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Ras-related protein Rab-1B

 RAB1B_RAT               Reviewed;         201 AA.
P10536;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
12-SEP-2018, entry version 148.
RecName: Full=Ras-related protein Rab-1B;
Name=Rab1b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2493636; DOI=10.1093/nar/17.4.1770;
Zahraoui A., Touchot N., Chardin P., Tavitian A.;
"Nucleotide sequence of a rat cDNA: rab1B, encoding a rab1-YPT related
protein.";
Nucleic Acids Res. 17:1770-1770(1989).
[2]
CHARACTERIZATION, AND MUTAGENESIS OF LYS-21 AND ALA-65.
PubMed=2509243; DOI=10.1016/0014-5793(89)81722-3;
Touchot N., Zahraoui A., Vielh E., Tavitian A.;
"Biochemical properties of the YPT-related rab1B protein. Comparison
with rab1A.";
FEBS Lett. 256:79-84(1989).
[3]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=1918138; DOI=10.1083/jcb.115.1.31;
Plutner H., Cox A.D., Pind S., Khosravi-Far R., Bourne J.R.,
Schwaninger R., Der C.J., Balch W.E.;
"Rab1b regulates vesicular transport between the endoplasmic reticulum
and successive Golgi compartments.";
J. Cell Biol. 115:31-43(1991).
[4]
ISOPRENYLATION AT CYS-200 AND CYS-201.
PubMed=1648736; DOI=10.1073/pnas.88.14.6264;
Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R.,
Sinensky M., Balch W.E., Buss J.E., Der C.J.;
"Isoprenoid modification of rab proteins terminating in CC or CXC
motifs.";
Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991).
-!- FUNCTION: The small GTPases Rab are key regulators of
intracellular membrane trafficking, from the formation of
transport vesicles to their fusion with membranes. Rabs cycle
between an inactive GDP-bound form and an active GTP-bound form
that is able to recruit to membranes different set of downstream
effectors directly responsible for vesicle formation, movement,
tethering and fusion. Rab1B regulates vesicular transport between
the endoplasmic reticulum and successive Golgi compartments. Plays
a role in the initial events of the autophagic vacuole development
which take place at specialized regions of the endoplasmic
reticulum (By similarity). {ECO:0000250|UniProtKB:Q9H0U4,
ECO:0000269|PubMed:1918138}.
-!- ACTIVITY REGULATION: Rab activation is generally mediated by a
guanine exchange factor (GEF), while inactivation through
hydrolysis of bound GTP is catalyzed by a GTPase activating
protein (GAP). {ECO:0000305}.
-!- SUBUNIT: Interacts with MICAL1 and MICAL2. Interacts (GTP-bound
form) with MICALCL, MICAL1 and MILCAL3. Interacts with GDI1; the
interaction requires the GDP-bound state. Interacts with CHM/REP1;
the interaction requires the GDP-bound form and is necessary for
prenylation by GGTase II. {ECO:0000250|UniProtKB:Q9H0U4}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1918138}.
Membrane {ECO:0000269|PubMed:1918138}; Lipid-anchor
{ECO:0000269|PubMed:1918138}; Cytoplasmic side
{ECO:0000269|PubMed:1918138}. Preautophagosomal structure membrane
{ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Targeted by REP1 to membranes
of specific subcellular compartments including endoplasmic
reticulum, Golgi apparatus, and intermediate vesicles between
these two compartments. In the GDP-form, colocalizes with GDI in
the cytoplasm. {ECO:0000250|UniProtKB:Q9H0U4}.
-!- PTM: Prenylated; by GGTase II, only after interaction of the
substrate with Rab escort protein 1 (REP1).
{ECO:0000250|UniProtKB:Q9H0U4}.
-!- MISCELLANEOUS: Rab-1B binds GTP and GDP and possesses intrinsic
GTPase activity. {ECO:0000250|UniProtKB:Q9H0U4}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; X13905; CAA32105.1; -; mRNA.
PIR; S06147; S06147.
UniGene; Rn.155100; -.
ProteinModelPortal; P10536; -.
SMR; P10536; -.
IntAct; P10536; 1.
STRING; 10116.ENSRNOP00000067788; -.
iPTMnet; P10536; -.
PhosphoSitePlus; P10536; -.
SwissPalm; P10536; -.
PaxDb; P10536; -.
PRIDE; P10536; -.
RGD; 1642882; Rab1b.
eggNOG; KOG0084; Eukaryota.
eggNOG; ENOG410XQN5; LUCA.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; P10536; -.
PhylomeDB; P10536; -.
PRO; PR:P10536; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
Acetylation; Autophagy; Complete proteome; Cytoplasm; GTP-binding;
Lipoprotein; Membrane; Methylation; Nucleotide-binding;
Phosphoprotein; Prenylation; Protein transport; Reference proteome;
Transport.
CHAIN 1 201 Ras-related protein Rab-1B.
/FTId=PRO_0000121063.
NP_BIND 15 23 GTP. {ECO:0000250|UniProtKB:P62820}.
NP_BIND 33 40 GTP. {ECO:0000250|UniProtKB:P62820}.
NP_BIND 63 67 GTP. {ECO:0000250|UniProtKB:Q9H0U4}.
NP_BIND 121 124 GTP. {ECO:0000250|UniProtKB:Q9H0U4}.
NP_BIND 151 153 GTP. {ECO:0000250|UniProtKB:P62820}.
REGION 64 83 Switch 2 region; required for interaction
with REP1/CHM.
{ECO:0000250|UniProtKB:Q9H0U4}.
MOTIF 37 45 Effector region.
{ECO:0000250|UniProtKB:Q9H0U4}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9H0U4}.
MOD_RES 76 76 O-(2-cholinephosphoryl)serine.
{ECO:0000250|UniProtKB:Q9H0U4}.
MOD_RES 201 201 Cysteine methyl ester. {ECO:0000255}.
LIPID 200 200 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:1648736}.
LIPID 201 201 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:1648736}.
MUTAGEN 21 21 K->M: Abolishes GTP-binding.
{ECO:0000269|PubMed:2509243}.
MUTAGEN 65 65 A->T: Reduced GTPase activity.
{ECO:0000269|PubMed:2509243}.
SEQUENCE 201 AA; 22163 MW; 8D3EEDC2AEF4A2FE CRC64;
MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ
IWDTAGQERF RTVTSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG
NKSDLTTKKV VDNTTAKEFA DSLGVPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG
GERPNLKIDS TPVKSASGGC C


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