ID A0A672QC94_SINGR Unreviewed; 593 AA.
AC A0A672QC94;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Suppressor of cytokine signaling 5-like {ECO:0000313|Ensembl:ENSSGRP00000073427.1};
GN Name=LOC107586485 {ECO:0000313|Ensembl:ENSSGRP00000073427.1};
OS Sinocyclocheilus grahami (Dianchi golden-line fish) (Barbus grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=75366 {ECO:0000313|Ensembl:ENSSGRP00000073427.1, ECO:0000313|Proteomes:UP000472262};
RN [1] {ECO:0000313|Ensembl:ENSSGRP00000073427.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSGRP00000073427.1}
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 RefSeq; XP_016129347.1; XM_016273861.1.
DR AlphaFoldDB; A0A672QC94; -.
DR Ensembl; ENSSGRT00000078188.1; ENSSGRP00000073427.1; ENSSGRG00000037384.1.
DR GeneID; 107586485; -.
DR KEGG; sgh:107586485; -.
DR InParanoid; A0A672QC94; -.
DR OMA; RAAICCW; -.
DR OrthoDB; 8820570at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000472262; 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:0007259; P:cell surface receptor signaling pathway via JAK-STAT; IEA:InterPro.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:InterPro.
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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd03739; SOCS_SOCS5; 1.
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; IPR037343; SOCS5_SOCS.
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:UP000472262};
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 437..532
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 527..576
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 122..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..202
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 66349 MW; 8BE47515E2DCA873 CRC64;
MWDSSESNSL QTKDGCEVIF TNKKGRCLHS MEKVGKMWGN LRSRCQALFH NDGSESHLCS
QDLDCVHCVV DLGRGAHAEL YETRSFTPSQ TLSPLPLVPV GRRGHNCVAD IPQIVEISID
KESEDARRGP HVRRDSYSRH APWGGKKKHS CSTKTQSSLE ADRRTGRSRG STARRERRYG
VSSIQEINDS VGAGSSGRSL STRSLRQRLR DTVGLCLPLP TQRRSQSAKG QVSSKRKIHL
TELMLETCPF PPGSDLANKW HLIKQHTAPV SPHSSTALLD AFDSAHPSPE DEEERLRERR
RLSIEEGVDP PPNAQIHTLE ATSQNSSLYK LGPKMAPGVG EGLSEGRSLG TISTISGGLS
GLAAQVAANM AVPSHTVDCD SEEDSTTLCL QTRRPKQRHA SGDTHCSRQP GPWKVHTQID
YIHCLVPDLQ AITALPCYWG VMDRYQAEAL LDGRPEGTFL LRDSAQEDYL FSVSFRRYNR
SLHARIEQWN HNFSFDAHDP CVFHSSTVTG LLEHYKDPSA CMFFEPLLTA PLHRTFPFSL
QHLARAAICR HTTYDGIGAL PLPPTMQDFL KEYHYKQKVR VRWLERETPL KVK
//