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RAB8A_CANLF
ID   RAB8A_CANLF             Reviewed;         207 AA.
AC   P61007; P24407;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Ras-related protein Rab-8A;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P61006};
DE   AltName: Full=Oncogene c-mel;
DE   Flags: Precursor;
GN   Name=RAB8A; Synonyms=MEL, RAB8;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RX   PubMed=2123294; DOI=10.1128/mcb.10.12.6578-6585.1990;
RA   Chavrier P., Vingron M., Sander C., Simons K., Zerial M.;
RT   "Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell
RT   line.";
RL   Mol. Cell. Biol. 10:6578-6585(1990).
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 sets of downstream effectors directly responsible for vesicle
CC       formation, movement, tethering and fusion. That Rab is involved in
CC       polarized vesicular trafficking and neurotransmitter release. Together
CC       with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42
CC       and DNMBP promotes transcytosis of PODXL to the apical membrane
CC       initiation sites (AMIS), apical surface formation and lumenogenesis.
CC       Regulates the compacted morphology of the Golgi (By similarity).
CC       Together with MYO5B and RAB11A participates in epithelial cell
CC       polarization. Also involved in membrane trafficking to the cilium and
CC       ciliogenesis (By similarity). Together with MICALL2, may also regulate
CC       adherens junction assembly (By similarity). May play a role in insulin-
CC       induced transport to the plasma membrane of the glucose transporter
CC       GLUT4 and therefore play a role in glucose homeostasis (By similarity).
CC       Involved in autophagy (By similarity). {ECO:0000250|UniProtKB:P35280,
CC       ECO:0000250|UniProtKB:P55258, ECO:0000250|UniProtKB:P61006}.
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:P61006};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P61006};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC       activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC       and GDP dissociation inhibitors which inhibit the dissociation of the
CC       nucleotide from the GTPase (By similarity). Activated in response to
CC       insulin (By similarity). {ECO:0000250|UniProtKB:P35280,
CC       ECO:0000250|UniProtKB:P61006}.
CC   -!- SUBUNIT: Interacts (GTP-bound form) with MICALL1; regulates RAB8A
CC       association with recycling endosomes (By similarity). Interacts with
CC       MICALL2; competes with RAB13 and is involved in E-cadherin endocytic
CC       recycling (By similarity). Interacts (GTP-bound form) with MICAL1,
CC       MICALCL, MICAL3 and EHBP1L1; two molecules of RAB8A can bind to one
CC       molecule of the effector protein; ternary complexes of RAB8A, RAB13 and
CC       either MICAL1 or EHBP1L1 are possible (By similarity). Interacts (GTP-
CC       bound form) with EHBP1 (By similarity). Interacts with EHD1 (By
CC       similarity). Interacts with MAP4K2 and SYTL4 (By similarity). Interacts
CC       with SGSM1 and SGSM3 (By similarity). Interacts with RABIF, RIMS2,
CC       RPH3A and RPH3A (By similarity). Interacts with OPTN (By similarity).
CC       Interacts with RAB3IP (By similarity). Interacts with MYO5B (By
CC       similarity). Interacts with PIFO (By similarity). Interacts with
CC       BIRC6/bruce (By similarity). Interacts with OCRL (By similarity).
CC       Interacts with AHI1 (By similarity). Interacts with DCDC1 (By
CC       similarity). Interacts with LRRK2; interaction facilitates
CC       phosphorylation of Thr-72 (By similarity). Interacts with RAB31P, GDI1,
CC       GDI2, CHM, CHML, RABGGTA, RABGGTB, TBC1D15 and INPP5B; these
CC       interactions are dependent on Thr-72 not being phosphorylated (By
CC       similarity). Interacts with RILPL1 and RILPL2; these interactions are
CC       dependent on the phosphorylation of Thr-72 by LRRK2 (By similarity).
CC       Interacts with DZIP1; prevents inhibition by the GDP-dissociation
CC       inhibitor GDI2 (By similarity). {ECO:0000250|UniProtKB:P55258,
CC       ECO:0000250|UniProtKB:P61006}.
