RAB10_CHICK
ID RAB10_CHICK Reviewed; 200 AA.
AC Q5ZIT5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ras-related protein Rab-10;
DE EC=3.6.5.2;
GN Name=RAB10; ORFNames=RCJMB04_23k10;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is mainly involved
CC in the biosynthetic transport of proteins from the Golgi to the plasma
CC membrane. Also plays a specific role in asymmetric protein transport to
CC the plasma membrane within the polarized neuron and epithelial cells.
CC In neurons, it is involved in axonogenesis through regulation of
CC vesicular membrane trafficking toward the axonal plasma membrane while
CC in epithelial cells, it regulates transport from the Golgi to the
CC basolateral membrane. Moreover, may play a role in the basolateral
CC recycling pathway and in phagosome maturation. Finally, may play a role
CC in endoplasmic reticulum dynamics and morphology controlling tubulation
CC along microtubules and tubules fusion (By similarity).
CC {ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P61026};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P61026};
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}.
CC Endosome membrane {ECO:0000250|UniProtKB:P61026}. Recycling endosome
CC membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000250|UniProtKB:P24409}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:P61027}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P61027}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P61027}. Note=Associates with SLC2A4/GLUT4
CC storage vesicles (By similarity). Localizes to the base of the cilium
CC (By similarity). Transiently associates with phagosomes (By
CC similarity). Localizes to the endoplasmic reticulum at domains of new
CC tubule growth (By similarity). {ECO:0000250|UniProtKB:P24409,
CC ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AJ720699; CAG32358.1; -; mRNA.
DR RefSeq; NP_001026268.1; NM_001031097.1.
DR AlphaFoldDB; Q5ZIT5; -.
DR SMR; Q5ZIT5; -.
DR STRING; 9031.ENSGALP00000036002; -.
DR PaxDb; Q5ZIT5; -.
DR GeneID; 421994; -.
DR KEGG; gga:421994; -.
DR CTD; 10890; -.
DR VEuPathDB; HostDB:geneid_421994; -.
DR eggNOG; KOG0078; Eukaryota.
DR InParanoid; Q5ZIT5; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; Q5ZIT5; -.
DR PRO; PR:Q5ZIT5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0045200; P:establishment of neuroblast polarity; ISS:UniProtKB.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Endosome; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..200
FT /note="Ras-related protein Rab-10"
FT /id="PRO_0000260526"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 200 AA; 22549 MW; F3419AA3D9283091 CRC64;
MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDLKIKT VELQGKKIKL
QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNAKSFENI SKWLRNIDEH ANEDVERMLL
GNKCDMEDKR VVPKAKGEQI AREHGIRFFE TSAKANINIE KAFLTLAEDI LRKTPVKEPN
SENVDISSGG GVTGWKSKCC
