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RALB_MACFA
ID   RALB_MACFA              Reviewed;         206 AA.
AC   Q4R379;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ras-related protein Ral-B;
DE            EC=3.6.5.2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=RALB; ORFNames=QtsA-18830;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Multifunctional GTPase involved in a variety of cellular
CC       processes including gene expression, cell migration, cell
CC       proliferation, oncogenic transformation and membrane trafficking.
CC       Accomplishes its multiple functions by interacting with distinct
CC       downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis
CC       of dense core vesicles (By similarity). Required both to stabilize the
CC       assembly of the exocyst complex and to localize functional exocyst
CC       complexes to the leading edge of migrating cells (By similarity).
CC       Required for suppression of apoptosis (By similarity). In late stages
CC       of cytokinesis, upon completion of the bridge formation between
CC       dividing cells, mediates exocyst recruitment to the midbody to drive
CC       abscission (By similarity). Involved in ligand-dependent receptor
CC       mediated endocytosis of the EGF and insulin receptors (By similarity).
CC       {ECO:0000250|UniProtKB:P11234, ECO:0000250|UniProtKB:P36860}.
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:0000305};
CC   -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC       and an active form bound to GTP. Activated by a guanine nucleotide-
CC       exchange factor (GEF) and inactivated by a GTPase-activating protein
CC       (GAP).
CC   -!- SUBUNIT: Interacts with EXOC2/Sec5 and EXOC8/Exo84. Interacts (via
CC       effector domain) with RALBP1. {ECO:0000250|UniProtKB:P11234}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11234};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P11234}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P11234}. Midbody {ECO:0000250|UniProtKB:P11234}.
CC       Note=During late cytokinesis, enriched at the midbody.
CC       {ECO:0000250|UniProtKB:P11234}.
CC   -!- PTM: Prenylation is essential for membrane localization.
CC       {ECO:0000250|UniProtKB:P11234}.
CC   -!- PTM: The farnesylated form confers resistance to the proapoptotic and
CC       anti-anchorage-dependent growth effects of some
CC       geranylgeranyltransferase I inhibitors. {ECO:0000250|UniProtKB:P11234}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; AB179387; BAE02438.1; -; mRNA.
DR   RefSeq; NP_001306496.1; NM_001319567.1.
DR   RefSeq; XP_005572982.2; XM_005572925.2.
DR   RefSeq; XP_005572983.1; XM_005572926.2.
DR   RefSeq; XP_015287459.1; XM_015431973.1.
DR   AlphaFoldDB; Q4R379; -.
DR   BMRB; Q4R379; -.
DR   SMR; Q4R379; -.
DR   IntAct; Q4R379; 1.
DR   STRING; 9541.XP_005572982.1; -.
DR   GeneID; 101925782; -.
DR   KEGG; mcf:101925782; -.
DR   CTD; 5899; -.
DR   VEuPathDB; HostDB:ENSMFAG00000038532; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   OrthoDB; 1259506at2759; -.
DR   Proteomes; UP000233100; Chromosome 12.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007265; P:Ras protein signal transduction; IEA:InterPro.
DR   GO; GO:0001928; P:regulation of exocyst assembly; ISS:UniProtKB.
DR   GO; GO:0060178; P:regulation of exocyst localization; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR028412; Ral.
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   PANTHER; PTHR24070:SF199; PTHR24070:SF199; 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   Apoptosis; Cell cycle; Cell division; Cell membrane; GTP-binding;
KW   Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Prenylation; Reference proteome.
FT   CHAIN           1..203
FT                   /note="Ras-related protein Ral-B"
FT                   /id="PRO_0000260755"
FT   PROPEP          204..206
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281350"
FT   REGION          180..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           43..51
FT                   /note="Effector region"
FT   BINDING         21..29
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..131
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         203
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           203
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  23379 MW;  E0AC95130FA7012C CRC64;
     MAANKSKGQS SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE
     EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKAEEDK
     IPLLVVGNKS DLEERRQVPV EEARSKAEEW GVQYVETSAK TRANVDKVFF DLMREIRTKK
     MSENKDKNGK KSGKNKKSFK ERCCLL
 
 
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