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Database: UniProt
Entry: A0A3Q1J9V9_ANATE
LinkDB: A0A3Q1J9V9_ANATE
Original site: A0A3Q1J9V9_ANATE 
ID   A0A3Q1J9V9_ANATE        Unreviewed;       544 AA.
AC   A0A3Q1J9V9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   08-OCT-2025, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSATEP00000031712.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000031712.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000031712.2, ECO:0000313|Proteomes:UP000265040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Wellcome Sanger Institute Data Sharing;
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSATEP00000031712.2}
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   RefSeq; XP_026222589.1; XM_026366804.1.
DR   RefSeq; XP_026222595.1; XM_026366810.1.
DR   AlphaFoldDB; A0A3Q1J9V9; -.
DR   STRING; 64144.ENSATEP00000031712; -.
DR   Ensembl; ENSATET00000032179.3; ENSATEP00000031712.2; ENSATEG00000021848.3.
DR   Ensembl; ENSATET00000079365.1; ENSATEP00000075203.1; ENSATEG00000021848.3.
DR   GeneID; 113166695; -.
DR   CTD; 100003691; -.
DR   GeneTree; ENSGT00940000164285; -.
DR   InParanoid; A0A3Q1J9V9; -.
DR   OrthoDB; 8820570at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000265040; Chromosome 13.
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:UP000265040};
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          392..487
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          482..531
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..365
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"
FT   COMPBIAS        25..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..47
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  60783 MW;  001CC6F4DE976FD1 CRC64;
     MSLPKESGNR GKDRERGARP KVRQSRSEER RDAGGGRKGG KEKKKGLASH EPAAERPVSD
     GFEYGELLSD LESRDQSSSS LKESWRWQGL EVAASLLGQE RVTTKPGLGT AGSVSDLSAP
     SEGDCRGSSS SRTLRQKIQD AMGQCFPIKT HSAAAPPSPP QALSSSTACA SSKRKILLSE
     LMLDDCPFPV GSELAQKWYL IKQHTAPITQ PPTLDSAVVC SPPKSAMATV VEDVDDRLRE
     RRRISIEQGV EPPPNAEIHT FEVTAQINPL YKHGPKLAHG MNELAGTDRA SVHQQQQLLL
     QRQQQHQLLL QSCLDTLDEV VASASASASV HTCDTISDPL VDPEATATNM PSRTTLPQTE
     HQKSHDGYRI HTQIDYIHCL VPDLLQITNL PCYWGVMDRY EAETLLEGKP EGTFLLRDSA
     QEDYLFSVSF RRYGRSLHAR IEQWNHNFSF DVHDPSVFHA PTVTGLLEHY KDPNSCMFFE
     PLLSNPIHRT QPFSLQHICR AVISSCTTYD GINMLPIPNA LKKHLKEYHY KQRVRVRRMD
     TWWE
//
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