WDR83_MOUSE
ID WDR83_MOUSE Reviewed; 315 AA.
AC Q9DAJ4; Q505C2; Q8VEB7; Q99JX9; Q9D235;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH MAP2K1; MAP2K2; LAMTOR3; ARAF; MAPK1 AND MAPK3.
RC TISSUE=Brain;
RX PubMed=15118098; DOI=10.1073/pnas.0305894101;
RA Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
RA Bissonette E.A., Weber M.J.;
RT "Modular construction of a signaling scaffold: MORG1 interacts with
RT components of the ERK cascade and links ERK signaling to specific
RT agonists.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Mammary gland, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Molecular scaffold protein for various multimeric protein
CC complexes. Involved in response to hypoxia by acting as a negative
CC regulator of HIF1A/HIF-1-alpha via its interaction with EGLN3/PHD3. May
CC promote degradation of HIF1A. May act by recruiting signaling complexes
CC to a specific upstream activator (By similarity). Also acts as a module
CC in the assembly of a multicomponent scaffold for the ERK pathway,
CC linking ERK responses to specific agonists. At low concentrations it
CC enhances ERK activation, whereas high concentrations lead to the
CC inhibition of ERK activation. May also be involved in pre-mRNA
CC splicing. {ECO:0000250, ECO:0000269|PubMed:15118098}.
CC -!- SUBUNIT: Interacts with EGLN3/PHD3. Identified in the spliceosome C
CC complex (By similarity). Interacts with ERK signaling proteins
CC MAP2K1/MEK1, MAP2K2/MEK2, LAMTOR3, ARAF/Raf-1, MAPK1/ERK2 and
CC MAPK3/ERK1. {ECO:0000250, ECO:0000269|PubMed:15118098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9DAJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DAJ4-2; Sequence=VSP_018418, VSP_018419;
CC Name=3;
CC IsoId=Q9DAJ4-3; Sequence=VSP_018417, VSP_018420;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15118098}.
CC -!- SIMILARITY: Belongs to the WD repeat MORG1 family. {ECO:0000305}.
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DR EMBL; AY365434; AAQ64635.1; -; mRNA.
DR EMBL; AK005790; BAB24241.1; -; mRNA.
DR EMBL; AK020654; BAB32164.1; -; mRNA.
DR EMBL; BC005587; AAH05587.1; -; mRNA.
DR EMBL; BC019369; AAH19369.1; -; mRNA.
DR EMBL; BC094624; AAH94624.1; -; mRNA.
DR CCDS; CCDS22493.1; -. [Q9DAJ4-1]
DR RefSeq; NP_080675.2; NM_026399.2. [Q9DAJ4-1]
DR AlphaFoldDB; Q9DAJ4; -.
DR SMR; Q9DAJ4; -.
DR BioGRID; 212467; 2.
DR STRING; 10090.ENSMUSP00000091048; -.
DR PhosphoSitePlus; Q9DAJ4; -.
DR EPD; Q9DAJ4; -.
DR MaxQB; Q9DAJ4; -.
DR PaxDb; Q9DAJ4; -.
DR PeptideAtlas; Q9DAJ4; -.
DR PRIDE; Q9DAJ4; -.
DR ProteomicsDB; 299757; -. [Q9DAJ4-1]
DR ProteomicsDB; 299758; -. [Q9DAJ4-2]
DR ProteomicsDB; 299759; -. [Q9DAJ4-3]
DR Antibodypedia; 26076; 221 antibodies from 29 providers.
DR DNASU; 67836; -.
DR Ensembl; ENSMUST00000093357; ENSMUSP00000091048; ENSMUSG00000005150. [Q9DAJ4-1]
DR Ensembl; ENSMUST00000149050; ENSMUSP00000121568; ENSMUSG00000005150. [Q9DAJ4-2]
DR GeneID; 67836; -.
DR KEGG; mmu:67836; -.
DR UCSC; uc009mph.1; mouse. [Q9DAJ4-1]
DR CTD; 84292; -.
DR MGI; MGI:1915086; Wdr83.
DR VEuPathDB; HostDB:ENSMUSG00000005150; -.
DR eggNOG; KOG0316; Eukaryota.
DR GeneTree; ENSGT00940000159016; -.
DR HOGENOM; CLU_000288_57_1_1; -.
DR InParanoid; Q9DAJ4; -.
DR OMA; MCWDIRT; -.
DR OrthoDB; 1090342at2759; -.
DR PhylomeDB; Q9DAJ4; -.
DR TreeFam; TF314828; -.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR BioGRID-ORCS; 67836; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Wdr83; mouse.
DR PRO; PR:Q9DAJ4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9DAJ4; protein.
DR Bgee; ENSMUSG00000005150; Expressed in right kidney and 241 other tissues.
DR ExpressionAtlas; Q9DAJ4; baseline and differential.
DR Genevisible; Q9DAJ4; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0090594; P:inflammatory response to wounding; IMP:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; ISO:MGI.
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 Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Spliceosome; WD repeat.
FT CHAIN 1..315
FT /note="WD repeat domain-containing protein 83"
FT /id="PRO_0000235264"
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"
FT VAR_SEQ 111..138
FT /note="KVNTVQFNEEATVILSGSIDSSVRCWDC -> VSTSEKTLVNVCIVEQAEAY
FT GPDTKDAD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018417"
FT VAR_SEQ 111..130
FT /note="KVNTVQFNEEATVILSGSID -> VSTSEKTLVNVCIVEIHISP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018418"
FT VAR_SEQ 131..315
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018419"
FT VAR_SEQ 139..315
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018420"
FT CONFLICT 123
FT /note="V -> G (in Ref. 2; BAB32164)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> N (in Ref. 2; BAB32164)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="E -> D (in Ref. 2; BAB32164)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="A -> Q (in Ref. 2; BAB32164)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="R -> S (in Ref. 2; BAB32164)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="S -> G (in Ref. 3; AAH19369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 34444 MW; 678024513FAA1192 CRC64;
MAFPEPKPRA PELPQKRMKT LDCSQGAVRA VRFNVDGNYC LTCGSDKTLK LWNPLRGTLL
RTYSGHGYEV LDAAGSFDNS HLCSGGGDKT VVLWDVATGQ VVRKFRGHAG KVNTVQFNEE
ATVILSGSID SSVRCWDCRS RKPEPVQTLD EARDGISSVK VSDHEILAGS VDGRVRRYDL
RMGQVSSDYV GSPITCTCFS RDGQCTLISS LDSTLRLLDK DTGELLGEYV GHKNQQYKLD
CCLSERDTHV VSCSEDGKVF FWDLVEGALA LALPVGSNVV QSLAYHPTEP CLLTAMGGSI
QYWREETYEA EGGAG
