ID   WDR83_RAT               Reviewed;         315 AA.
AC   Q5BLX8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=WD repeat domain-containing protein 83;
DE   AltName: Full=Mitogen-activated protein kinase organizer 1;
DE            Short=MAPK organizer 1;
GN   Name=Wdr83; Synonyms=Morg1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH EGLN3.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=16407229; DOI=10.1074/jbc.m513751200;
RA   Hopfer U., Hopfer H., Jablonski K., Stahl R.A.K., Wolf G.;
RT   "The novel WD-repeat protein Morg1 acts as a molecular scaffold for
RT   hypoxia-inducible factor prolyl hydroxylase 3 (PHD3).";
RL   J. Biol. Chem. 281:8645-8655(2006).
CC   -!- FUNCTION: Molecular scaffold protein for various multimeric protein
CC       complexes. Acts as a module in the assembly of a multicomponent
CC       scaffold for the ERK pathway, linking ERK responses to specific
CC       agonists. At low concentrations it enhances ERK activation, whereas
CC       high concentrations lead to the inhibition of ERK activation (By
CC       similarity). Also involved in response to hypoxia by acting as a
CC       negative regulator of HIF1A/HIF-1-alpha via its interaction with
CC       EGLN3/PHD3. May promote degradation of HIF1A. May act by recruiting
CC       signaling complexes to a specific upstream activator. May also be
CC       involved in pre-mRNA splicing. {ECO:0000250,
CC       ECO:0000269|PubMed:16407229}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC       Interacts with ERK signaling proteins MAP2K1/MEK1, MAP2K2/MEK2,
CC       LAMTOR3, ARAF/Raf-1, MAPK1/ERK2 and MAPK3/ERK1 (By similarity).
CC       Interacts with EGLN3/PHD3. {ECO:0000250, ECO:0000269|PubMed:16407229}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16407229}. Nucleus
CC       {ECO:0000269|PubMed:16407229}. Note=Predominantly cytoplasmic.
CC       Partially nuclear.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis and brain. Expressed at
CC       intermediate level in heart, liver and kidney. Weakly expressed in
CC       spleen and lung and absent in muscle. {ECO:0000269|PubMed:16407229}.
CC   -!- SIMILARITY: Belongs to the WD repeat MORG1 family. {ECO:0000305}.
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DR   EMBL; AY940050; AAX23986.1; -; mRNA.
DR   RefSeq; NP_001041312.1; NM_001047847.1.
DR   AlphaFoldDB; Q5BLX8; -.
DR   SMR; Q5BLX8; -.
DR   BioGRID; 252752; 1.
DR   STRING; 10116.ENSRNOP00000005917; -.
DR   PaxDb; Q5BLX8; -.
DR   GeneID; 288924; -.
DR   KEGG; rno:288924; -.
DR   CTD; 84292; -.
DR   RGD; 1306947; Wdr83.
DR   eggNOG; KOG0316; Eukaryota.
DR   InParanoid; Q5BLX8; -.
DR   OrthoDB; 1090342at2759; -.
DR   PhylomeDB; Q5BLX8; -.
DR   Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR   PRO; PR:Q5BLX8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR   GO; GO:0090594; P:inflammatory response to wounding; ISO:RGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:RGD.
DR   GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR   GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR   GO; GO:0009611; P:response to wounding; ISO:RGD.
DR   GO; GO:0000375; P:RNA splicing, via transesterification reactions; ISO:RGD.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Repeat; Spliceosome; WD repeat.
FT   CHAIN           1..315
FT                   /note="WD repeat domain-containing protein 83"
FT                   /id="PRO_0000235265"
FT   REPEAT          23..62
FT                   /note="WD 1"
FT   REPEAT          65..104
FT                   /note="WD 2"
FT   REPEAT          107..146
FT                   /note="WD 3"
FT   REPEAT          151..188
FT                   /note="WD 4"
FT   REPEAT          190..228
FT                   /note="WD 5"
FT   REPEAT          231..272
FT                   /note="WD 6"
FT   REPEAT          275..313
FT                   /note="WD 7"
SQ   SEQUENCE   315 AA;  34382 MW;  C2F85DBEF658FD4B CRC64;
     MAFPEPKPRA PELPRKQLKT LDCGQGAVRA VRFNVDGNYC LTCGSDKTLK LWNPLRGTLL
     RTYSGHGYEV LDAAGSFDNS HLCSGGGDKT VVLWDVATGQ VVRKFRGHAG KVNTVQFNEE
     ATVILSGSID SSVRCWDCRS RKPEPVQTLD EARDGISSVK VSDHEILAGS VDGRVRRYDL
     RMGQVTSDYV GSPITCTCFS RDGQCTLISS LDSTLRLLDK DTGELLGEYV GHKNQKYKLD
     CCLSERDTHV VSCSEDGKVF FWDLVEGSLA LALPVGSNVV QSLAYHPADP CLLTAMGGSI
     QYWREETYEA EGGAG