WDR41_MOUSE
ID WDR41_MOUSE Reviewed; 460 AA.
AC Q3UDP0; Q8C4F1; Q8C8K5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=WD repeat-containing protein 41 {ECO:0000305};
GN Name=Wdr41 {ECO:0000312|MGI:MGI:2445123};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, and Medulla oblongata;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=27617292; DOI=10.1126/sciadv.1601167;
RA Yang M., Liang C., Swaminathan K., Herrlinger S., Lai F., Shiekhattar R.,
RA Chen J.F.;
RT "A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in
RT autophagy.";
RL Sci. Adv. 2:E1601167-E1601167(2016).
CC -!- FUNCTION: Non-catalytic component of the C9orf72-SMCR8 complex, a
CC complex that has guanine nucleotide exchange factor (GEF) activity and
CC regulates autophagy. The C9orf72-SMCR8 complex promotes the exchange of
CC GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their
CC active GTP-bound form, thereby promoting autophagosome maturation. As
CC part of the C9orf72-SMCR8 complex, stimulates RAB8A and RAB11A GTPase
CC activity in vitro, however WDR42 is shown not be an essential complex
CC component for this function (By similarity). The C9orf72-SMCR8 complex
CC also acts as a negative regulator of autophagy initiation by
CC interacting with the ULK1/ATG1 kinase complex and inhibiting its
CC protein kinase activity. {ECO:0000250|UniProtKB:Q9HAD4}.
CC -!- SUBUNIT: Component of the C9orf72-SMCR8 complex, at least composed of
CC C9orf72, SMCR8 and WDR41. The complex is formed of two protomers, each
CC individually consisting of one molecule each of C9orf72, SMCR8 and
CC WDR41 (By similarity). The protomers homodimerize via an interaction
CC between C9orf72 (via C-terminus) and SMCR8 (via N-terminus) (By
CC similarity). Within each protomer SMCR8 (via DENN domain) acts as a
CC bridging protein between WDR41 (via C-terminus and N-terminus) and
CC C9orf72 (via C-terminus) (By similarity). The C9orf72-SMCR8 complex
CC associates with the ULK1/ATG1 kinase complex.
CC {ECO:0000250|UniProtKB:Q9HAD4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27617292}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UDP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UDP0-2; Sequence=VSP_016182, VSP_016183;
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DR EMBL; AK046853; BAC32897.1; -; mRNA.
DR EMBL; AK082348; BAC38474.1; -; mRNA.
DR EMBL; AK149993; BAE29221.1; -; mRNA.
DR CCDS; CCDS56896.2; -. [Q3UDP0-1]
DR RefSeq; NP_766178.2; NM_172590.3. [Q3UDP0-1]
DR RefSeq; XP_017170980.1; XM_017315491.1. [Q3UDP0-1]
DR AlphaFoldDB; Q3UDP0; -.
DR SMR; Q3UDP0; -.
DR BioGRID; 230033; 3.
DR ComplexPortal; CPX-3962; C9orf72-SMCR8 complex.
DR IntAct; Q3UDP0; 2.
DR MINT; Q3UDP0; -.
DR STRING; 10090.ENSMUSP00000138543; -.
DR iPTMnet; Q3UDP0; -.
DR PhosphoSitePlus; Q3UDP0; -.
DR EPD; Q3UDP0; -.
DR MaxQB; Q3UDP0; -.
DR PaxDb; Q3UDP0; -.
DR PeptideAtlas; Q3UDP0; -.
DR PRIDE; Q3UDP0; -.
DR ProteomicsDB; 297648; -. [Q3UDP0-1]
DR ProteomicsDB; 297649; -. [Q3UDP0-2]
DR Antibodypedia; 24490; 94 antibodies from 18 providers.
DR DNASU; 218460; -.
DR Ensembl; ENSMUST00000056512; ENSMUSP00000055145; ENSMUSG00000042015. [Q3UDP0-1]
DR Ensembl; ENSMUST00000160801; ENSMUSP00000124033; ENSMUSG00000042015. [Q3UDP0-1]
DR GeneID; 218460; -.
DR KEGG; mmu:218460; -.
DR UCSC; uc033gmt.1; mouse. [Q3UDP0-1]
DR CTD; 55255; -.
DR MGI; MGI:2445123; Wdr41.
DR VEuPathDB; HostDB:ENSMUSG00000042015; -.
DR eggNOG; ENOG502QURA; Eukaryota.
DR GeneTree; ENSGT00390000017026; -.
DR HOGENOM; CLU_047570_0_0_1; -.
DR InParanoid; Q3UDP0; -.
DR OMA; QLQCHRQ; -.
DR OrthoDB; 1152122at2759; -.
DR PhylomeDB; Q3UDP0; -.
DR TreeFam; TF332914; -.
DR BioGRID-ORCS; 218460; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Wdr41; mouse.
DR PRO; PR:Q3UDP0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UDP0; protein.
DR Bgee; ENSMUSG00000042015; Expressed in interventricular septum and 221 other tissues.
DR ExpressionAtlas; Q3UDP0; baseline and differential.
DR Genevisible; Q3UDP0; MM.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0045920; P:negative regulation of exocytosis; IC:ComplexPortal.
DR GO; GO:0050777; P:negative regulation of immune response; IC:ComplexPortal.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
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 InterPro; IPR040102; WDR41.
DR PANTHER; PTHR22805; PTHR22805; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
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; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..460
FT /note="WD repeat-containing protein 41"
FT /id="PRO_0000051391"
FT REPEAT 40..79
FT /note="WD 1"
FT REPEAT 82..128
FT /note="WD 2"
FT REPEAT 131..168
FT /note="WD 3"
FT REPEAT 220..258
FT /note="WD 4"
FT REPEAT 321..359
FT /note="WD 5"
FT REPEAT 403..441
FT /note="WD 6"
FT VAR_SEQ 233..308
FT /note="DTGFVTGSHVGELLIWDALDWTVQACERTFWSPTAQLDAQQEIKLFQKQNDI
FT SINHFTCDEENIFAAVGRGLYVYN -> GSVLTMGSVLTTGSVLTIGSVLTTGSVLTMG
FT SVLTTGSAADRRLCADHGLCADRRLCADHGLCADCRRLCCPQALC (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016182"
FT VAR_SEQ 309..460
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016183"
FT CONFLICT 135
FT /note="T -> K (in Ref. 1; BAC32897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 51511 MW; DADD97BFB0787D0F CRC64;
MLRWLIGGGR EPQGLAEKAA LQTIGEDQGQ NPYTELLVLE AHRDIVRFLV RLDDFRFASA
GDDGIIVVWN AQTGEKLLEL RGHTQKITAV IAFPPLDSCE ASSQLLLTAS ADRTVGVWDC
DTGRQIQRVT CFQSTVKCLT VLQRLDIWLS GGSDLGVWNR KLDLLCKTSH LSDTGISALV
EIPGNCVAAA VGRELIIFRL VTPTEELPEW DIIEVKRLLD HQDNILSLAN INDTGFVTGS
HVGELLIWDA LDWTVQACER TFWSPTAQLD AQQEIKLFQK QNDISINHFT CDEENIFAAV
GRGLYVYNLQ LKRVIACQKT AHDSNILHID KLPNRQLISC SEDGAVRMWE VREKQQLAAE
PVPTGFFNMW GFGRVNKQAS QPVKKQEENV TTCSLELIGD LIGHSSSVEM FLYFEDHGLV
TCSADHLIIL WKNGERESGV RSLKLFQKLE ENGDLYPESP
