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RAP2C_BOVIN
ID   RAP2C_BOVIN             Reviewed;         183 AA.
AC   Q08DI5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Ras-related protein Rap-2c;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P10114};
DE   Flags: Precursor;
GN   Name=RAP2C;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-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. May play a role in cytoskeletal
CC       rearrangements and regulate cell spreading through activation of the
CC       effector TNIK. May play a role in SRE-mediated gene transcription (By
CC       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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Recycling endosome
CC       membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- PTM: Palmitoylated. Palmitoylation is required for association with
CC       recycling endosome membranes and activation of TNIK.
CC       {ECO:0000250|UniProtKB:Q8BU31}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; BC123730; AAI23731.1; -; mRNA.
DR   RefSeq; NP_001069168.1; NM_001075700.1.
DR   RefSeq; XP_005227569.1; XM_005227512.3.
DR   RefSeq; XP_005227570.1; XM_005227513.3.
DR   RefSeq; XP_010819712.1; XM_010821410.2.
DR   AlphaFoldDB; Q08DI5; -.
DR   SMR; Q08DI5; -.
DR   STRING; 9913.ENSBTAP00000005408; -.
DR   PaxDb; Q08DI5; -.
DR   PRIDE; Q08DI5; -.
DR   Ensembl; ENSBTAT00000005408; ENSBTAP00000005408; ENSBTAG00000004131.
DR   Ensembl; ENSBTAT00000068302; ENSBTAP00000061865; ENSBTAG00000004131.
DR   Ensembl; ENSBTAT00000079003; ENSBTAP00000066215; ENSBTAG00000004131.
DR   Ensembl; ENSBTAT00000080153; ENSBTAP00000059791; ENSBTAG00000004131.
DR   GeneID; 515181; -.
DR   KEGG; bta:515181; -.
DR   CTD; 57826; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004131; -.
DR   VGNC; VGNC:33721; RAP2C.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000157245; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; Q08DI5; -.
DR   OMA; QFTGINE; -.
DR   OrthoDB; 1353024at2759; -.
DR   TreeFam; TF313014; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000004131; Expressed in caput epididymis and 105 other tissues.
DR   ExpressionAtlas; Q08DI5; baseline and differential.
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: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; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
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   Cytoplasm; Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Palmitate; Prenylation;
KW   Reference proteome.
FT   CHAIN           1..180
FT                   /note="Ras-related protein Rap-2c"
FT                   /id="PRO_0000280802"
FT   PROPEP          181..183
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU31"
FT                   /id="PRO_0000280803"
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:Q8BU31"
FT   LIPID           176
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU31"
FT   LIPID           177
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU31"
FT   LIPID           180
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU31"
SQ   SEQUENCE   183 AA;  20745 MW;  6763385F76638324 CRC64;
     MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
     TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI VRVKRYEKVP LILVGNKVDL
     EPEREVMSSE GRALAQEWGC PFMETSAKSK SMVDELFAEI VRQMNYSSLP EKQDQCCTTC
     VVQ
 
 
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