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Database: UniProt
Entry: U6CQX2_NEOVI
LinkDB: U6CQX2_NEOVI
Original site: U6CQX2_NEOVI 
ID   U6CQX2_NEOVI            Unreviewed;       441 AA.
AC   U6CQX2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   28-JAN-2026, entry version 59.
DE   SubName: Full=Suppressor of cytokine signaling 4 {ECO:0000313|EMBL:CCP73045.1, ECO:0000313|Ensembl:ENSNVIP00000004961.1};
GN   Name=SOCS4 {ECO:0000313|EMBL:CCP73045.1,
GN   ECO:0000313|Ensembl:ENSNVIP00000004961.1};
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Neogale.
OX   NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP73045.1};
RN   [1] {ECO:0000313|EMBL:CCP73045.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pool of brain {ECO:0000313|EMBL:CCP73045.1};
RA   Anistoroaei R., Christensen K.;
RT   "An American mink transcriptome.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNVIP00000004961.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-2025) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; HAAF01001219; CCP73045.1; -; mRNA.
DR   RefSeq; XP_044085812.1; XM_044229877.1.
DR   AlphaFoldDB; U6CQX2; -.
DR   Ensembl; ENSNVIT00000005855.1; ENSNVIP00000004961.1; ENSNVIG00000004005.1.
DR   GeneID; 122893081; -.
DR   KEGG; nvs:122893081; -.
DR   CTD; 122809; -.
DR   GeneTree; ENSGT00940000161456; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000694425; 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   2: Evidence at transcript level;
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694425};
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;  50343 MW;  AE1BC8EECBAABA93 CRC64;
     MAENSESISK NVDVRPKTSR SRSADRKDGY VWSGKKLSWS KKSESCSDAE TVNAVEKTEV
     PLRSQERKHS CSSIELDLDH SCGHRFLGRS LKQKLQDAVG QCFPIKNCSG RHSSGLPSKR
     KIHISELMLD KCPFPPRSDL AFRWHFIKRH TAPINSKSSE WVSTDSSQSE LRDGQLKQRR
     NVEEEVNCFS QTNVQPCVIT TNSASSCRGG PVTGSVMNLL 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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