ID WDR44_BOVIN Reviewed; 912 AA.
AC Q9XSC3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 128.
DE RecName: Full=WD repeat-containing protein 44;
DE AltName: Full=Rab11-binding protein {ECO:0000303|PubMed:10077598};
DE Short=Rab11BP {ECO:0000303|PubMed:10077598};
DE AltName: Full=Rabphilin-11 {ECO:0000250|UniProtKB:Q9R037};
GN Name=WDR44; Synonyms=RAB11BP {ECO:0000303|PubMed:10077598}, RPH11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 88-117; 217-228; 376-389;
RP 536-540; 541-550; 695-704; 791-811 AND 837-860, FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH RAB11.
RX PubMed=10077598; DOI=10.1073/pnas.96.6.2840;
RA Zeng J., Ren M., Gravotta D., De Lemos-Chiarandini C., Tempst P.,
RA Erdjument-Bromage H., Liu M., Xu G., Shen T., Morimoto T., Adesnik M.,
RA Sabatini D.D.;
RT "Identification of a putative effector protein for rab11 that participates
RT in transferrin recycling.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2840-2845(1999).
CC -!- FUNCTION: Downstream effector for Rab11 which regulates Rab11
CC intracellular membrane trafficking functions such as endocytic
CC recycling, intracellular ciliogenesis and protein export
CC (PubMed:10077598). ATK1-mediated phosphorylation of WDR44 induces
CC binding to Rab11 which activates endocytic recycling of transferrin
CC receptor back to the plasma membrane (PubMed:10077598). When bound to
CC Rab11, prevents the formation of the ciliogenic Rab11-Rabin8/RAB3IP-
CC RAB11FIP3 complex, therefore inhibiting preciliary trafficking and
CC ciliogenesis (By similarity). Participates in neo-synthesized protein
CC export by connecting the endoplasmic reticulum (ER) with the endosomal
CC tubule via direct interactions with the integral ER proteins VAPA or
CC VAPB and the endosomal protein GRAFs (GRAF1/ARHGAP26 or
CC GRAF2/ARHGAP10), which facilitates the transfer of proteins such as E-
CC cadherin, MPP14 and CFTR into a Rab8-Rab10-Rab11-dependent export route
CC (By similarity). {ECO:0000250|UniProtKB:Q5JSH3,
CC ECO:0000269|PubMed:10077598}.
CC -!- SUBUNIT: Interacts with the GTP-bound form of RAB11A when membrane-
CC associated (PubMed:10077598). Interacts with GRAF1/ARHGAP26 or
CC GRAF2/ARHGAP10; the interaction connects the endoplasmic reticulum (ER)
CC with the endosomal tubule (By similarity). Interacts (via FFAT-like
CC motif) with VAPA (via MSP domain) or VAPB (via MSP domain); the
CC interaction connects the ER with the endosomal tubule (By similarity).
CC Does not bind to other Rab and Rho small G proteins (PubMed:10077598).
CC {ECO:0000250|UniProtKB:Q5JSH3, ECO:0000269|PubMed:10077598}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10077598}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:10077598}. Endosome
CC membrane {ECO:0000269|PubMed:10077598}. Golgi apparatus, trans-Golgi
CC network {ECO:0000269|PubMed:10077598}. Note=Colocalized with RAB11
CC along microtubules oriented toward lamellipodia.
CC {ECO:0000250|UniProtKB:Q9R037}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC {ECO:0000269|PubMed:10077598}.
CC -!- DOMAIN: The FFAT-like motif is important for interaction with VAPA or
CC VAPB. {ECO:0000250|UniProtKB:Q5JSH3}.
CC -!- PTM: Phosphorylated by ATK1; the phosphorylation stabilizes its
CC interaction with RAB11A and RAB11B. {ECO:0000250|UniProtKB:Q5JSH3}.
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DR EMBL; AF117897; AAD21616.1; -; mRNA.
DR RefSeq; NP_777199.1; NM_174774.2.
DR AlphaFoldDB; Q9XSC3; -.
DR SMR; Q9XSC3; -.
DR STRING; 9913.ENSBTAP00000024883; -.
DR PaxDb; 9913-ENSBTAP00000024883; -.
DR Ensembl; ENSBTAT00000024883.6; ENSBTAP00000024883.6; ENSBTAG00000018697.6.
