ID   RAB4B_RAT               Reviewed;         213 AA.
AC   P51146;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Ras-related protein Rab-4B;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P20338};
GN   Name=Rab4b;
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=Heart muscle;
RA   Schuermann A., Muehl-Zuerbes P., Lie C., Joost H.G.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
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; X78605; CAA55339.1; -; mRNA.
DR   PIR; S58279; S58279.
DR   RefSeq; NP_059051.1; NM_017355.1.
DR   RefSeq; XP_017445097.1; XM_017589608.1.
DR   AlphaFoldDB; P51146; -.
DR   SMR; P51146; -.
DR   IntAct; P51146; 1.
DR   MINT; P51146; -.
DR   STRING; 10116.ENSRNOP00000002052; -.
DR   PhosphoSitePlus; P51146; -.
DR   jPOST; P51146; -.
DR   PaxDb; 10116-ENSRNOP00000002052; -.
DR   Ensembl; ENSRNOT00000002052.4; ENSRNOP00000002052.3; ENSRNOG00000001500.7.
DR   Ensembl; ENSRNOT00055058013; ENSRNOP00055047853; ENSRNOG00055033560.
DR   Ensembl; ENSRNOT00060055897; ENSRNOP00060046233; ENSRNOG00060032248.
DR   Ensembl; ENSRNOT00065057438; ENSRNOP00065047279; ENSRNOG00065033404.
DR   GeneID; 50866; -.
DR   KEGG; rno:50866; -.
DR   UCSC; RGD:620931; rat.
DR   AGR; RGD:620931; -.
DR   CTD; 53916; -.
DR   RGD; 620931; Rab4b.
DR   eggNOG; KOG0086; Eukaryota.
DR   GeneTree; ENSGT00940000159399; -.
DR   HOGENOM; CLU_041217_23_1_1; -.
DR   InParanoid; P51146; -.
DR   OMA; ASQNICI; -.
DR   OrthoDB; 4819304at2759; -.
DR   PhylomeDB; P51146; -.
DR   TreeFam; TF300032; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR   Reactome; R-RNO-8875656; MET receptor recycling.
DR   PRO; PR:P51146; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000001500; Expressed in thymus and 20 other cell types or tissues.
DR   GO; GO:0032593; C:insulin-responsive compartment; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:SynGO.
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; ISO:RGD.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041819; Rab4.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47979; DRAB11-RELATED; 1.
DR   PANTHER; PTHR47979:SF17; RAS-RELATED PROTEIN RAB-4B; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; P51146; RN.
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_0000121101"
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;  23629 MW;  0C3D76DC328B0018 CRC64;
     MAETYDFLFK FLVIGSAGTG KSCLLHQFIE NKFKQDSNHT IGVEFGSRVV NVGGKTVKLQ
     IWDTAGQERF RSVTRSYYRG AAGALLVYDI TSRETYNSLA AWLTDARTLA SPNIVVILCG
     NKKDLDPERE VTFLEASRFA QENELMFLET SALTGENVEE AFLKCARTIL NKIDSGELDP
     ERMGSGIQYG DISLRQLRQP RSAQAVAPQP CGC
//