ID M7C574_CHEMY Unreviewed; 541 AA.
AC M7C574;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Suppressor of cytokine signaling 6 {ECO:0000313|EMBL:EMP35652.1};
GN ORFNames=UY3_07184 {ECO:0000313|EMBL:EMP35652.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP35652.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KB528134; EMP35652.1; -; Genomic_DNA.
DR AlphaFoldDB; M7C574; -.
DR STRING; 8469.M7C574; -.
DR eggNOG; KOG4566; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040008; P:regulation of growth; IEA:InterPro.
DR CDD; cd10387; SH2_SOCS6; 1.
DR CDD; cd03740; SOCS_SOCS6; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.750.20; SOCS box; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
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; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10155:SF28; SUPPRESSOR OF CYTOKINE SIGNALING 6; 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; 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:UP000031443};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 390..497
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 492..541
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
FT REGION 86..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 60647 MW; 76AD1C211D78D0D1 CRC64;
MKKISLKTIR KSFNLNKSKE ESDFVVVQQP SLWFQQPSLS EFGKDDSLFG SCYGKDLASC
EVNSEDEKGG KNRSKSESLM GTLKRRLSAK QKQKGKGSTP SVSSADDDTF SSSSAPITFK
DVRAQRPLRS TSLRNHHYSP TPWPLRSTNS EETCIKMEVK VKALVHSSNP SPALNGVRKD
FHDLQSDSVF QEQNNTLKST ESQNGDLHLH IDEHVPVVIG LMPQDYIQYT VPLDEGMYPL
EGSRSYCLDS SSPMEVSTVS SQVGGNAFHE DEGQVDQDVV VAPDIFVDQP VNGLLIGTTG
VMLQSPRVNH SDVPPLSPLL PPMQNNQIQR NFNGLNGTDA HVAESMRCHL NFDPNSAPGV
GRVYDSVQNS GPMVVTSLTE ELKKLAKQGW YWGPITRWEA EGKLANVPDG SFLVRDSSDD
RYLLSLSFRS HGKTLHTRIE HSNGRFSFYE QPDVEGHTSI VDLIEHSIRD SENGAFCYSR
SRLPGSATYP VRLTNPVSRF MQVRSLQYLC RFVIRQYTRI DLIQKLPLPN KMKDYLQEKH
Y
//