DR GeneID; 286825; -.
DR KEGG; bta:286825; -.
DR CTD; 54521; -.
DR VEuPathDB; HostDB:ENSBTAG00000018697; -.
DR VGNC; VGNC:36900; WDR44.
DR eggNOG; KOG0283; Eukaryota.
DR GeneTree; ENSGT00940000157557; -.
DR InParanoid; Q9XSC3; -.
DR OMA; SQECVRP; -.
DR OrthoDB; 11918at2759; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000018697; Expressed in neutrophil and 104 other cell types or tissues.
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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0140313; F:molecular sequestering activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0061824; P:cytosolic ciliogenesis; ISS:UniProtKB.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR040324; WDR44/Dgr2.
DR PANTHER; PTHR14221; WD REPEAT DOMAIN 44; 1.
DR PANTHER; PTHR14221:SF0; WD REPEAT-CONTAINING PROTEIN 44; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Endosome;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT CHAIN 2..912
FT /note="WD repeat-containing protein 44"
FT /id="PRO_0000262768"
FT REPEAT 508..547
FT /note="WD 1"
FT REPEAT 604..642
FT /note="WD 2"
FT REPEAT 644..684
FT /note="WD 3"
FT REPEAT 689..728
FT /note="WD 4"
FT REPEAT 739..778
FT /note="WD 5"
FT REPEAT 783..822
FT /note="WD 6"
FT REPEAT 871..912
FT /note="WD 7"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..170
FT /note="Binding activity"
FT REGION 79..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..256
FT /note="Important for interaction with ARHGAP26 AND
FT ARHGAP10"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT REGION 318..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..346
FT /note="Important for interaction with RAB11A"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT REGION 334..504
FT /note="Interaction with RAB11"
FT /evidence="ECO:0000269|PubMed:10077598"
FT REGION 396..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..15
FT /note="FFAT-like motif"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT COMPBIAS 87..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
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 96
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 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 478
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6NVE8"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSH3"
SQ SEQUENCE 912 AA; 101293 MW; 9158F1125D5107E9 CRC64;
MASESDTEEF FDAPEDVHLE GGDPIGYPGK VGISALKETE NSAYKVGNES TVQELKQDVS
KKIIESIIEE SQKVIQLEDD SLDSKGKGQS DQATASPVTA GTELSNIPGL LAIDQVLQED
SQKAESQDVS EETELESKQC FPSDDTCEKP VDETTKLTEI SSTAQLNVPE TVTEVLNKEE
VEVKESDVLE SASSHSLSTK DFAVVEEVAP AKPPRQLTPE PDIVASTKKP VPARPPPPAN
FPPPRPPPPS RPAPPPRKKK SELEFEALKT PDLDVPKENI TSDTLLTTNM ASESTVKDSQ
PSLDLASATS GDKIVTAQEN GKAPDGQTIA GEVMGPQRPR SNSGRELTDE EILASVMIKN
LDTGEEIPLS LAEEKLPTGI NPLTLHIMRR TKEYVSNDAA QSDDEEKLQS QQTDTDGGRL
KQKTTQLKKF LGKSVKRAKH LAEEYGERAV NKVKSVRDEV FHTDQDDPSS SDDEGMPYTR
PVKFKAAHGF KGPYDFDQIK VVQDLSGEHM GAVWTMKFSH CGRLLASAGQ DNVVRIWALK
NAFDYFNNMR MKYNTEGRVS PSPSQESLNS SKSDTDTGVC SGTDEDPDDK NAPFRQRPFC
KYKGHTADLL DLSWSKNYFL LSSSMDKTVR LWHISRRECL CCFQHIDFVT AIAFHPRDDR
YFLSGSLDGK LRLWNIPDKK VALWNEVDGQ TKLITAANFC QNGKYAVIGT YDGRCIFYDT
EHLKYHTQIH VRSTRGRNKV GRKITGIEPL PGENKILVTS NDSRIRLYDL RDLSLSMKYK
GYVNSSSQIK ASFSHDFNYL VSGSEDKYVY IWSTYHDLSK FTSVRRDRND FWEGIKAHNA
VVTSAIFAPN PSLMLSLDVQ SEKSEGNEKG EDAEVLETMP SGIMKTDNTE VLLSADFTGA
IKVFINKRKN LS
//
