GBP1_PONAB
ID GBP1_PONAB Reviewed; 592 AA.
AC Q5RBE1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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}.
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DR EMBL; CR858710; CAH90919.1; -; mRNA.
DR RefSeq; NP_001125525.1; NM_001132053.1.
DR AlphaFoldDB; Q5RBE1; -.
DR SMR; Q5RBE1; -.
DR STRING; 9601.ENSPPYP00000001360; -.
DR GeneID; 100172437; -.
DR CTD; 2633; -.
DR eggNOG; KOG2037; Eukaryota.
DR InParanoid; Q5RBE1; -.
DR OrthoDB; 1027269at2759; -.
DR Proteomes; UP000001595; Unplaced.
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:0051607; P:defense response to virus; 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 Antiviral defense; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome; Secreted.
FT CHAIN 1..589
FT /note="Guanylate-binding protein 1"
FT /id="PRO_0000250482"
FT PROPEP 590..592
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396778"
FT DOMAIN 35..278
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..311
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 589
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 589
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 592 AA; 67876 MW; FBE4F484EA466797 CRC64;
MASEIHMTGP MCLIESTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG KSYLMNKLAG
KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG LGDVEKGDNQ NDSWIFALAV
LLSSTFVYNS IGTINQQAMD QLYYVTELTH RIRSKSSPDE NENEVEDSAD FVSFFPDFVW
TLRDFSLDLE ADGQPLTPDE YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR
PVHRRKLAQL EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY
VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTESL QELLDLHRDS
EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ EASSDRCSGL LQVIFSPLEE
EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE PRKGIQAEEI LQTYLKSKES MTDAILQTDQ
TLTEKEKEIE VERVKAESAQ ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV
QLLKEQERTL ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKACT IS
