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Database: UniProt
Entry: A0AAY5EF03_ELEEL
LinkDB: A0AAY5EF03_ELEEL
Original site: A0AAY5EF03_ELEEL 
ID   A0AAY5EF03_ELEEL        Unreviewed;       484 AA.
AC   A0AAY5EF03;
DT   05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2025, sequence version 1.
DT   28-JAN-2026, entry version 5.
DE   RecName: Full=Suppressor of cytokine signaling 5b {ECO:0008006|Google:ProtNLM};
GN   Name=socs5a {ECO:0000313|Ensembl:ENSEEEP00000055581.1};
OS   Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC   Gymnotoidei; Gymnotidae; Electrophorus.
OX   NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000055581.1, ECO:0000313|Proteomes:UP000314983};
RN   [1] {ECO:0000313|Ensembl:ENSEEEP00000055581.1, ECO:0000313|Proteomes:UP000314983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Myers G., Meyer A., Fedrigo O., Formenti G., Rhie A., Tracey A., Sims Y.,
RA   Jarvis E.D.;
RT   "Electrophorus electricus (electric eel) genome, fEleEle1, primary
RT   haplotype.";
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSEEEP00000055581.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSEEEP00000055581.1}
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   AlphaFoldDB; A0AAY5EF03; -.
DR   Ensembl; ENSEEET00000036088.2; ENSEEEP00000055581.1; ENSEEEG00000016982.2.
DR   GeneTree; ENSGT00940000164285; -.
DR   Proteomes; UP000314983; Chromosome 14.
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   Gene3D; 3.30.505.10; SH2 domain; 2.
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   SMART; SM00252; SH2; 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:UP000314983};
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          366..435
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          432..468
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000259|PROSITE:PS50225"
FT   REGION          16..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  54381 MW;  1CF7DD0B3029A58B CRC64;
     MEKVGKVWSN LKKGCQSLLH PDRGSHGEMR PPTQTHPCCQ SVDQTQGENE REPASPSRSL
     SALPLVSRRV NGSKVRRGHN CVADVPQILE ITVEQEAEDG RGPLGTRRDS YSRHAPWSGK
     KRHSCSTKAQ SSLESTERRS GRSRRRHGAE DLESGVPRSL RQQFHDTMGL CLPLRSSTRG
     TQARPPKRKI QITELMLETC PFPPGSDLAR KWHLIKQHTA PVPSSMACSK DAPDAAHASP
     EDEEERLRER RRLSIEEGVD PPPDAQIHTV EAITAPLASI YKLGPKLAPG MGEAPGESRG
     ATATDCDSED DDTTMLCLQA RRPKQRHASL EGQAACKQPG PWKVHTQIDY IHCLVPDLLQ
     ITALPCYWGV MDRYEAEALL DGRPEGTFLL RDSAQEDYLF SVSFRRYGRS LHARIEQWNH
     NFSFDAHDPC VFHSLARAAI CRGTSYDGIA ALPLPQTLQD YLREYHYKQR VRVRWLEREP
     LKAK
//
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