ID   SPSB1_BOVIN             Reviewed;         273 AA.
AC   Q5E9X6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=SPRY domain-containing SOCS box protein 1;
DE            Short=SSB-1;
GN   Name=SPSB1; Synonyms=SSB1;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Substrate recognition component of a SCF-like ECS (Elongin
CC       BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which
CC       mediates the ubiquitination and subsequent proteasomal degradation of
CC       target proteins (By similarity). Negatively regulates nitric oxide (NO)
CC       production and limits cellular toxicity in activated macrophages by
CC       mediating the ubiquitination and proteasomal degradation of NOS2 (By
CC       similarity). Acts as a bridge which links NOS2 with the ECS E3
CC       ubiquitin ligase complex components ELOC and CUL5 (By similarity).
CC       {ECO:0000250|UniProtKB:Q96BD6}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the probable ECS(SPSB1) E3 ubiquitin-protein
CC       ligase complex which contains CUL5, RNF7/RBX2, Elongin BC complex and
CC       SPSB1 (By similarity). Interacts with CUL5, RNF7, ELOB and ELOC (By
CC       similarity). Directly interacts with MET tyrosine kinase domain in the
CC       presence and in the absence of HGF, however HGF treatment has a
CC       positive effect on this interaction (By similarity). When
CC       phosphorylated, interacts with RASA1 without affecting its stability
CC       (By similarity). Interacts (via B30.2/SPRY domain) with PAWR; this
CC       interaction is direct and occurs in association with the Elongin BC
CC       complex (By similarity). Interacts with NOS2 and EPHB2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q96BD6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q96BD6}. Note=Exhibits a diffuse cytosolic
CC       localization. {ECO:0000250|UniProtKB:Q96BD6}.
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 (By similarity). Essential for its ability to link NOS2 and
CC       the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96BD6}.
CC   -!- DOMAIN: The B30.2/SPRY domain is involved in MET and PAWR binding.
CC       {ECO:0000250|UniProtKB:Q96BD6}.
CC   -!- SIMILARITY: Belongs to the SPSB family. {ECO:0000305}.
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DR   EMBL; BT020794; AAX08811.1; -; mRNA.
DR   RefSeq; NP_001029381.1; NM_001034209.1.
DR   AlphaFoldDB; Q5E9X6; -.
DR   SMR; Q5E9X6; -.
DR   STRING; 9913.ENSBTAP00000034027; -.
DR   PaxDb; Q5E9X6; -.
DR   PRIDE; Q5E9X6; -.
DR   GeneID; 504407; -.
DR   KEGG; bta:504407; -.
DR   CTD; 80176; -.
DR   eggNOG; KOG3953; Eukaryota.
DR   InParanoid; Q5E9X6; -.
DR   OrthoDB; 938259at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR003877; SPRY_dom.
DR   Pfam; PF07525; SOCS_box; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00969; SOCS_box; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50225; SOCS; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..273
FT                   /note="SPRY domain-containing SOCS box protein 1"
FT                   /id="PRO_0000238471"
FT   DOMAIN          33..231
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          232..273
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT   MOD_RES         31
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BD6"
SQ   SEQUENCE   273 AA;  30811 MW;  603D5690A327B789 CRC64;
     MGQKVTGGIK TVDMRDPTYR PLKQELQGLD YCKPTRLDLL LDMPPVSYDV QLLHSWNNND
     RSLNVFVKED DKLIFHRHPV AQSTDAIRGK VGYTRGLHVW QITWAMRQRG THAVVGVATA
     DAPLHSVGYT TLVGNNHESW GWDLGRNRLY HDGKNQPSKT YPAFLEPDET FIVPDSFLVA
     LDMDDGTLSF IVDGQYMGVA FRGLKGKKLY PVVSAVWGHC EIRMRYLNGL DPEPLPLMDL
     CRRSVRLALG KGRLGEIHAL PLPASLKAYL LYQ