RAB8B_BOVIN
ID RAB8B_BOVIN Reviewed; 207 AA.
AC Q2HJI8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ras-related protein Rab-8B;
DE Flags: Precursor;
GN Name=RAB8B;
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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 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 may be involved in
CC polarized vesicular trafficking and neurotransmitter release. May
CC participate in cell junction dynamics in Sertoli cells (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Associated with actin, delta-catenin and alpha and beta
CC tubulins (By similarity). Interacts with OTOF (By similarity).
CC Interacts with PEX5R (By similarity). Interacts with RAB3IP (By
CC similarity). Interacts with VIM (By similarity). Interacts with CDH1
CC (By similarity). Interacts with MICALL2 (By similarity). Interacts with
CC GDI1, GDI2, CHML and CHM; phosphorylation at Thr-72 disrupts these
CC interactions (By similarity). {ECO:0000250|UniProtKB:P61028,
CC ECO:0000250|UniProtKB:P70550, ECO:0000250|UniProtKB:Q92930}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing
CC S.aureus or Mycobacterium. {ECO:0000250}.
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:Q92930}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC105330; AAI05331.1; -; mRNA.
DR RefSeq; NP_001069785.1; NM_001076317.1.
DR AlphaFoldDB; Q2HJI8; -.
DR SMR; Q2HJI8; -.
DR STRING; 9913.ENSBTAP00000014802; -.
DR PaxDb; Q2HJI8; -.
DR PRIDE; Q2HJI8; -.
DR GeneID; 614242; -.
DR KEGG; bta:614242; -.
DR CTD; 51762; -.
DR eggNOG; KOG0078; Eukaryota.
DR InParanoid; Q2HJI8; -.
DR OrthoDB; 1426655at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 membrane; Cytoplasmic vesicle; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..204
FT /note="Ras-related protein Rab-8B"
FT /id="PRO_0000253740"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370799"
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 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92930"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61028"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61028"
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; 23656 MW; 4A54ACA537242B04 CRC64;
MAKTYDYLFK LLLIGDSGVG KTCLLFRFSE DAFNTTFIST IGIDFKIRTI ELDGKKIKLQ
IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIK NWIRNIEEHA SSDVERMILG
NKCDMNDKRQ VSKERGEKLA IDYGIKFLEA SAKSSMNVEE AFFTLARDIM TKLNRKMNDS
NSSGAGGPVK ITENRSKKTS FFRCLLL
