SOCS5_BOVIN
ID SOCS5_BOVIN Reviewed; 536 AA.
AC Q29RN6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Suppressor of cytokine signaling 5;
DE Short=SOCS-5;
GN Name=SOCS5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: SOCS family proteins form part of a classical negative
CC feedback system that regulates cytokine signal transduction. May be a
CC substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-
CC SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins. Inhibits for instance EGF signaling by mediating the
CC degradation of the EGF receptor/EGFR. Involved in the regulation of T-
CC helper cell differentiation by inhibiting of the IL4 signaling pathway
CC which promotes differentiation into the Th2 phenotype. Can also
CC partially inhibit IL6 and LIF signaling (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with EGFR. Interacts with ELOB and ELOC; mediates
CC EGFR ubiquitination and degradation. Interacts with IL4R; inhibits IL4
CC signaling (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin ligase
CC complexes. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation is induced by EGF (By similarity).
CC {ECO:0000250}.
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DR EMBL; BC114096; AAI14097.1; -; mRNA.
DR RefSeq; NP_001039647.1; NM_001046182.1.
DR AlphaFoldDB; Q29RN6; -.
DR BMRB; Q29RN6; -.
DR SMR; Q29RN6; -.
DR STRING; 9913.ENSBTAP00000011826; -.
DR PaxDb; Q29RN6; -.
DR PRIDE; Q29RN6; -.
DR GeneID; 514773; -.
DR KEGG; bta:514773; -.
DR CTD; 9655; -.
DR eggNOG; KOG4566; Eukaryota.
DR InParanoid; Q29RN6; -.
DR OrthoDB; 722019at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
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:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
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 GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR CDD; cd03739; SOCS_SOCS5; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR022252; SOCS4/SOCS5_dom.
DR InterPro; IPR028420; SOCS5.
DR InterPro; IPR037343; SOCS5_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR10155:SF15; PTHR10155:SF15; 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; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW Growth regulation; Reference proteome; SH2 domain;
KW Signal transduction inhibitor; Ubl conjugation pathway.
FT CHAIN 1..536
FT /note="Suppressor of cytokine signaling 5"
FT /id="PRO_0000244382"
FT DOMAIN 381..476
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 471..520
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 1..50
FT /note="Required for interaction with IL4R"
FT /evidence="ECO:0000250"
FT REGION 115..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 61172 MW; 64AEAFB80EE6BB71 CRC64;
MDKVGKMWNN FKYRCQNLFG HEGGSRSENV DMNSNRCLSV KKKNISLGDS APQQQSSPLR
ENVALQLGLS PSKNSSRRNQ NCAAEIPQIV EISIEKDNDS CVTPGTRLAR RDSYSRHAPW
GGKKKHSCST KTQSSLDTDK KFGRTRSGLQ RRERRYGVSS VHDMDSVSSR TVGSRSLRQR
LQDTVGLCFP MRTYSKQSKP LFSNKRKIHL SELMLEKCPF PAGSDLAQKW HLIKQHTAPV
SPHSTFFDTF DPSLVSTEDE EDRLRERRRL SIEEGVDPPP NAQIHTFEAT AQVNPLYKLG
PKLAPGMTEV NGDSCAVPQA NCDSEEDTTT LCLQSRRQKQ RQVSGDSHAH VSRQGAWKVH
TQIDYIHCLV PDLLQITGNP CYWGVMDRYE AEALLEGKPE GTFLLRDSAQ EDYLFSVSFR
RYNRSLHARI EQWNHNFSFD AHDPCVFHSS TVTGLLEHYK DPSSCMFFEP LLTISLNRTF
PFSLQYICRA VICRCTTYDG IDGLPLPSML QDFLKEYHYK QKVRVRWLER EPVKAK