WDR44_BOVIN
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 03-AUG-2022, entry version 121.
DE RecName: Full=WD repeat-containing protein 44;
DE AltName: Full=Rab11-binding protein;
DE AltName: Full=Rabphilin-11;
GN Name=WDR44; Synonyms=RAB11BP, 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. May be involved in vesicle
CC recycling. {ECO:0000269|PubMed:10077598}.
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.
CC {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. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC {ECO:0000269|PubMed:10077598}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; Q9XSC3; -.
DR PRIDE; Q9XSC3; -.
DR Ensembl; ENSBTAT00000024883; ENSBTAP00000024883; ENSBTAG00000018697.
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; MENANRP; -.
DR OrthoDB; 1332590at2759; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000018697; Expressed in neutrophil and 104 other 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 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; 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 318..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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
