GenomeNet

Database: UniProt
Entry: A0A6A5EPS1_PERFL
LinkDB: A0A6A5EPS1_PERFL
Original site: A0A6A5EPS1_PERFL 
ID   A0A6A5EPS1_PERFL        Unreviewed;       555 AA.
AC   A0A6A5EPS1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   02-APR-2025, entry version 14.
DE   RecName: Full=Suppressor of cytokine signaling 5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PFLUV_G00226350 {ECO:0000313|EMBL:KAF1376032.1};
OS   Perca fluviatilis (European perch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX   NCBI_TaxID=8168 {ECO:0000313|EMBL:KAF1376032.1, ECO:0000313|Proteomes:UP000465112};
RN   [1] {ECO:0000313|EMBL:KAF1376032.1, ECO:0000313|Proteomes:UP000465112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:KAF1376032.1};
RA   Roques C., Zahm M., Cabau C., Klopp C., Bouchez O., Donnadieu C., Kuhl H.,
RA   Gislard M., Guendouz S., Journot L., Haffray P., Bestin A., Morvezen R.,
RA   Feron R., Wen M., Jouanno E., Herpin A., Schartl M., Postlethwait J.,
RA   Schaerlinger B., Chardard D., Lecocq T., Poncet C., Jaffrelo L.,
RA   Lampietro C., Guiguen Y.;
RT   "A chromosome-scale genome assembly of the European perch, Perca
RT   fluviatilis.";
RL   Submitted (JUN-2019) 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:KAF1376032.1}.
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DR   EMBL; VHII01000019; KAF1376032.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6A5EPS1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000465112; Chromosome 19.
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:SF15; SUPPRESSOR OF CYTOKINE SIGNALING 5; 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:UP000465112};
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          399..494
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          489..538
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          38..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..325
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  61171 MW;  869EE019F1443ED5 CRC64;
     MWSNLKSKCQ TLFHNNGSSE SRVEANAVHC VVDLGQGGSS GEAQAPGASS PSRSLLPVPM
     APAGRRHHNC VSDSPQIVEI TIDKDTEDVR GRSGGVPLAR RDSYSRHAPW GGKKKHSCST
     KTQSSLEADR RSGRLRGSGN RRDRRYGVSS IQEMSDSVSG GRSLTARSLR QRLSDTVGLC
     LPLPARRRSR SSKNPVMSKR KIHLTELMLE TCPFPPGSDL AHKWHLIKQH TAPVSPHSST
     ALLDAFDPAQ PSPEDEEERL RERRRLSIEE GVDPPPNAQI HTLEASVPGS SLHKLGPKMA
     PGMGEASGEG RASGAGSSAG AGSSGACGQV LGAAASAQDC DSEEDSTTLC LQARRPKQRH
     ASGDGHLSRQ QPGPWKVHTQ IDYIHCLVPD LLQITALPCY WGVMDRYEAE ALLDGRPEGT
     FLLRDSAQED YLFSVSFRRY NRSLHARIEQ WNHNFSFDAH DPCVFHSSTV TGLLEHYKDP
     SACMFFEPLL TAPLHRTFPF GLQHLARAAI CRWTTYDGIG SLPLPPALQD FLKEYHYKQK
     VRVRWLEREP PFKVK
//
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