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Database: UniProt
Entry: A0A498L996_LABRO
LinkDB: A0A498L996_LABRO
Original site: A0A498L996_LABRO 
ID   A0A498L996_LABRO        Unreviewed;       506 AA.
AC   A0A498L996;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   05-FEB-2025, entry version 17.
DE   SubName: Full=Suppressor of cytokine signaling 5-like protein {ECO:0000313|EMBL:RXN02457.1};
GN   ORFNames=ROHU_035876 {ECO:0000313|EMBL:RXN02457.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN02457.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN02457.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN02457.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN02457.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXN02457.1}.
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DR   EMBL; QBIY01013533; RXN02457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498L996; -.
DR   STRING; 84645.A0A498L996; -.
DR   OrthoDB; 8820570at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000290572; 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: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:UP000290572};
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          354..449
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          444..493
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          1..125
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        33..46
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  56496 MW;  3A3340C4232E25B7 CRC64;
     MSLPEDTGDR GKERERGARP KVRQSRSEER RDGGRRKGGR GKKKSHPSHD LTSERPVSDG
     FEYGDLLNGL QESSEAGSSS PLREHRRRQV LGSSERVSAR LSLGSPAADV GCDTESKASG
     SSRTLRQKIQ DAVGQCFPIK THSQGLSHSP STASTSSRRK IHLSELMLDS CPFPAGSDLA
     QKWYLIKQHT APISQAPVLD SGSTSAALVC AVTPVEDEED RLRERRRISI EQGVEPPPNA
     QIHTFEVTAQ INPLYKLGPK LAHGMNELAG DERATLHQLL LQSCLDTLDE VAASTTSSDF
     DLGAASPSTR SLTGATLVHP DSPKSQDGHH RIHTQIDYIH CLVPDLLQIT NLACYWGVMD
     RYQAETLLEG KPEGTFLLRD SAQEDYLFSV SFRRYGRSLH ARIEQWNHNF SFDVHDPSVF
     HAPTVTGLLE HYKDPNSCMF FEPLLSNPIH RSQPFSLQRI CRAVISSCTT YDGINALPLP
     NALKEHLKEY HYKQRVRIRR LDTWWE
//
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