ID   ASB5_RABIT              Reviewed;         329 AA.
AC   Q862Z2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Ankyrin repeat and SOCS box protein 5;
DE            Short=ASB-5;
GN   Name=ASB5;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12593841; DOI=10.1016/s0006-291x(03)00095-0;
RA   Boengler K., Pipp F., Fernandez B., Richter A., Schaper W., Deindl E.;
RT   "The ankyrin repeat containing SOCS box protein 5: a novel protein
RT   associated with arteriogenesis.";
RL   Biochem. Biophys. Res. Commun. 302:17-22(2003).
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 (By similarity). May play a role in the
CC       initiation of arteriogenesis. {ECO:0000250,
CC       ECO:0000269|PubMed:12593841}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- TISSUE SPECIFICITY: Expressed in endothelial and smooth muscle cells of
CC       collateral arteries as well as in satellite cells.
CC       {ECO:0000269|PubMed:12593841}.
CC   -!- INDUCTION: Up-regulated in growing collateral arteries.
CC       {ECO:0000269|PubMed:12593841}.
CC   -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC       BC complex, an adapter module in different E3 ubiquitin-protein ligase
CC       complexes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family.
CC       {ECO:0000305}.
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DR   EMBL; AY165034; AAO39148.1; -; mRNA.
DR   RefSeq; NP_001156539.1; NM_001163067.1.
DR   AlphaFoldDB; Q862Z2; -.
DR   SMR; Q862Z2; -.
DR   STRING; 9986.ENSOCUP00000010841; -.
DR   GeneID; 100302410; -.
DR   KEGG; ocu:100302410; -.
DR   CTD; 140458; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   InParanoid; Q862Z2; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd03724; SOCS_ASB5; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037328; ASB5_SOCS.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF07525; SOCS_box; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00969; SOCS_box; 1.
DR   SUPFAM; SSF158235; SSF158235; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50225; SOCS; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..329
FT                   /note="Ankyrin repeat and SOCS box protein 5"
FT                   /id="PRO_0000066932"
FT   REPEAT          69..98
FT                   /note="ANK 1"
FT   REPEAT          102..131
FT                   /note="ANK 2"
FT   REPEAT          135..164
FT                   /note="ANK 3"
FT   REPEAT          167..196
FT                   /note="ANK 4"
FT   REPEAT          200..229
FT                   /note="ANK 5"
FT   REPEAT          232..261
FT                   /note="ANK 6"
FT   DOMAIN          278..329
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
SQ   SEQUENCE   329 AA;  36447 MW;  74A747A7A7303A3F CRC64;
     MSVLEESRPF AQQLFNVYFT ILSLFCFKLF VKISLAILSH FYIVKGNRKE AARIAAEFYG
     VTQGQGSWAD RSPLHEAASQ GRLLALRTLL SQGYNVNAVT IDHITPLHEA CLGDHVACAR
     TLLEAGANVN AITIDGVTPL FNACSQGSTS CTELLLEYGA KAQLESCLPS PTHEAASKGH
     HEFLDLLISW GIDVDQDIPH LGTPLYVACM SQQFHCIWKL LYAGADVQKG KYWDTPLHAA
     AQQSSTEIVN LLIEFGADIN AKNTELLRPV DVATTSSMVE RILLQHEATP SSLCQLCRLC
     IRNYIGRPRL HLIPQLQLPT LLQNFLQYR