GBP1_CHLAE
ID GBP1_CHLAE Reviewed; 590 AA.
AC Q5D1D6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Guanylate-binding protein 1;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P32455};
DE AltName: Full=GTP-binding protein 1;
DE Short=GBP-1;
DE AltName: Full=Guanine nucleotide-binding protein 1;
DE AltName: Full=Interferon-induced guanylate-binding protein 1;
DE Flags: Precursor;
GN Name=GBP1;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Terajima M.;
RT "Cloning of African green monkey guanylate binding protein 1 cDNA.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions (By
CC similarity). Confers protection to several pathogens, including the
CC bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG
CC as well as the protozoan pathogen Toxoplasma gondii (By similarity).
CC Promotes IFN-gamma-mediated host defense against bacterial infections
CC by regulating bacteriolytic peptide generation via its interaction with
CC ubiquitin-binding protein SQSTM1, which delivers monoubiquitylated
CC proteins to autolysosomes for the generation of bacteriolytic peptides
CC (By similarity). Exhibits antiviral activity against influenza virus
CC (By similarity). {ECO:0000250|UniProtKB:P32455,
CC ECO:0000250|UniProtKB:Q01514}.
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;
CC Evidence={ECO:0000250|UniProtKB:P32455};
CC -!- SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is
CC required for the second hydrolysis step from GDP to GMP. Heterodimer
CC with other family members, including GBP2, GBP3, GBP4 and GBP5.
CC Dimerization regulates subcellular location to membranous structures
CC (By similarity). Interacts with SQSTM1 (By similarity).
CC {ECO:0000250|UniProtKB:P32455, ECO:0000250|UniProtKB:Q01514}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32455}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q01514}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P32455}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q01514}. Cell membrane
CC {ECO:0000250|UniProtKB:P32455}. Secreted
CC {ECO:0000250|UniProtKB:P32455}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q01514}. Note=Secreted from endothelial cells in
CC the cerebrospinal fluid, upon bacterial challenge and independently of
CC IFNG induction. Golgi membrane localization requires isoprenylation and
CC the presence of another IFNG-induced factor (By similarity).
CC {ECO:0000250|UniProtKB:Q01514}.
CC -!- PTM: Isoprenylation is required for proper subcellular location (By
CC similarity). {ECO:0000250|UniProtKB:P32455}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY920435; AAX13804.1; -; mRNA.
DR AlphaFoldDB; Q5D1D6; -.
DR SMR; Q5D1D6; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR CDD; cd16269; GBP_C; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR037684; GBP_C.
DR InterPro; IPR003191; Guanylate-bd/ATL_C.
DR InterPro; IPR036543; Guanylate-bd_C_sf.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02263; GBP; 1.
DR Pfam; PF02841; GBP_C; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Antiviral defense; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Hydrolase; Immunity;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Secreted.
FT CHAIN 1..587
FT /note="Guanylate-binding protein 1"
FT /id="PRO_0000250481"
FT PROPEP 588..590
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396776"
FT DOMAIN 35..276
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..309
FT /note="GTPase domain (Globular)"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 67..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT BINDING 97..101
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32455"
FT MOD_RES 587
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 587
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 590 AA; 67821 MW; 40B437B9038BACCE CRC64;
MASEIHMTGP MCLIENTNGR LMVNPEALKI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG
KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HVLVLLDTEG LGDVEKGDNQ NDSWIFALAI
LLSSTFVYNS MGTINQQAMD QLHYVTELTH RIRSKSSPDE NENEDSADFV SFFPDFVWTL
RDFSLDLEAD GQPITADEYL TYSLKLKKGT SEKDKTFNLP RLCIRKFFPK KKCFVFDRPV
HRKKLAQLEK LHDEELDPEF VQQVADFCSY IFSNSKTKTL SGGIKVNGPR LESLVLTYVN
AISSGDLPCM ENAVLALAQI ENSAAVQKAV AHYEQQMGQK VQLPTETLQE LLDLHRDSER
EAIEVFIRSS FKDVDHLFQK ELAAQLEKKR DDFCKQNQEA SSDRCSALLQ DIFSPLEEEV
KMGIYSKPGG YRLFIQKLQD LKKKYYEEPR KGIQAEEILQ TYLKSKESMT DAILQTDQTL
TEKEKEIEVE RVKAESAQAS TKMLQEIQRK NEQMMEQKER SYQEHLKQLT EKMERDRAQL
LKEQERTLAL KLQEQERLLK EGFQTESRKM QNEIQDLQKK MRQRRTCTIS
