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SOCS4_MOUSE
ID   SOCS4_MOUSE             Reviewed;         436 AA.
AC   Q91ZA6; Q149F7; Q149F8;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Suppressor of cytokine signaling 4;
DE            Short=SOCS-4;
DE   AltName: Full=Suppressor of cytokine signaling 7;
DE            Short=SOCS-7;
GN   Name=Socs4; Synonyms=Socs7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hilton D.J.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: SOCS family proteins form part of a classical negative
CC       feedback system that regulates cytokine signal transduction. Substrate-
CC       recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box
CC       protein) E3 ubiquitin-protein ligase complex which mediates the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. Inhibits EGF signaling by mediating the degradation of the
CC       Tyr-phosphorylated EGF receptor/EGFR (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC       BC complex, an adapter module in different E3 ubiquitin ligase
CC       complexes. {ECO:0000250}.
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DR   EMBL; AY046322; AAL03942.1; -; mRNA.
DR   EMBL; CH466605; EDL20739.1; -; Genomic_DNA.
DR   EMBL; BC117814; AAI17815.1; -; mRNA.
DR   EMBL; BC117815; AAI17816.1; -; mRNA.
DR   CCDS; CCDS26985.1; -.
DR   RefSeq; NP_543119.2; NM_080843.2.
DR   AlphaFoldDB; Q91ZA6; -.
DR   SMR; Q91ZA6; -.
DR   BioGRID; 212083; 3.
DR   STRING; 10090.ENSMUSP00000066031; -.
DR   iPTMnet; Q91ZA6; -.
DR   PhosphoSitePlus; Q91ZA6; -.
DR   PaxDb; Q91ZA6; -.
DR   PRIDE; Q91ZA6; -.
DR   ProteomicsDB; 261546; -.
DR   Antibodypedia; 4604; 295 antibodies from 34 providers.
DR   DNASU; 67296; -.
DR   Ensembl; ENSMUST00000065562; ENSMUSP00000066031; ENSMUSG00000048379.
DR   GeneID; 67296; -.
DR   KEGG; mmu:67296; -.
DR   UCSC; uc007thx.1; mouse.
DR   CTD; 122809; -.
DR   MGI; MGI:1914546; Socs4.
DR   VEuPathDB; HostDB:ENSMUSG00000048379; -.
DR   eggNOG; KOG4566; Eukaryota.
DR   GeneTree; ENSGT00940000161456; -.
DR   HOGENOM; CLU_035609_0_0_1; -.
DR   InParanoid; Q91ZA6; -.
DR   OMA; PSPMKLY; -.
DR   OrthoDB; 722019at2759; -.
DR   PhylomeDB; Q91ZA6; -.
DR   TreeFam; TF321368; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 67296; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Socs4; mouse.
DR   PRO; PR:Q91ZA6; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q91ZA6; protein.
DR   Bgee; ENSMUSG00000048379; Expressed in humerus cartilage element and 235 other tissues.
DR   ExpressionAtlas; Q91ZA6; baseline and differential.
DR   Genevisible; Q91ZA6; MM.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   CDD; cd10385; SH2_SOCS4; 1.
DR   CDD; cd03738; SOCS_SOCS4; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR028416; SOCS4.
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:SF21; PTHR10155:SF21; 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; SSF158235; SSF158235; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50225; SOCS; 1.
PE   2: Evidence at transcript level;
KW   Growth regulation; Reference proteome; SH2 domain;
KW   Signal transduction inhibitor; Ubl conjugation pathway.
FT   CHAIN           1..436
FT                   /note="Suppressor of cytokine signaling 4"
FT                   /id="PRO_0000181248"
FT   DOMAIN          283..378
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          373..422
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        12
FT                   /note="R -> W (in Ref. 1; AAL03942 and 3; AAI17815)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   436 AA;  49918 MW;  B64BF54C75F27A21 CRC64;
     MAENNSKNVD VRPKTSRSRS ADRKDGYVWS GKKLSWSKKS ESCSESEAIG TVENVEIPLR
     SQERQLSCSS IELDLDHSCG HRFLGRSLKQ KLQDAVGQCF PIKNCSGRHS PGLPSKRKIH
     ISELMLDKCP FPPRSDLAFR WHFIKRHTVP MSPNSDEWVS ADLSERKLRD AQLKRRNTED
     DIPCFSHTNG QPCVITANSA SCTGGHITGS MMNLVTNNSI EDSDMDSEDE IITLCTSSRK
     RNKPRWEMEE EILQLEAPPK FHTQIDYVHC LVPDLLQISN NPCYWGVMDK YAAEALLEGK
     PEGTFLLRDS AQEDYLFSVS FRRYSRSLHA RIEQWNHNFS FDAHDPCVFH SPDITGLLEH
     YKDPSACMFF EPLLSTPLIR TFPFSLQHIC RTVICNCTTY DGIDALPIPS PMKLYLKEYH
     YKSKVRLLRI DVPEQQ
 
 
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