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RB27B_RAT
ID   RB27B_RAT               Reviewed;         218 AA.
AC   Q99P74;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Ras-related protein Rab-27B;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:O00194};
GN   Name=Rab27b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Bone;
RA   Zhao H., Vaananen K.;
RT   "Expression of small GTP binding rab proteins in rat long bones.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=21775604; DOI=10.1523/jneurosci.0436-11.2011;
RA   Huang S.H., Duan S., Sun T., Wang J., Zhao L., Geng Z., Yan J., Sun H.J.,
RA   Chen Z.Y.;
RT   "JIP3 mediates TrkB axonal anterograde transport and enhances BDNF
RT   signaling by directly bridging TrkB with kinesin-1.";
RL   J. Neurosci. 31:10602-10614(2011).
CC   -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC       inactive GDP-bound states. In its active state, binds to a variety of
CC       effector proteins to regulate homeostasis of late endocytic pathway,
CC       including endosomal positioning, maturation and secretion (By
CC       similarity). Plays a role in NTRK2/TRKB axonal anterograde transport by
CC       facilitating the association of NTRK2/TRKB with KLC1 (PubMed:21775604).
CC       May be involved in targeting uroplakins to urothelial apical membranes.
CC       {ECO:0000250|UniProtKB:O00194, ECO:0000250|UniProtKB:Q8HZJ5,
CC       ECO:0000269|PubMed:21775604}.
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:O00194};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:O00194};
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. Activated by GEFs such as DENND10.
CC       {ECO:0000250|UniProtKB:O00194}.
CC   -!- SUBUNIT: Interacts with SYTL2, SYTL4, MYRIP and MLPH. Interacts with
CC       RPH3A and RPH3A (By similarity). Interacts (GDP-bound form
CC       preferentially) with DENND10 (By similarity).
CC       {ECO:0000250|UniProtKB:O00194, ECO:0000250|UniProtKB:Q99P58}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O00194}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:O00194}. Late endosome
CC       {ECO:0000250|UniProtKB:O00194}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AF325693; AAG49587.1; -; mRNA.
DR   RefSeq; NP_445911.1; NM_053459.1.
DR   RefSeq; XP_006254992.1; XM_006254930.3.
DR   AlphaFoldDB; Q99P74; -.
DR   SMR; Q99P74; -.
DR   CORUM; Q99P74; -.
DR   STRING; 10116.ENSRNOP00000016369; -.
DR   iPTMnet; Q99P74; -.
DR   PhosphoSitePlus; Q99P74; -.
DR   jPOST; Q99P74; -.
DR   PaxDb; Q99P74; -.
DR   PRIDE; Q99P74; -.
DR   Ensembl; ENSRNOT00000106463; ENSRNOP00000095120; ENSRNOG00000012176.
DR   GeneID; 84590; -.
DR   KEGG; rno:84590; -.
DR   CTD; 5874; -.
DR   RGD; 620114; Rab27b.
DR   eggNOG; KOG0081; Eukaryota.
DR   GeneTree; ENSGT00940000157449; -.
DR   HOGENOM; CLU_041217_10_1_1; -.
DR   InParanoid; Q99P74; -.
DR   OMA; IGWMRDI; -.
DR   OrthoDB; 1190514at2759; -.
DR   PhylomeDB; Q99P74; -.
DR   TreeFam; TF312895; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR   Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:Q99P74; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000012176; Expressed in stomach and 17 other tissues.
DR   Genevisible; Q99P74; RN.
DR   GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO-UCL.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0005795; C:Golgi stack; ISO:RGD.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; ISO:RGD.
DR   GO; GO:0032585; C:multivesicular body membrane; ISO:RGD.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:RGD.
DR   GO; GO:0042589; C:zymogen granule membrane; IDA:RGD.
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; ISS:UniProtKB.
DR   GO; GO:0031489; F:myosin V binding; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0099641; P:anterograde axonal protein transport; IMP:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; ISO:RGD.
DR   GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:RGD.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd04127; Rab27A; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041837; Rab27a/b.
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   Acetylation; Disulfide bond; Endosome; GTP-binding; Hydrolase; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O00194"
FT   CHAIN           2..218
FT                   /note="Ras-related protein Rab-27B"
FT                   /id="PRO_0000121226"
FT   MOTIF           38..46
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         16..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         74..78
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         163..165
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O00194"
FT   MOD_RES         218
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           216
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           218
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..188
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   218 AA;  24620 MW;  784C894F9B935FEA CRC64;
     MTDGDYDYLI KLLALGDSGV GKTTFLYRYT DNKFNPKFIT TVGIDFREKR VVYDTQGADG
     SSGKAFKVHL QLWDTAGQER FRSLTTAFFR DAMGFLLMFD LTSQQSFLNV RNWMSQLQAN
     AYCENPDIVL IGNKADLLDQ REVNERQARE LAEKYGIPYF ETSAATGQNV EKSVETLLDL
     IMKRMEKCVE KTQVPDTVNG VNSGKVDGEK PAEKKCAC
 
 
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