RAB4B_CANLF
ID RAB4B_CANLF Reviewed; 213 AA.
AC P61017; P22750;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ras-related protein Rab-4B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20338};
GN Name=RAB4B;
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: Small GTPase which cycles between an active GTP-bound and an
CC inactive GDP-bound state (By similarity). Protein transport. Probably
CC involved in vesicular traffic (By similarity). Acts as a regulator of
CC platelet alpha-granule release during activation and aggregation of
CC platelets (By similarity). {ECO:0000250|UniProtKB:P20338,
CC ECO:0000250|UniProtKB:Q91ZR1}.
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:P20338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P20338};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- PTM: Serotonylation of Gln-67 by TGM2 during activation and aggregation
CC of platelets leads to constitutive activation of GTPase activity.
CC {ECO:0000250|UniProtKB:Q91ZR1}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X56389; CAA39800.1; -; mRNA.
DR PIR; F36364; F36364.
DR RefSeq; NP_001003275.1; NM_001003275.3.
DR RefSeq; XP_013969478.1; XM_014114003.1.
DR AlphaFoldDB; P61017; -.
DR SMR; P61017; -.
DR IntAct; P61017; 1.
DR MINT; P61017; -.
DR STRING; 9612.ENSCAFP00000007571; -.
DR PaxDb; P61017; -.
DR Ensembl; ENSCAFT00030003681; ENSCAFP00030003264; ENSCAFG00030002004.
DR Ensembl; ENSCAFT00040018705; ENSCAFP00040016232; ENSCAFG00040010068.
DR Ensembl; ENSCAFT00845005358; ENSCAFP00845004269; ENSCAFG00845003023.
DR GeneID; 403956; -.
DR KEGG; cfa:403956; -.
DR CTD; 53916; -.
DR VEuPathDB; HostDB:ENSCAFG00845003023; -.
DR eggNOG; KOG0086; Eukaryota.
DR GeneTree; ENSGT00940000159399; -.
DR InParanoid; P61017; -.
DR Proteomes; UP000002254; Chromosome 1.
DR Bgee; ENSCAFG00000005083; Expressed in temporal lobe and 48 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProt.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0032593; C:insulin-responsive compartment; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046323; P:glucose import; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04113; Rab4; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041819; Rab4.
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; Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT CHAIN 2..213
FT /note="Ras-related protein Rab-4B"
FT /id="PRO_0000121098"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT BINDING 151..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT MOD_RES 67
FT /note="5-glutamyl serotonin"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR1"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20338"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT MOD_RES 213
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 213 AA; 23587 MW; 0C3D76DC3285DB98 CRC64;
MAETYDFLFK FLVIGSAGTG KSCLLHQFIE NKFKQDSNHT IGVEFGSRVV NVGGKTVKLQ
IWDTAGQERF RSVTRSYYRG AAGALLVYDI TSRETYNSLA AWLTDARTLA SPNIVVILCG
NKKDLDPERE VTFLEASRFA QENELMFLET SALTGENVEE AFLKCARTIL NKIDSGELDP
ERMGSGIQYG DASLRQLRQP RSAQAVAPQP CGC
