IDENTIFICATION.
RC TISSUE=Skeletal muscle {ECO:0000313|RefSeq:XP_013910236.1};
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_013910236.1; XM_014054761.1.
DR AlphaFoldDB; A0A6I9X7K1; -.
DR GeneID; 106539854; -.
DR KEGG; tsr:106539854; -.
DR CTD; 122809; -.
DR OrthoDB; 8820570at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000504617; 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:UP000504617};
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 281..376
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 371..420
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 50103 MW; 2EB24EFFA151797D CRC64;
MAENKERKPK NADVRPKTSR SRSADRKDGY VWSGKKLSWT KKSENSSNAE MANASGIPTL
SLRNQERKQS CSSAEMELEH VCGHRFLSRS FKQKLQDAMG QCFPIKSCNT RHSSGLSPKR
KIHISELMLD KCPFPPRSEL AFRWHLIKQH TAPVRQKSES WLSVGSSKGE RKDEDLREID
GTDEPDSNVL QESNVIDSYP CDPQEESAMG GKQLKSSREE SDMDSDDEVV TLCTSSRKRN
KPRWEIEDDL LQLQMPLRYH TQIDYVHCLV PDLLQINNNP CYWGVMDKYA AEALLDGKPE
GTFLLRDSAQ EDYLFSVSFR RYSRSLHARI EQWNHNFSFD AHDPCVFHSR DITGLLEHYK
DPSSCMFFEP LLSTPLHRTF PFSLQHLCRT VICNSTTYDG INALPVPPSV KLYLKEYHYK
SKVRVLRIDV PDQHA
//
