RAP2A_PONAB
ID RAP2A_PONAB Reviewed; 183 AA.
AC Q5R988;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ras-related protein Rap-2a;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P10114};
DE Flags: Precursor;
GN Name=RAP2A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-183.
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. In its active form interacts with
CC and regulates several effectors including MAP4K4, MINK1 and TNIK. Part
CC of a signaling complex composed of NEDD4, RAP2A and TNIK which
CC regulates neuronal dendrite extension and arborization during
CC development. More generally, it is part of several signaling cascades
CC and may regulate cytoskeletal rearrangements, cell migration, cell
CC adhesion and cell spreading (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 -!- ACTIVITY REGULATION: Activated by the guanine nucleotide-exchange
CC factors RAPGEF3 and RAPGEF4 in a cAMP-dependent manner. Nucleotide
CC exchange is also specifically stimulated by RAPGEF5, RASGEF1A and
CC RASGEF1B (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with RUNDC3A. Interacts with PLCE1.
CC Interacts with ARHGAP29, SGSM1, SGSM2 and SGSM3. Interacts (GTP-bound
CC form preferentially) with TNIK (via the CNH domain); the interaction is
CC direct and recruits RAP2A to the E3 ubiquitin ligase NEDD4. Interacts
CC with MINK1. Interacts (GTP-bound form preferentially) with MAP4K4.
CC Interacts with cytoskeletal actin. Interacts with RGS14; the
CC interaction is GTP-dependent (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Midbody {ECO:0000250}. Recycling endosome
CC membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Localizes to midbody at telophase. May also
CC localize to the Golgi and the gelatinase-containing granules of
CC neutrophils. {ECO:0000250}.
CC -!- DOMAIN: The effector domain mediates the interaction with RUNDC3A.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-63' monoubiquitination and
CC diubiquitination by NEDD4. Multiple lysine residues are probably
CC modified. Ubiquitination requires TNIK, prevents interaction with
CC effectors and inactivates RAP2A (By similarity). {ECO:0000250}.
CC -!- PTM: Palmitoylated. Palmitoylation is required for association with
CC recycling endosome membranes and activation of TNIK.
CC {ECO:0000250|UniProtKB:Q80ZJ1}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; CR859503; CAH91672.1; -; mRNA.
DR AlphaFoldDB; Q5R988; -.
DR SMR; Q5R988; -.
DR STRING; 9601.ENSPPYP00000006222; -.
DR PRIDE; Q5R988; -.
DR Ensembl; ENSPPYT00000040236; ENSPPYP00000031621; ENSPPYG00000031802.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160594; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q5R988; -.
DR OrthoDB; 1353024at2759; -.
DR Proteomes; UP000001595; Chromosome 13.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR GO; GO:0030033; P:microvillus assembly; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; 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;
KW Ubl conjugation.
FT CHAIN 1..180
FT /note="Ras-related protein Rap-2a"
FT /id="PRO_0000082689"
FT PROPEP 181..183
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q80ZJ1"
FT /id="PRO_0000281340"
FT MOTIF 32..40
FT /note="Effector region"
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:Q80ZJ1"
FT LIPID 176
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q80ZJ1"
FT LIPID 177
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q80ZJ1"
FT LIPID 180
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q80ZJ1"
SQ SEQUENCE 183 AA; 20642 MW; A46054762765E431 CRC64;
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYEKVP VILVGNKVDL
ESEREVSSNE GRALAEEWGC PFMETSAKSK TMVDELFAEI VRQMNYAAQP DKDDPCCSAC
NIQ
