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RAP2A_PIG
ID   RAP2A_PIG               Reviewed;         183 AA.
AC   Q06AU2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu G.Y.;
RL   Submitted (AUG-2006) 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; DQ917633; ABI97178.1; -; mRNA.
DR   RefSeq; NP_001116657.1; NM_001123185.1.
DR   AlphaFoldDB; Q06AU2; -.
DR   SMR; Q06AU2; -.
DR   STRING; 9823.ENSSSCP00000010152; -.
DR   PaxDb; Q06AU2; -.
DR   PeptideAtlas; Q06AU2; -.
DR   PRIDE; Q06AU2; -.
DR   Ensembl; ENSSSCT00000050005; ENSSSCP00000058825; ENSSSCG00000038366.
DR   Ensembl; ENSSSCT00015016671; ENSSSCP00015006491; ENSSSCG00015012636.
DR   Ensembl; ENSSSCT00025035653; ENSSSCP00025014877; ENSSSCG00025026371.
DR   Ensembl; ENSSSCT00030070947; ENSSSCP00030032366; ENSSSCG00030050921.
DR   Ensembl; ENSSSCT00035034891; ENSSSCP00035013825; ENSSSCG00035026447.
DR   Ensembl; ENSSSCT00040066343; ENSSSCP00040028118; ENSSSCG00040049208.
DR   Ensembl; ENSSSCT00045045201; ENSSSCP00045031350; ENSSSCG00045026575.
DR   Ensembl; ENSSSCT00050043540; ENSSSCP00050017972; ENSSSCG00050032431.
DR   Ensembl; ENSSSCT00055015095; ENSSSCP00055011871; ENSSSCG00055007730.
DR   Ensembl; ENSSSCT00060027417; ENSSSCP00060011693; ENSSSCG00060020269.
DR   Ensembl; ENSSSCT00065057828; ENSSSCP00065025105; ENSSSCG00065042296.
DR   Ensembl; ENSSSCT00070006762; ENSSSCP00070005516; ENSSSCG00070003610.
DR   GeneID; 100144507; -.
DR   KEGG; ssc:100144507; -.
DR   CTD; 5912; -.
DR   VGNC; VGNC:92089; RAP2B.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000160283; -.
DR   InParanoid; Q06AU2; -.
DR   OMA; IEDCFRT; -.
DR   OrthoDB; 1353024at2759; -.
DR   Reactome; R-SSC-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008227; Chromosome 13.
DR   Proteomes; UP000314985; Chromosome 13.
DR   Bgee; ENSSSCG00000038366; Expressed in granulosa cell and 42 other tissues.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR   GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0070527; P:platelet aggregation; 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: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   GO; GO:0061097; P:regulation of protein tyrosine kinase activity; IEA:Ensembl.
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_0000281338"
FT   PROPEP          181..183
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q80ZJ1"
FT                   /id="PRO_0000281339"
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;  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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