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RAB6B_BOVIN
ID   RAB6B_BOVIN             Reviewed;         208 AA.
AC   A6QR46;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Ras-related protein Rab-6B;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:Q9NRW1};
GN   Name=RAB6B;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 active GTP-bound and inactive
CC       GDP-bound states. In their active state, drive transport of vesicular
CC       carriers from donor organelles to acceptor organelles to regulate the
CC       membrane traffic that maintains organelle identity and morphology.
CC       Regulates the compacted morphology of the Golgi. Seems to have a role
CC       in retrograde membrane traffic at the level of the Golgi complex. May
CC       function in retrograde transport in neuronal cells.
CC       {ECO:0000250|UniProtKB:Q9NRW1}.
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:Q9NRW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRW1};
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. {ECO:0000250|UniProtKB:Q9NRW1}.
CC   -!- SUBUNIT: Interacts with RAB6KIFL. Interacts (GTP-bound) with BICD1 (via
CC       C-terminus); the interaction is direct. Interacts (GDP-bound) with
CC       DYNLRB1. Interacts with BICDL1/BICDR1; leads to its accumulation in the
CC       pericentrosomal region (By similarity). Interacts (GTP-bound) with
CC       APBA1/MINT1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9NRW1}; Lipid-anchor {ECO:0000305}. Endoplasmic
CC       reticulum-Golgi intermediate compartment
CC       {ECO:0000250|UniProtKB:Q9NRW1}. Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:Q9NRW1}. Note=Colocalizes with BICD1 at
CC       vesicular structures that align along microtubules.
CC       {ECO:0000250|UniProtKB:Q9NRW1}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; BC150111; AAI50112.1; -; mRNA.
DR   RefSeq; NP_001094599.1; NM_001101129.1.
DR   AlphaFoldDB; A6QR46; -.
DR   SMR; A6QR46; -.
DR   STRING; 9913.ENSBTAP00000001199; -.
DR   PaxDb; A6QR46; -.
DR   PRIDE; A6QR46; -.
DR   GeneID; 526526; -.
DR   KEGG; bta:526526; -.
DR   CTD; 51560; -.
DR   eggNOG; KOG0094; Eukaryota.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; A6QR46; -.
DR   OrthoDB; 1277051at2759; -.
DR   TreeFam; TF300803; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:1903292; P:protein localization to Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; 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   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW   Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Prenylation; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..208
FT                   /note="Ras-related protein Rab-6B"
FT                   /id="PRO_0000371507"
FT   MOTIF           42..50
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         20..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         208
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           206
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           208
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  23462 MW;  E81C831996E2446D CRC64;
     MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
     TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNLNS FQQTSKWIDD VRTERGSDVI
     IMLVGNKTDL ADKRQITIEE GEQRAKELSV MFIETSAKTG YNVKQLFRRV ASALPGMENV
     QEKSKEGMID IKLDKPQEPP ASEGGCSC
 
 
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