ID A0A3L8RVB5_CHLGU Unreviewed; 284 AA.
AC A0A3L8RVB5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Ankyrin repeat and SOCS box protein 8 {ECO:0000256|ARBA:ARBA00017640};
GN ORFNames=DV515_00015891 {ECO:0000313|EMBL:RLV86594.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV86594.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV86594.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV86594.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV86594.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- FUNCTION: May be a substrate-recognition component of a SCF-like ECS
CC (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex
CC which mediates the ubiquitination and subsequent proteasomal
CC degradation of target proteins. {ECO:0000256|ARBA:ARBA00003062}.
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:RLV86594.1}.
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DR EMBL; QUSF01000220; RLV86594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8RVB5; -.
DR STRING; 44316.ENSEGOP00005013373; -.
DR Ensembl; ENSEGOT00005015242; ENSEGOP00005013373; ENSEGOG00005010590.
DR OMA; LHCACMA; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd03727; SOCS_ASB8; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.750.20; SOCS box; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037332; ASB8_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR24193:SF121; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF158235; SOCS box-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50225; SOCS; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT REPEAT 48..80
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 81..112
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 113..145
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 146..178
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 231..284
FT /note="SOCS box"
FT /evidence="ECO:0000259|PROSITE:PS50225"
SQ SEQUENCE 284 AA; 31352 MW; BEEDB7195466E5C9 CRC64;
MWYIMQSIQS KYSLSERLIR TIAAIRSFPR DNVEDLIGRG ADVNCLHGTL KPLHCACMVA
DADCVELLLQ KGAEVNALDG YNRTALHYAA EKDETCVEIL LEYGANPNAL DGNKDTPLHW
AAFKNNAECV RALLANGALV NALDYNNDTP LSWAAMKGNL ESVSVLLDFG AEVRVVNLKG
QSPISRLVAL LVRGLGTERE DSCLDLLHRA TGHFELRKNG SLPWEVARDP QLCQRLTRLC
SAPGTLQALS RYAVRRSLGL RFLPQAVQQL PLPACLKDYL LLLT
//
