ID A0A9J7Y4V2_CYPCA Unreviewed; 526 AA.
AC A0A9J7Y4V2;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=Suppressor of cytokine signaling 5a {ECO:0000313|Ensembl:ENSCCRP00000113798.1};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000113798.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000113798.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR AlphaFoldDB; A0A9J7Y4V2; -.
DR Ensembl; ENSCCRT00000125954.1; ENSCCRP00000113798.1; ENSCCRG00000061434.1.
DR Ensembl; ENSCCRT00000143915.1; ENSCCRP00000166255.1; ENSCCRG00000061434.1.
DR Ensembl; ENSCCRT00000161119.1; ENSCCRP00000149677.1; ENSCCRG00000061434.1.
DR Ensembl; ENSCCRT00000164235.1; ENSCCRP00000155700.1; ENSCCRG00000061434.1.
DR Ensembl; ENSCCRT00000202042.1; ENSCCRP00000169884.1; ENSCCRG00000061434.1.
DR GeneTree; ENSGT00940000164285; -.
DR Proteomes; UP001108240; 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 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:UP001108240};
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 371..466
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 461..510
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 99..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 58361 MW; 90F63486598143A0 CRC64;
MEKVGKVWSN LKKGCQSLLH TDGGSRIETP PQLQPQTDTV CQSVNKAQGD NTLEASSPSS
SVATLPLVAW RTGGSVTRHN CVVDAPQILE ITVEQDTEDA RAPLGARRDS YSRHAPWSGK
KRHSCSTKAQ SSLETTDRRS GRSRRRHGTG SSREELESGG TRSLRQQIHD TVGLCLPLRS
SSRNSHLPPP KRKIQITELM LETCPFAPGS DLARKWHLIK QHTAPVTVTP VDSSSDASGA
TCASPEDEEE RLRERRRLSI EEGVDPPPDA QIHTVEAITA PLASLYKLGP KLAPGMGEAQ
GDSLGATAAN CDSEDDDTTT LCLQARRPKQ RHGSAEGHLS SKQQGPWKVH TQIDYIHCLV
PDLLQITALS CYWGVMDRYE AEALLDGRPE GTFLLRDSAQ EDYLFSVSFR RYGRSLHARI
EQWNHNFSFD AHDPCVFHAA TVTALLEHYK DPSACMFFEP LLTVPLHRTF PFGLQSLARS
AICNGITYDG IGALPLPPAL QEHLREYHYK QRVRVRWLER EPVKAK
//