SOCS6_PONAB
ID SOCS6_PONAB Reviewed; 535 AA.
AC Q5RCM6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Suppressor of cytokine signaling 6;
DE Short=SOCS-6;
GN Name=SOCS6;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. Regulates KIT degradation by ubiquitination of the tyrosine-
CC phosphorylated receptor (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RBCK1. Interacts with phosphorylated IRS4.
CC Interacts with KIT (phosphorylated). Interacts with PIM3 (By
CC 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}.
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DR EMBL; CR858244; CAH90481.1; -; mRNA.
DR RefSeq; NP_001125251.1; NM_001131779.1.
DR AlphaFoldDB; Q5RCM6; -.
DR SMR; Q5RCM6; -.
DR STRING; 9601.ENSPPYP00000010362; -.
DR PRIDE; Q5RCM6; -.
DR Ensembl; ENSPPYT00000010774; ENSPPYP00000010362; ENSPPYG00000009234.
DR GeneID; 100172146; -.
DR KEGG; pon:100172146; -.
DR CTD; 9306; -.
DR eggNOG; KOG4566; Eukaryota.
DR GeneTree; ENSGT00940000154847; -.
DR HOGENOM; CLU_038160_0_0_1; -.
DR InParanoid; Q5RCM6; -.
DR OMA; FHEEESQ; -.
DR OrthoDB; 924518at2759; -.
DR TreeFam; TF321368; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Chromosome 18.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:InterPro.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; 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:0050868; P:negative regulation of T cell activation; IEA:Ensembl.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR CDD; cd10387; SH2_SOCS6; 1.
DR CDD; cd03740; SOCS_SOCS6; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR028421; SOCS6.
DR InterPro; IPR035865; SOCS6_SH2.
DR InterPro; IPR037345; SOCS6_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR10155:SF17; PTHR10155:SF17; 1.
DR Pfam; PF00017; SH2; 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..535
FT /note="Suppressor of cytokine signaling 6"
FT /id="PRO_0000285849"
FT DOMAIN 384..491
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 486..535
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 80..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 59535 MW; 72376BCF9CE4F362 CRC64;
MKKISLKTLR KSFNLNKSKE ETDFMVVQQP SLASDFGKDD SLFGSCYGKD MASCDINGED
EKGGKNRSKS ESLMGTLKRR LSAKQKSKGK AGTPSGSSAD EDTFSSSSAP IVFKDVRAQR
PIRSTSLRSH HYSPTPWPLR PTNSEETCIK MEVRVKALVH SSSPSPALNG VRKDFHDLQS
ETACQEQANS LKSSASHNGD LHLHLDEHVP VVIGLMPQDY IQYTVPLDEG MYPLEGSRSY
CLDSSSPMEV SAVPPQVGGR SFPEDESQVD QDLVVAPEIF VDQSVNGLLI GTTGVMLQSP
RAGQDDVPPL SPLLPPMQNN QIQRNFSGLT GTEAHVAESM RCHLNFDPNS APGVARVYDS
VQSSGPMVVT SLTEELKKLA KQGWYWGPIT RWEAEGKLAN VPDGSFLVRD SSDDRYLLSL
SFRSHGKTLH TRIEHSNGRF SFYEQPDVEG HTSIVDLIEH SIRDSENGAF CYSRSRLPGS
ATYPVRLTNP VSRFMQVRSL QYLCRFVIRQ YTRIDLIQKL PLPNKMKDYL QEKHY