GenomeNet

Database: UniProt
Entry: M3Z7E3_MUSPF
LinkDB: M3Z7E3_MUSPF
Original site: M3Z7E3_MUSPF 
ID   M3Z7E3_MUSPF            Unreviewed;       441 AA.
AC   M3Z7E3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   28-JAN-2026, entry version 75.
DE   SubName: Full=Suppressor of cytokine signaling 4 {ECO:0000313|Ensembl:ENSMPUP00000019506.1, ECO:0000313|RefSeq:XP_004738877.1};
GN   Name=SOCS4 {ECO:0000313|Ensembl:ENSMPUP00000019506.1,
GN   ECO:0000313|RefSeq:XP_004738877.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000019506.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000019506.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2024) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_004738877.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004738877.1};
RG   RefSeq;
RL   Submitted (APR-2025) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; AEYP01003656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004738877.1; XM_004738820.3.
DR   AlphaFoldDB; M3Z7E3; -.
DR   STRING; 9669.ENSMPUP00000019506; -.
DR   Ensembl; ENSMPUT00000019786.1; ENSMPUP00000019506.1; ENSMPUG00000019634.1.
DR   GeneID; 101673021; -.
DR   KEGG; mpuf:101673021; -.
DR   CTD; 122809; -.
DR   eggNOG; KOG4566; Eukaryota.
DR   GeneTree; ENSGT00940000161456; -.
DR   HOGENOM; CLU_035609_0_0_1; -.
DR   OMA; RINNNPC; -.
DR   OrthoDB; 8820570at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000715; 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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd10385; SH2_SOCS4; 1.
DR   CDD; cd03738; SOCS_SOCS4; 1.
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; IPR035864; SOCS4_SH2.
DR   InterPro; IPR037342; SOCS4_SOCS.
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:UP000000715};
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          288..383
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          378..427
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   COMPBIAS        1..10
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  50402 MW;  D024860194D6A092 CRC64;
     MAENSESISK NVDVRPKTSR SRSADRKDGY VWSGKKLSWS KKNESCSDAE TVNAVEKTEV
     PLRSQERKHS CSSIELDLDH SCGHRFLGRS LKQKLQDAVG QCFPIKNCSG RHSSGLPSKR
     KIHISELMLD KCPFPPRSDL AFRWHFIKRH TAPINSKSSE WVSTDSSQSE LRDGQLKQRR
     NVEEEVNCFS QTNVQPCVIT TNSASSCRGG PMTGSVMNLL SNNSIEDSDM DSDDEIITLC
     TSSRKRNKPK WEMDEEILQL ETPPKYHTQI DYVHCLVPDL LQINNNPCYW GVMDKYAAEA
     LLEGKPEGTF LLRDSAQEDY LFSVSFRRYS RSLHARIEQW NHNFSFDAHD PCVFHSPDIT
     GLLEHYKDPS ACMFFEPLLS TPLIRTFPFS LQHICRTVIC NCTTYDGIDA LPIPSSMKLY
     LKEYHYKSKV RVLRIDAPEQ C
//
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