ID A0AA35K3U0_9SAUR Unreviewed; 532 AA.
AC A0AA35K3U0;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE SubName: Full=Suppressor of cytokine signaling 5 {ECO:0000313|EMBL:CAI5771140.1};
GN ORFNames=PODLI_1B031240 {ECO:0000313|EMBL:CAI5771140.1};
OS Podarcis lilfordi (Lilford's wall lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=74358 {ECO:0000313|EMBL:CAI5771140.1, ECO:0000313|Proteomes:UP001178461};
RN [1] {ECO:0000313|EMBL:CAI5771140.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T., Gomez Garrido J.;
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; OX395128; CAI5771140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA35K3U0; -.
DR Proteomes; UP001178461; Chromosome 3.
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:UP001178461};
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 377..472
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 467..516
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 112..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..150
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..165
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 60615 MW; CFB5C0BD92E69C51 CRC64;
MGKVGKMWNS FKYRCQNLFN SEGGNRSENV DVNSNCSSVR DKSVFVPDPA VQRPSSPLRD
VSLQLSLNPS RSSARKNQNC AAEIPQIVEI SIERESDLGV GTGARLARRD SYSRHAPWGG
KKKHSCSTKT QSSLDSDKRF GRSRLQRRER RYGVSSVHDT DSVSSRTIGS RSLRQRLQDT
VGLCFPMRTY CKPSKPLFSN KRKIHLSELM LEKCPFPPGS DLAQKWHLIK QHTAPVSPHS
TLFDAFDPSV ASTEDEEDRL RERRRLSIEE GVDPPPNAQI HTFEATAQVN PLYKLGPKLA
PGMSELTGDG SSTPQGSCDL EEDTTTLCLQ SRRQKQRQVS GESHSHTSRQ GAWKVHTQID
YIHCLVPDLL QITGNPCYWG VMDRYEAEAL LEGKPEGTFL LRDSAQEDYL FSVSFRRYNR
SLHARIEQWN HNFSFDAHDP CVFHSSTVTG LLEHYKDPSS CMFFEPLLTV SLNRTFPFSL
QYICRAVICR YTSYDGIDCL PLPSMLQDFL KEYHYKQKVR VRWLEREPIK AK
//
