GBP6_PONAB
ID GBP6_PONAB Reviewed; 633 AA.
AC Q5R9T9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Guanylate-binding protein 6;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P32455};
DE AltName: Full=GTP-binding protein 6;
DE Short=GBP-6;
DE AltName: Full=Guanine nucleotide-binding protein 6;
GN Name=GBP6;
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 {ECO:0000250|UniProtKB:A0A0G2JDV3, ECO:0000250|UniProtKB:P32455}.
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 -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:A0A0G2JDV3}.
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; CR859293; CAH91471.1; -; mRNA.
DR RefSeq; NP_001125866.1; NM_001132394.1.
DR AlphaFoldDB; Q5R9T9; -.
DR SMR; Q5R9T9; -.
DR STRING; 9601.ENSPPYP00000001356; -.
DR GeneID; 100172797; -.
DR KEGG; pon:100172797; -.
DR CTD; 163351; -.
DR eggNOG; KOG2037; Eukaryota.
DR InParanoid; Q5R9T9; -.
DR OrthoDB; 1027269at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISS:CAFA.
DR GO; GO:0042742; P:defense response to bacterium; ISS:CAFA.
DR GO; GO:0006955; P:immune response; ISS:CAFA.
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 Antimicrobial; Cytoplasmic vesicle; GTP-binding; Hydrolase; Immunity;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..633
FT /note="Guanylate-binding protein 6"
FT /id="PRO_0000313812"
FT DOMAIN 35..277
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..310
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"
SQ SEQUENCE 633 AA; 72364 MW; B29DD1EE666DD76F CRC64;
MESGPKMLAP ICLVENNNEQ LLVNQQAIQI LEKISQPVVV VAIVGLYRTG KSYLMNHLAG
QNHGFPLGST VQSETKGIWM WCVPHPSKPN HTLVLLDTEG LGDVEKGDPK NDSWIFALAV
LLCSTFIYNS MSTINHQALE QLHYVTELTE LIKAKSSPRP DGVDDSTEFV SFFPDFIWTV
RDFTLELKLN GHPITEDEYL ENALKLIQGN NPRVQTSNLP RECIRRFFPK RKCFIFDRPT
NDKDLLANIE KVSEKQLDPK FQEQTNIFSS YIFTHARTKT LREGIIVTGN RLGTLAVTYV
EAVNSGAVPC LENAVITLAQ RENSAAVQRA ADYYSQQMAQ RVKFPTDTLQ ELLDMHAACE
REAIAIFMEH SFKDENQEFQ KKFMETTMNK KGDFLLQNEE SSVQYCQAKL NELSKGLMES
ISAGSFSVPG GHKLYMETKE RIEQDYWQVP RKGVKAKEVF QRFLESQVVI EESILQSDKA
LTDREKAVAV DRAKKEAAEK EQELLKQKLQ EQQQQMEAQD KSLKENIAQL KQKLQMEREQ
LLREQIMMLE HTQKVQNDWL HEGFKKKYEE MNAEISQFKR MIDITKNDDT PWIARTLDKL
ADELTAVLSA PAKLIGHGVK GVSSLFKKHK LPF