GenomeNet

Database: UniProt
Entry: A0A091SIR3_PELCR
LinkDB: A0A091SIR3_PELCR
Original site: A0A091SIR3_PELCR 
ID   A0A091SIR3_PELCR        Unreviewed;       436 AA.
AC   A0A091SIR3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-OCT-2025, entry version 49.
DE   SubName: Full=Suppressor of cytokine signaling 4 {ECO:0000313|EMBL:KFQ58522.1};
GN   ORFNames=N334_06548 {ECO:0000313|EMBL:KFQ58522.1};
OS   Pelecanus crispus (Dalmatian pelican).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Pelecaniformes;
OC   Pelecanidae; Pelecanus.
OX   NCBI_TaxID=36300 {ECO:0000313|EMBL:KFQ58522.1, ECO:0000313|Proteomes:UP000054150};
RN   [1] {ECO:0000313|EMBL:KFQ58522.1, ECO:0000313|Proteomes:UP000054150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N334 {ECO:0000313|EMBL:KFQ58522.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK474357; KFQ58522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091SIR3; -.
DR   KEGG; pcri:104039047; -.
DR   OrthoDB; 8820570at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000054150; Unassembled WGS sequence.
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:UP000054150};
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..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..207
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        185..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  49836 MW;  8180E1C600775276 CRC64;
     MAEKKDSNIK NADVRPKSSR SRSADRKDGY VWSGKKLSWS KKSEQCSDAE TANAAGRSGT
     NLRSQERKYS CSSIELDLDR SCGHRFLGRS LKQKLQDAVG QCFPIKNCSS RLTSGLPSKR
     KIHISELMLD KCPFPPRSEL AFRWHLIKRH TAPISPKAED WIIADLSQRE EREDQLRDDE
     IANGGTDSPS QSCDFTDGGS CRSDSRSELV TGKVVRSSKD ESDMDSDDEV ITLCTSSRKR
     NKPKWETDDE LLRMETPPKY HTQIDYVHCL VPDLLQINNN PCYWGVMDKY AAEALLEGKP
     EGTFLLRDSA QEDYLFSVSF RRYSRSLHAR IEQWNHNFSF DAHDPCVFHS PDITGLLEHY
     KDPSSCMFFE PLLSTPLNRT FPFSLQHICR TVICNCTTYD GIDALPIPPS VKLYLKEYHY
     KSKVRVLRID VPEQQS
//
DBGET integrated database retrieval system