ID A0A6I9PZT7_9TELE Unreviewed; 561 AA.
AC A0A6I9PZT7;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Suppressor of cytokine signaling 5b {ECO:0000313|RefSeq:XP_010793715.1};
GN Name=socs5b {ECO:0000313|RefSeq:XP_010793715.1};
OS Notothenia coriiceps (black rockcod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Notothenia.
OX NCBI_TaxID=8208 {ECO:0000313|Proteomes:UP000504611, ECO:0000313|RefSeq:XP_010793715.1};
RN [1] {ECO:0000313|RefSeq:XP_010793715.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_010793715.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR RefSeq; XP_010793715.1; XM_010795413.1.
DR AlphaFoldDB; A0A6I9PZT7; -.
DR KEGG; ncc:104966231; -.
DR CTD; 559639; -.
DR OrthoDB; 8820570at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000504611; 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: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:UP000504611};
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 405..500
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 495..544
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 91..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..329
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 61953 MW; 5BE75B11BC404F63 CRC64;
MKKVGNMWSN LKSRCQTLFH NNSSGPSESR LEADGVHCVV ELGGSSGEAE ASGSSSPSRS
LLPVPMVTAG RRHHNCVSDI PQIVEITIDK DSEDVRGGSG GVPLARRDSY SRHAPWGGKK
KHSCSTKTQS SLETDRRSGR LRGSGSRRDR RYGVSSIQEM SDSVSGGRSL NARSLRQRLS
DTVGLCLPLP ARRRPRSSKN PVTSKRKIHL TELMLETCPF PPGSDLAHKW HLIKQHTAPV
SPHSSTALLD AFDPAHPSPE DEEERLRERR RLSIEEGVDP PPNAQIHTLE ASVPGSSLYK
LGPKLAPCTA EASGEGRASG AGSSTGAGSS GACAQVLGAA VSAQDCDSEE DSTTLCLQAR
RPKQRHASGD GHLSRQQPGP WKVHTQIDYI HCLVPDLMQI TALPCYWGVM DRYEAEALLD
GRPEGTFLLR DSAQEDYLFS VSFRRYNRSL HARIEQWNHN FSFDAHDPCV FHSSTVTGLL
EHYKDPSACM FFEPLLTAPL HRTFPFGLQH LARAAICRWT TYDGIGSLPL PPALQDFLKE
YHYKQKVRVR WLEREPQLKV K
//
