WDR44_RAT
ID WDR44_RAT Reviewed; 908 AA.
AC Q9R037;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=WD repeat-containing protein 44;
DE AltName: Full=Rabphilin-11;
GN Name=Wdr44; Synonyms=RPH11;
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], PROTEIN SEQUENCE OF 53-75; 194-216; 701-709;
RP 272-289; 294-306; 488-496; 537-546; 667-688; 740-751; 786-803; 832-856 AND
RP 882-895, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=10464283; DOI=10.1074/jbc.274.36.25517;
RA Mammoto A., Ohtsuka T., Hotta I., Sasaki T., Takai Y.;
RT "Rab11BP/Rabphilin-11, a downstream target of rab11 small G protein
RT implicated in vesicle recycling.";
RL J. Biol. Chem. 274:25517-25524(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; THR-396; SER-398;
RP SER-465; SER-466; SER-467 AND SER-556, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Downstream effector for RAB11. May be involved in vesicle
CC recycling. {ECO:0000269|PubMed:10464283}.
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 {ECO:0000269|PubMed:10464283}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:10464283}. Endosome
CC membrane {ECO:0000269|PubMed:10464283}. Golgi apparatus, trans-Golgi
CC network {ECO:0000269|PubMed:10464283}. Note=Colocalized with RAB11
CC along microtubules oriented toward lamellipodia.
CC -!- TISSUE SPECIFICITY: Expressed in heart; brain; spleen; lung; liver;
CC muscle and kidney. {ECO:0000269|PubMed:10464283}.
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DR EMBL; AF130121; AAF02478.1; -; mRNA.
DR AlphaFoldDB; Q9R037; -.
DR SMR; Q9R037; -.
DR STRING; 10116.ENSRNOP00000047275; -.
DR iPTMnet; Q9R037; -.
DR PhosphoSitePlus; Q9R037; -.
DR jPOST; Q9R037; -.
DR PaxDb; Q9R037; -.
DR UCSC; RGD:727965; rat.
DR RGD; 727965; Wdr44.
DR eggNOG; KOG0283; Eukaryota.
DR InParanoid; Q9R037; -.
DR PhylomeDB; Q9R037; -.
DR PRO; PR:Q9R037; -.
DR Proteomes; UP000002494; Unplaced.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; IDA:RGD.
DR GO; GO:0030334; P:regulation of cell migration; IMP: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; 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 Cytoplasm; Direct protein sequencing; Endosome; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..908
FT /note="WD repeat-containing protein 44"
FT /id="PRO_0000262771"
FT REPEAT 504..543
FT /note="WD 1"
FT REPEAT 600..638
FT /note="WD 2"
FT REPEAT 640..680
FT /note="WD 3"
FT REPEAT 685..724
FT /note="WD 4"
FT REPEAT 735..774
FT /note="WD 5"
FT REPEAT 779..818
FT /note="WD 6"
FT REGION 1..163
FT /note="Binding activity"
FT REGION 108..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 61
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 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 263
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 474
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6NVE8"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
SQ SEQUENCE 908 AA; 100948 MW; E5F45471D10DD2CA CRC64;
MMPLKMCTWG GSYPVGSPGK VGLLSFKETK NTGNKAGNES PVQELRQDVS KKIIECIIEE
SQKVLQLEDD SLDSKGKGLS DQATASHSVA GTEFSNIPGL LAIQHELQQG SRKADSQNAA
EETELETQKC FPSDNNCEKS EKTEDETNNL TEVSSADQLD ASKLETEILN KEAVEVKEGD
VVNPASSDAL STKDFAAVEE VAPAKPPRHL TPEPDIVAST KKPVPARPPP PTNFPPPRPP
PPSRPAPPPR KKKSDLEFEA LKTPDLDVPK DNIASDSLLT TNMASESTVR DSLPSLDLAS
ATSGDKIVTA QENGKAPDVQ TVAGEVMGPQ RPRSNSGREL TDEEILASVM IKNLDTGEEI
PLSLAEEKLP TGINPLTPLT LHIMRRTKEY VSNDATQSDD EEKLQSQQTD TDGGRLKQKT
TQLKKFLGKS VKRAKHLAEE YGERAINKVK SVRDEVFHTD QDDPSSSDDE GMPYTRPVKF
KAAHGFKGPY DFDQIKVVQD LSGEHMGAVW TMKFSHCGRL LASAGQDNIV RIWALKNAFD
YFNNMRMKYN TEGRVSPSPS QESLSSSKSD TDMGVCSGTD EDPDDKNAPF RQRPFCKYKG
HTADLLDLSW SKNYFLLSSS MDKTVRLWHI SRRECLCCFQ HIDFVTAIAF HPRDDRYFLS
GSLDGKLRLW NIPDKKVALW NEVDGQTKLI TAANFCQNGK YAVIGTYDGR CIFYDTEHLK
YHTQIHVRST RGRNKVGRKI TGIEPLPGEN KILVTSNDSR IRLYDLRDLS LSMKYKGYVN
SSSQIKASFS HDFTYLVSGS EDKYVYIWST YHDLSKFTSV RRDRNDFWEG IKAHNAVVTS
AIFAPNPSLM LSLDVQSEKL EGIDKYEDAE VLDNTSTGIV KTDNTEVLLS ADFTGAQCFY
VKNSFLYP