ID U3KKV7_FICAL Unreviewed; 436 AA.
AC U3KKV7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 28-JAN-2026, entry version 74.
DE SubName: Full=Suppressor of cytokine signaling 4 {ECO:0000313|Ensembl:ENSFALP00000015661.1};
GN Name=SOCS4 {ECO:0000313|Ensembl:ENSFALP00000015661.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000015661.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000015661.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000015661.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSFALP00000015661.1}
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 RefSeq; XP_005047826.1; XM_005047769.1.
DR AlphaFoldDB; U3KKV7; -.
DR STRING; 59894.ENSFALP00000015661; -.
DR Ensembl; ENSFALT00000015726.2; ENSFALP00000015661.1; ENSFALG00000015043.2.
DR GeneID; 101815072; -.
DR KEGG; fab:101815072; -.
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; UP000016665; Chromosome 5.
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:UP000016665};
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 282..377
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 372..421
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..201
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 49782 MW; 61A68EB4226D26FC CRC64;
MAENKDSSAK NADVRPKSSR SRSADRKDGY VWSGKKLSWS KKSEHCPDAE AASAAGRSGT
NLRSQERKYS CSSIELDLDR SCGHRFLGRS LKQKLQDAVG QCFPIKNCSS RHGSALPSKR
KIHISELMLD KCPFPPRSEL AFRWHLIKRH TAPISPKAEE WIIADLSQHE EREDQLRDEE
IANGGMDSPS QSCDFTDSSS SRGDPRPELV TGKVARSSRD ESDMDSDDEV ITLCTSSRKR
NKPKWETDDE LLRMETPPKY HTQIDYVHCL VPDLLQINNN PCYWGVMDKY AAEALLEGKP
EGTFLLRDSA QEDYLFSVSF RRYSRSLHAR IEQWNHNFSF DAHDPCVFHS PDITGLLEHY
KDPSSCMFFE PLLSTPLNRT FPFSLQHICR TVICNCTTYD GIDALPIPPS VKLYLKEYHY
KSKVRVLRID VPEQQS
//