CC   -!- INTERACTION:
CC       P61007; Q8BMD2-1: Dzip1; Xeno; NbExp=3; IntAct=EBI-7473289, EBI-16153101;
CC       P61007; P50395: GDI2; Xeno; NbExp=2; IntAct=EBI-7473289, EBI-1049143;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P55258};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P55258}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P55258}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:P61006}. Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:P61006}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:P61006}. Cytoplasmic vesicle, phagosome membrane
CC       {ECO:0000250|UniProtKB:P61006, ECO:0000250|UniProtKB:Q92930}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:Q92930}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q92930}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:P55258}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:P55258}. Midbody
CC       {ECO:0000250|UniProtKB:P61006}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P61006}. Note=Colocalizes with OPTN at the Golgi
CC       complex and in vesicular structures close to the plasma membrane. In
CC       the GDP-bound form, present in the perinuclear region. Shows a
CC       polarized distribution to distal regions of cell protrusions in the
CC       GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and
CC       RAB11A in apical membrane initiation sites (AMIS) during the generation
CC       of apical surface and lumenogenesis. Localizes to tubular recycling
CC       endosome. Recruited to phagosomes containing S.aureus or Mycobacterium
CC       (By similarity). Non-phosphorylated RAB8A predominantly localizes to
CC       the cytoplasm whereas phosphorylated RAB8A localizes to the membrane
CC       (By similarity). {ECO:0000250|UniProtKB:P61006}.
CC   -!- PTM: Phosphorylation of Thr-72 in the switch II region by LRRK2
CC       prevents the association of RAB regulatory proteins, including CHM,
CC       CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC       {ECO:0000250|UniProtKB:P61006}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; X56385; CAB56776.1; -; mRNA.
DR   PIR; B36364; B36364.
DR   RefSeq; NP_001003152.1; NM_001003152.1.
DR   AlphaFoldDB; P61007; -.
DR   SMR; P61007; -.
DR   DIP; DIP-42002N; -.
DR   IntAct; P61007; 3.
DR   MINT; P61007; -.
DR   STRING; 9615.ENSCAFP00000023207; -.
DR   PaxDb; P61007; -.
DR   PRIDE; P61007; -.
DR   Ensembl; ENSCAFT00030040626; ENSCAFP00030035461; ENSCAFG00030022117.
DR   Ensembl; ENSCAFT00040034659; ENSCAFP00040030179; ENSCAFG00040018726.
DR   Ensembl; ENSCAFT00845054077; ENSCAFP00845042481; ENSCAFG00845030471.
DR   GeneID; 403773; -.
DR   KEGG; cfa:403773; -.
DR   CTD; 4218; -.
DR   VEuPathDB; HostDB:ENSCAFG00845030471; -.
DR   eggNOG; KOG0078; Eukaryota.
DR   GeneTree; ENSGT00940000157246; -.
DR   HOGENOM; CLU_041217_23_1_1; -.
DR   InParanoid; P61007; -.
DR   OMA; SKMEQNE; -.
DR   OrthoDB; 1426655at2759; -.
DR   Reactome; R-CFA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-CFA-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-CFA-5620916; VxPx cargo-targeting to cilium.
DR   Reactome; R-CFA-8854214; TBC/RABGAPs.
DR   Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR   Reactome; R-CFA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   Proteomes; UP000002254; Chromosome 20.
DR   Bgee; ENSCAFG00000015782; Expressed in lymph node and 48 other tissues.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0097546; C:ciliary base; IEA:Ensembl.
DR   GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0097730; C:non-motile cilium; IEA:Ensembl.
DR   GO; GO:0045335; C:phagocytic vesicle; 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:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
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; IEA:Ensembl.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IBA:GO_Central.
DR   GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; IBA:GO_Central.
DR   GO; GO:0061512; P:protein localization to cilium; 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:0010506; P:regulation of autophagy; ISS:UniProtKB.
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   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   1: Evidence at protein level;
KW   Autophagy; Cell membrane; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Cytoplasm; Cytoplasmic vesicle;
KW   Cytoskeleton; Endosome; Golgi apparatus; GTP-binding; Hydrolase;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW   Prenylation; Protein transport; Proto-oncogene; Reference proteome;
KW   Transport.
FT   CHAIN           1..204
FT                   /note="Ras-related protein Rab-8A"
FT                   /id="PRO_0000121129"
FT   PROPEP          205..207
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370792"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         17..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         34..40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         63..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006,
FT                   ECO:0000250|UniProtKB:Q9H0U4"
FT   BINDING         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         152..154
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006,
FT                   ECO:0000250|UniProtKB:Q9H0U4"
FT   MOD_RES         72
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   MOD_RES         204
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           204
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  23668 MW;  AA52DBF54A2CD056 CRC64;
     MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI ELDGKRIKLQ
     IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR NWIRNIEEHA SADVEKMILG
     NKCDVNDKRQ VSKERGEKLA LDYGIKFMET SAKANINVEN AFFTLARDIK AKMDKKLEGN
     SPQGSNQGVK ITPDQQKRSS FFRCVLL
 
 
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