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RAP2B_RAT
ID   RAP2B_RAT               Reviewed;         183 AA.
AC   P61227; P17964; Q96EG5; Q9CXG0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Ras-related protein Rap-2b;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P10114};
DE   Flags: Precursor;
GN   Name=Rap2b;
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=Wistar; TISSUE=Brain;
RA   Zhou J., Asada S., Fukamizu A., Kimura S., Kasuya Y.;
RT   "Rat RAP2B, member of ras oncogene family (RAP2B), mRNA sequence.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Small GTP-binding protein which cycles between a GDP-bound
CC       inactive and a GTP-bound active form. Involved in EGFR and CHRM3
CC       signaling pathways through stimulation of PLCE1. May play a role in
CC       cytoskeletal rearrangements and regulate cell spreading through
CC       activation of the effector TNIK. May regulate membrane vesiculation in
CC       red blood cells (By similarity). {ECO:0000250}.
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:P10114};
CC   -!- SUBUNIT: Interacts with PLCE1. Interacts with SGSM1, SGSM2 and SGSM3.
CC       The GTP-bound form of RAP2B interacts with RUNDC3A (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor;
CC       Cytoplasmic side. Note=Associated with red blood cells-released
CC       vesicles. {ECO:0000250}.
CC   -!- DOMAIN: The effector domain mediates the interaction with RUNDC3A.
CC       {ECO:0000250}.
CC   -!- PTM: Palmitoylated. Unlike RAP2A and RAP2C, palmitoylation of RAP2B is
CC       not required for association with recycling endosome membranes and
CC       activation of TNIK. {ECO:0000250|UniProtKB:P61226}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; AF386786; AAK66772.1; -; mRNA.
DR   RefSeq; NP_596901.1; NM_133410.1.
DR   AlphaFoldDB; P61227; -.
DR   SMR; P61227; -.
DR   BioGRID; 251033; 1.
DR   IntAct; P61227; 1.
DR   MINT; P61227; -.
DR   STRING; 10116.ENSRNOP00000019340; -.
DR   PaxDb; P61227; -.
DR   PRIDE; P61227; -.
DR   Ensembl; ENSRNOT00000106354; ENSRNOP00000092035; ENSRNOG00000065432.
DR   GeneID; 170923; -.
DR   KEGG; rno:170923; -.
DR   UCSC; RGD:620591; rat.
DR   CTD; 5912; -.
DR   RGD; 620591; Rap2b.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000160283; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; P61227; -.
DR   OMA; IEDCFRT; -.
DR   OrthoDB; 1353024at2759; -.
DR   PhylomeDB; P61227; -.
DR   TreeFam; TF313014; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:P61227; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000014420; Expressed in frontal cortex and 19 other tissues.
DR   Genevisible; P61227; RN.
DR   GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR   GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; ISO:RGD.
DR   GO; GO:0005525; F:GTP binding; ISO:RGD.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR   GO; GO:0030168; P:platelet activation; ISO:RGD.
DR   GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:RGD.
DR   GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0061097; P:regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR   CDD; cd04176; Rap2; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041840; Rap2.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR020849; Small_GTPase_Ras-type.
DR   PANTHER; PTHR24070; PTHR24070; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Palmitate; Prenylation; Reference proteome.
FT   CHAIN           1..180
FT                   /note="Ras-related protein Rap-2b"
FT                   /id="PRO_0000030219"
FT   PROPEP          181..183
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61226"
FT                   /id="PRO_0000030220"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         180
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P61226"
FT   LIPID           176
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P61226"
FT   LIPID           177
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P61226"
FT   LIPID           180
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P61226"
SQ   SEQUENCE   183 AA;  20504 MW;  A1139C2D5E7F5865 CRC64;
     MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
     TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYERVP MILVGNKVDL
     EGEREVSYGE GKALAEEWSC PFMETSAKNK ASVDELFAEI VRQMNYAAQP NGDEGCCSAC
     VIL
 
 
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