ID A0A5A9PAL9_9TELE Unreviewed; 564 AA.
AC A0A5A9PAL9;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 18.
DE SubName: Full=Suppressor of cytokine signaling 5 {ECO:0000313|EMBL:KAA0717687.1};
GN ORFNames=E1301_Tti014536 {ECO:0000313|EMBL:KAA0717687.1};
OS Triplophysa tibetana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0717687.1, ECO:0000313|Proteomes:UP000324632};
RN [1] {ECO:0000313|EMBL:KAA0717687.1, ECO:0000313|Proteomes:UP000324632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0717687.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA0717687.1};
RX PubMed=30977968;
RA Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA Wang W., Yang R.;
RT "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT to the harsh high-altitude environment of the Tibetan Plateau.";
RL Mol. Ecol. Resour. 19:1027-1036(2019).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA0717687.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SOYY01000008; KAA0717687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A9PAL9; -.
DR OrthoDB; 8820570at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000324632; Chromosome 8.
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:UP000324632};
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 408..503
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 498..547
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 43..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 62556 MW; 5197BBCE5DBD2938 CRC64;
MEKVGKMWGN LRNRCQALFH TDGSESNLCS QDVNRVLCVV DSRRGARASE PSGTRSSTPS
RSLSPLPVAT GGRRGHNCVA DIPQIVEISI DKDSEDARRG PHVRRDSYSR HAPWGGKKKH
SCSTKTQSSL EADSRTGRSR GSTARRERRY GISSIQEIND SVGAGSSGRS LSARSLRKRL
KDTVGLCLPL PTHHRSQSAR GPVSSKRKIH LTELMLETCP FPPGSDLANK WHLIKQHTAP
VSPHSSTALL DAFDSAHPSP EDEEERLRER RRLSIEEGVD PPPNAQIHTL EAASQSSSVY
KLGPKMAPGV GEGIGEGRSM GTVSSISGGL SGIAAQVAAS MSTPAHSVDC DSEEDSTTLC
LQTRRPKQRH ASGDAHCSRQ QGPWKVHTQI DYIHCLVPDL QAITALPCYW GVMDRYQAEA
LLDGRPEGTF LLRDSAQEDY LFSVSFRRYN RSLHARIEQW NHNFSFDAHD PCVFHSSTVT
GLLEHYKDPS ACMFFEPLLT APLHRTFPFS LQHLARAAIC RQTTYDGIGA LPLPPTMQDF
LKEYHYKQKV RVRWLEREPP LKVK
//
