GBP2_RAT
ID GBP2_RAT Reviewed; 589 AA.
AC Q63663;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Guanylate-binding protein 1;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P32456};
DE AltName: Full=GTP-binding protein 2;
DE Short=GBP-2;
DE AltName: Full=Guanine nucleotide-binding protein 2;
DE AltName: Full=Interferon-induced guanylate-binding protein 2;
DE AltName: Full=p67;
DE Flags: Precursor;
GN Name=Gbp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ISOPRENYLATION AT
RP CYS-586.
RX PubMed=8148370; DOI=10.1016/0167-4781(94)90284-4;
RA Asundi V.K., Stahl R.C., Showalter L., Conner K.J., Carey D.J.;
RT "Molecular cloning and characterization of an isoprenylated 67 kDa
RT protein.";
RL Biochim. Biophys. Acta 1217:257-265(1994).
CC -!- FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions,
CC but the major reaction product is GDP (By similarity). Exhibits
CC antiviral activity against influenza virus. Promotes oxidative killing
CC and delivers antimicrobial peptides to autophagolysosomes, providing
CC broad host protection against different pathogen classes (By
CC similarity). Confers protection to the protozoan pathogen Toxoplasma
CC gondii (By similarity). {ECO:0000250|UniProtKB:P32455,
CC ECO:0000250|UniProtKB:P32456, ECO:0000250|UniProtKB:Q9Z0E6}.
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:P32456};
CC -!- SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is
CC required for the association with membranous structures. Heterodimer
CC with other family members, including GBP1, GBP3, GBP4 and GBP5.
CC {ECO:0000250|UniProtKB:P32456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32456}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P32456}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P32456}. Membrane
CC {ECO:0000250|UniProtKB:P32456}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P32456}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q9Z0E6}. Note=GBP2-GBP5 dimers localize to the
CC Golgi apparatus. {ECO:0000250|UniProtKB:P32456}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8148370}.
CC -!- INDUCTION: By IFNG.
CC -!- PTM: Isoprenylation is required for proper subcellular location.
CC {ECO:0000250|UniProtKB:P32456}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA19909.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; M80367; AAA19909.1; ALT_INIT; mRNA.
DR PIR; S43506; S43506.
DR RefSeq; NP_598308.1; NM_133624.2.
DR AlphaFoldDB; Q63663; -.
DR SMR; Q63663; -.
DR BioGRID; 251165; 1.
DR STRING; 10116.ENSRNOP00000061437; -.
DR iPTMnet; Q63663; -.
DR PhosphoSitePlus; Q63663; -.
DR PaxDb; Q63663; -.
DR PRIDE; Q63663; -.
DR GeneID; 171164; -.
DR KEGG; rno:171164; -.
DR CTD; 2634; -.
DR RGD; 621810; Gbp2.
DR eggNOG; KOG2037; Eukaryota.
DR InParanoid; Q63663; -.
DR OrthoDB; 1027269at2759; -.
DR PRO; PR:Q63663; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044406; P:adhesion of symbiont to host; ISO:RGD.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0042832; P:defense response to protozoan; ISO:RGD.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
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 1: Evidence at protein level;
KW Antimicrobial; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW GTP-binding; Hydrolase; Immunity; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..586
FT /note="Guanylate-binding protein 1"
FT /id="PRO_0000190967"
FT PROPEP 587..589
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370784"
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 586
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 586
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:8148370"
SQ SEQUENCE 589 AA; 67109 MW; 5E52B79102C2D97F CRC64;
MASEIHMLQP MCLIENTEAH LVINQEALRI LSAINQPVVV VAIVGLYRTG KSYLMNKLAG
KRTGFSLGST VQSHTKGIWM WCVPHPKKAG QTLVLLDTEG LEDVEKGDNQ NDCWIFALAV
LLSSTFVYNS MGTINQQAMD QLHYVTELTD LIKSKSSPDQ SGIDDSANFV GFFPTFVWAL
RDFSLELEVN GKLVTPDEYL EHSLTLKKGA DKKTKSFNEP RLCIRKFFPK RKCFIFDRPA
LRKQLCKLET LGEEELCSEF VEQVAEFTSY IFSYSAVKTL SGGIIVNGPR LKSLVQTYVG
AISSGSLPCM ESAVLTLAQI ENSAAVQKAI THYEEQMNQK IQMPTETLQE LLDLHRLIER
EAIEIFLKNS FKDVDQKFQT ELGNLLISKR DAFIKKNSDV SSAHCSDLIE DIFGPLEEEV
KQGTFSKPGG YFLFLQMRQE LEKKYNQAPG KGLEAEAVLK KYFESKEDIV ETLLKTDQSL
TEAAKEIEVE RIKAETAEAA NRELAEKQEK FELMMQQKEE SYQEHVRQLT EKMKEEQKKL
IEEQDNIIAL KLREQEKFLR EGYENESKKL LREIENMKRR QSPGKCTIL
