(data stored in ACNUC4266 zone)

HOVERGEN: RASK_RIVMA

ID   RASK_RIVMA              Reviewed;         188 AA.
AC   Q5EFX7; Q5EFX6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   13-OCT-2009, entry version 30.
DE   RecName: Full=GTPase KRas;
DE   AltName: Full=Ki-Ras;
DE            Short=K-ras;
DE   Flags: Precursor;
GN   Name=kras;
OS   Rivulus marmoratus (Mangrove rivulus) (Kryptolebias marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Atherinomorpha;
OC   Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Lee Y.-M., Park E.-H., Lee J.-S.;
RT   "Tissue-specific alternative splicing of Ki-ras gene from the self-
RT   fertilizing fish Rivulus marmoratus (Cyprinodontiformes, Rivulidae).";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC       activity.
CC   -!- ENZYME REGULATION: Alternate between an inactive form bound to GDP
CC       and an active form bound to GTP. Activated by a guanine
CC       nucleotide-exchange factor (GEF) and inactivated by a GTPase-
CC       activating protein (GAP).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5EFX7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5EFX7-2; Sequence=VSP_015305, VSP_015306;
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
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CC   -!- GENE_FAMILY: HBG009351 [ FAMILY / ALN / TREE ]
DR   EMBL; AY886900; AAW78851.1; -; mRNA.
DR   EMBL; AY886901; AAW78852.1; -; mRNA.
DR   SMR; Q5EFX7; 1-166.
DR   HOVERGEN; Q5EFX7; -.
DR   GO; GO:0009898; C:internal side of plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR015592; Ras_Ras_related.
DR   InterPro; IPR005225; Small_GTP_bd.
DR   PANTHER; PTHR11708:SF125; Ras_Ras_related; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q5EFX7.
DR   SWISS-2DPAGE; Q5EFX7.
KW   Alternative splicing; Cell membrane; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Prenylation.
FT   CHAIN         1    185       GTPase KRas.
FT                                /FTId=PRO_0000082648.
FT   PROPEP      186    188       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000281298.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     116    119       GTP (By similarity).
FT   MOTIF        32     40       Effector region (By similarity).
FT   MOD_RES     185    185       Cysteine methyl ester (By similarity).
FT   LIPID       185    185       S-farnesyl cysteine (By similarity).
FT   VAR_SEQ     151    153       GVD -> RVE (in isoform 2).
FT                                /FTId=VSP_015305.
FT   VAR_SEQ     165    188       KHKEKMSKEGKKKKKKSKTKCILM -> QYRLSKISKEEKT
FT                                PGCVQLKKCVVM (in isoform 2).
FT                                /FTId=VSP_015306.
SQ   SEQUENCE   188 AA;  21527 MW;  58DD59FFAB219985 CRC64;
     MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKYDL
     PTRTVDTKQA QDLARSYGIP FIETSAKTRQ GVDDAFYTLV REIRKHKEKM SKEGKKKKKK
     SKTKCILM
//

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