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RHOC_CHICK
ID   RHOC_CHICK              Reviewed;         193 AA.
AC   Q9PSX7;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Rho-related GTP-binding protein RhoC;
DE   Flags: Precursor;
GN   Name=RHOC; Synonyms=ARHC;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ADP-RIBOSYLATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Hamburger-Hamilton; TISSUE=Embryo;
RX   PubMed=9811589; DOI=10.1242/dev.125.24.5055;
RA   Liu J.-P., Jessell T.M.;
RT   "A role for rhoB in the delamination of neural crest cells from the dorsal
RT   neural tube.";
RL   Development 125:5055-5067(1998).
CC   -!- FUNCTION: Regulates a signal transduction pathway linking plasma
CC       membrane receptors to the assembly of focal adhesions and actin stress
CC       fibers. Serves as a microtubule-dependent signal that is required for
CC       the myosin contractile ring formation during cell cycle cytokinesis.
CC       Regulates apical junction formation in bronchial epithelial cells (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow
CC       {ECO:0000250}. Note=Translocates to the equatorial region before furrow
CC       formation in a ECT2-dependent manner. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Detected in embryonic notochord.
CC       {ECO:0000269|PubMed:9811589}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; AF098514; AAD12256.1; -; mRNA.
DR   RefSeq; NP_001025020.1; NM_001029849.1.
DR   PDB; 4D0B; X-ray; 2.80 A; C=60-69.
DR   PDBsum; 4D0B; -.
DR   AlphaFoldDB; Q9PSX7; -.
DR   SMR; Q9PSX7; -.
DR   STRING; 9031.ENSGALP00000002383; -.
DR   PaxDb; Q9PSX7; -.
DR   Ensembl; ENSGALT00000002385; ENSGALP00000002383; ENSGALG00000001569.
DR   GeneID; 395869; -.
DR   KEGG; gga:395869; -.
DR   CTD; 389; -.
DR   VEuPathDB; HostDB:geneid_395869; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   GeneTree; ENSGT00950000182945; -.
DR   HOGENOM; CLU_041217_21_2_1; -.
DR   InParanoid; Q9PSX7; -.
DR   OMA; KINACAY; -.
DR   OrthoDB; 1166960at2759; -.
DR   PhylomeDB; Q9PSX7; -.
DR   Reactome; R-GGA-416482; G alpha (12/13) signalling events.
DR   Reactome; R-GGA-416572; Sema4D induced cell migration and growth-cone collapse.
DR   Reactome; R-GGA-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-GGA-5627117; RHO GTPases Activate ROCKs.
DR   Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-GGA-9013106; RHOC GTPase cycle.
DR   PRO; PR:Q9PSX7; -.
DR   Proteomes; UP000000539; Chromosome 26.
DR   Bgee; ENSGALG00000001569; Expressed in heart and 12 other tissues.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; 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:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0043297; P:apical junction assembly; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   PANTHER; PTHR24072; PTHR24072; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Cell membrane; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..190
FT                   /note="Rho-related GTP-binding protein RhoC"
FT                   /id="PRO_0000276771"
FT   PROPEP          191..193
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000276772"
FT   MOTIF           34..42
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         41
FT                   /note="ADP-ribosylasparagine; by botulinum toxin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         190
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           190
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:4D0B"
SQ   SEQUENCE   193 AA;  21973 MW;  358E9BD3AE3813A6 CRC64;
     MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG KQVELALWDT
     AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
     LRNDEHTRRE LAKMKQEPVK PEEGRDMANR INAFGYLECS AKTKEGVREV FEMATRAGLQ
     VRKNKKRRGC PLL
 
 
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