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Database: UniProt
Entry: A0A669DC23_ORENI
LinkDB: A0A669DC23_ORENI
Original site: A0A669DC23_ORENI 
ID   A0A669DC23_ORENI        Unreviewed;       541 AA.
AC   A0A669DC23;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 25.
DE   SubName: Full=Suppressor of cytokine signaling 9 {ECO:0000313|Ensembl:ENSONIP00000058177.1};
GN   Name=socs9 {ECO:0000313|Ensembl:ENSONIP00000058177.1};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000058177.1, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000058177.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSONIP00000058177.1}
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_003440161.2; XM_003440113.5.
DR   AlphaFoldDB; A0A669DC23; -.
DR   Ensembl; ENSONIT00000059831.1; ENSONIP00000058177.1; ENSONIG00000035585.1.
DR   GeneID; 100693056; -.
DR   KEGG; onl:100693056; -.
DR   CTD; 100003691; -.
DR   GeneTree; ENSGT00940000164285; -.
DR   InParanoid; A0A669DC23; -.
DR   OMA; SYRIHTQ; -.
DR   OrthoDB; 8820570at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000005207; Linkage group LG14.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10155:SF18; SUPPRESSOR OF CYTOKINE SIGNALING 9 ISOFORM X1; 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:UP000005207};
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          389..484
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          479..528
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..14
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..43
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  60426 MW;  4109B767DF7292DE CRC64;
     MDSGNRGKDR ERGARPKVRQ SRSEERRDAG GGRKGGKGKK KGLSSHDAAA ERPVSDGFEY
     GELLSELETR DQSSPSPLRD SWRWQGFEVA ASLLGQERVT AKPTLGATGS AAELPTSSEG
     EGRGSSSSRT LRQKIQDAMG QCFPIKTHTA AAPAPPPQAL SSSSACGSSR RKIHLSELML
     DDCPFPVGSE LAQKWYLIKQ HTAPITQPPL LDSTVVCTAP TSTMAAAVED VDDRLRERRR
     ISIEQGVEPP PNAEIHTFEV TAQINPLYKH GPKLAHGMND LAETDRSSIH QQQQLLLQRQ
     QQHQLLLQSC LDTLDEVAAS ASASASVHTC DAVSDALVDP DITATSMTSR AILPQTEHHK
     SHDSYRIHTQ IDYIHCLVPD LLQITNLPCY WGVMDRYEAE TLLEGKPEGT FLLRDSAQED
     YLFSVSFRRY GRSLHARIEQ WNHNFSFDVH DPSVFHAPTV TGLLEHYKDP NSCMFFEPLL
     SNPIHRTQPF SLQHICRAVI SSCTTYDGIN MLPIPNALKK HLKEYHYKQR VRVRRMDTWW
     E
//
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