ID   A0A3Q3N2A6_9TELE        Unreviewed;       545 AA.
AC   A0A3Q3N2A6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   28-JAN-2026, entry version 30.
DE   SubName: Full=Suppressor of cytokine signaling 9 {ECO:0000313|Ensembl:ENSMAMP00000026409.1};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000026409.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000026409.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSMAMP00000026409.1}
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_026154713.1; XM_026298928.1.
DR   AlphaFoldDB; A0A3Q3N2A6; -.
DR   STRING; 205130.ENSMAMP00000026409; -.
DR   Ensembl; ENSMAMT00000027085.2; ENSMAMP00000026409.1; ENSMAMG00000017742.2.
DR   GeneID; 113125459; -.
DR   CTD; 100003691; -.
DR   GeneTree; ENSGT00940000164285; -.
DR   InParanoid; A0A3Q3N2A6; -.
DR   OrthoDB; 8820570at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261640; 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: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:UP000261640};
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          393..488
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          483..532
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  60863 MW;  3C26FB7DBE404EA6 CRC64;
     MSLPKEPGNR GKDRERGARP KVRQSRSEER RDAGGNCKGG KGKKKGLASH DPASERPVSD
     GFEYGELLSD LETKDQSSSS PVKESWRWQG LDIGASLLGQ ERVITRPGLA AVGSACELSS
     HSEGDGRGSS SSSRTLRQKI QDAMGQCFPI KTHSPAAPAP PLQAFSSSAA CASRRKIHLS
     ELMLDDCPFP IGSELAQKWY LIKQHTAPIT KPPVLDSSVV CSAPTSAMAS VVEDVDDRLR
     ERRRISIEQG VEPPPNAEIH TFEVTAQINP LYKHGPKLAH GMNELAGADR ASVHQQQQLL
     IQRQQQHQLL LQSCLDTLDE VVASASASAS VHACDSISDT LVDPEVTANN LSSRTILPQT
     EHHKSHDGYR IHTQIDYIHC LVPDLLQITN LPCYWGVMDR YEAETLLEGK PEGTFLLRDS
     AQEDYLFSVS FRRYGRSLHA RIEQWNHNFS FDVHDPSVFH APTVTGLLEH YKDPNSCMFF
     EPLLSNPIHR THPFSLQHIC RAVISSCTTY DGINMLPIPN ALKKHLKEYH YKQRVRVRRM
     DTWWE
//