WDR44_MOUSE
ID WDR44_MOUSE Reviewed; 915 AA.
AC Q6NVE8; Q3UT13; Q8BTS1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=WD repeat-containing protein 44;
DE AltName: Full=Rabphilin-11;
GN Name=Wdr44; Synonyms=RPH11;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-259 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Egg, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-405; SER-472; SER-473 AND SER-474, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-221; SER-344;
RP THR-403; SER-405; SER-472; SER-473; SER-474; TYR-481; SER-563 AND SER-567,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
CC -!- FUNCTION: Downstream effector for RAB11. May be involved in vesicle
CC recycling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the GTP-bound form of RAB11 when membrane-
CC associated. Does not bind to other Rab and Rho small G proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, perinuclear
CC region. Endosome membrane. Golgi apparatus, trans-Golgi network.
CC Note=Colocalized with RAB11 along microtubules oriented toward
CC lamellipodia. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NVE8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NVE8-2; Sequence=VSP_021811;
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DR EMBL; AK088885; BAC40631.2; -; mRNA.
DR EMBL; AK139877; BAE24167.1; -; mRNA.
DR EMBL; BC068151; AAH68151.1; -; mRNA.
DR EMBL; BC049191; AAH49191.1; -; mRNA.
DR CCDS; CCDS40892.1; -. [Q6NVE8-1]
DR RefSeq; NP_001292604.1; NM_001305675.1. [Q6NVE8-1]
DR RefSeq; NP_780389.2; NM_175180.3. [Q6NVE8-1]
DR RefSeq; XP_006527763.1; XM_006527700.3. [Q6NVE8-1]
DR AlphaFoldDB; Q6NVE8; -.
DR SMR; Q6NVE8; -.
DR BioGRID; 215359; 4.
DR STRING; 10090.ENSMUSP00000044616; -.
DR iPTMnet; Q6NVE8; -.
DR PhosphoSitePlus; Q6NVE8; -.
DR EPD; Q6NVE8; -.
DR jPOST; Q6NVE8; -.
DR MaxQB; Q6NVE8; -.
DR PaxDb; Q6NVE8; -.
DR PeptideAtlas; Q6NVE8; -.
DR PRIDE; Q6NVE8; -.
DR ProteomicsDB; 297650; -. [Q6NVE8-1]
DR ProteomicsDB; 297651; -. [Q6NVE8-2]
DR Antibodypedia; 29682; 36 antibodies from 13 providers.
DR Ensembl; ENSMUST00000035766; ENSMUSP00000044616; ENSMUSG00000036769. [Q6NVE8-1]
DR Ensembl; ENSMUST00000101670; ENSMUSP00000099193; ENSMUSG00000036769. [Q6NVE8-1]
DR GeneID; 72404; -.
DR KEGG; mmu:72404; -.
DR UCSC; uc009suw.2; mouse. [Q6NVE8-1]
DR UCSC; uc009suy.1; mouse. [Q6NVE8-2]
DR CTD; 54521; -.
DR MGI; MGI:1919654; Wdr44.
DR VEuPathDB; HostDB:ENSMUSG00000036769; -.
DR eggNOG; KOG0283; Eukaryota.
DR GeneTree; ENSGT00940000157557; -.
DR HOGENOM; CLU_009835_2_1_1; -.
DR InParanoid; Q6NVE8; -.
DR OMA; WHISRSE; -.
DR OrthoDB; 1332590at2759; -.
DR PhylomeDB; Q6NVE8; -.
DR TreeFam; TF329226; -.
DR BioGRID-ORCS; 72404; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Wdr44; mouse.
DR PRO; PR:Q6NVE8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6NVE8; protein.
DR Bgee; ENSMUSG00000036769; Expressed in lumbar dorsal root ganglion and 200 other tissues.
DR ExpressionAtlas; Q6NVE8; baseline and differential.
DR Genevisible; Q6NVE8; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; 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; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR040324; WDR44/Dgr2.
DR PANTHER; PTHR14221; PTHR14221; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Endosome;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CHAIN 2..915
FT /note="WD repeat-containing protein 44"
FT /id="PRO_0000262770"
FT REPEAT 511..550
FT /note="WD 1"
FT REPEAT 607..645
FT /note="WD 2"
FT REPEAT 647..687
FT /note="WD 3"
FT REPEAT 692..731
FT /note="WD 4"
FT REPEAT 742..781
FT /note="WD 5"
FT REPEAT 786..825
FT /note="WD 6"
FT REPEAT 840..880
FT /note="WD 7"
FT REPEAT 882..915
FT /note="WD 8"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..173
FT /note="Binding activity"
FT REGION 79..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..139
FT /evidence="ECO:0000255"
FT COMPBIAS 117..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 403
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 481
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..478
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021811"
FT CONFLICT 629
FT /note="D -> E (in Ref. 1; BAE24167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 915 AA; 101555 MW; B5FDF8A4C87295DC CRC64;
MASESDTEEF YDAPEDVHLG TGYPVGSPGK VGLLSFKEAE NTANQAGNES PVQELRQDVS
KKIIESIIEE SQKVLQLEDD SLDSKGKGLS DEATAGPSVA GTEFSNIPGL LAIEHELQQD
SEKAESQNVA EESELETQKC FPSDETCEKS EKTVDETDNL TEVSSGEQLD ASGLEAETLN
KEALEVKEGD VLDPASLDTL STTDFAAVEE VAPAKPPRHL TPEPDIVAST KKPVPARPPP
PTNFPPPRPP PPSRPAPPPR KKKSELEFEA LKTPDLDVPK ENITSDSLLT TNMASENTVR
DSLPSLDLAS ATSGDKIVTA QENGKAPDVQ TVAGEVMGPQ RPRSNSGREL TDEEILASVM
IKNLDTGEEI PLSLAEEKLP TGINPLTLHI MRRTKEYVSN DATQSDDEEK LQSQQTDTDG
GRLKQKTTQL KKFLGKSVKR AKHLAEEYGE RAINKVKSVR DEVFHTDQDD PSSSDDEGMP
YTRPVKFKAA HGFKGPYDFD QIKVVQDLSG EHMGAVWTMK FSHCGRLLAS AGQDNIVRIW
ALKNAFDYFN NMRMKYNTEG RVSPSPSQES LSSSKSDTDM GVCSGTDEDP DDKNAPFRQR
PFCKYKGHTA DLLDLSWSKN YFLLSSSMDK TVRLWHISRR ECLCCFQHID FVTAIAFHPR
DDRYFLSGSL DGKLRLWNIP DKKVALWNEV DGQTKLITAA NFCQNGKYAV IGTYDGRCIF
YDTEHLKYHT QIHVRSTRGR NKVGRKITGI EPLPGENKIL VTSNDSRIRL YDLRDLSLSM
KYKGYVNSSS QIKASFSHDF TYLVSGSEDK YVYIWSTYHD LSKFTSVRRD RNDFWEGIKA
HNAVVTSAIF APNPSLMLSL DVQSEKLEGI DKYEDAEVLD STSTGIVKTD NTEVLLSADF
TGAIKVFINK RKTVS
