GOB1_CAEEL
ID GOB1_CAEEL Reviewed; 439 AA.
AC Q9XTQ5; Q95QD8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Trehalose-phosphatase;
DE EC=3.1.3.12 {ECO:0000269|PubMed:16197937};
DE AltName: Full=Trehalose-6-phosphate phosphatase {ECO:0000303|PubMed:16197937};
DE Short=TPP;
GN Name=gob-1 {ECO:0000312|WormBase:H13N06.3};
GN ORFNames=H13N06.3 {ECO:0000312|WormBase:H13N06.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=16197937; DOI=10.1016/j.ydbio.2005.08.027;
RA Kormish J.D., McGhee J.D.;
RT "The C. elegans lethal gut-obstructed gob-1 gene is trehalose-6-phosphate
RT phosphatase.";
RL Dev. Biol. 287:35-47(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=24992307; DOI=10.1371/journal.ppat.1004245;
RA Farelli J.D., Galvin B.D., Li Z., Liu C., Aono M., Garland M.,
RA Hallett O.E., Causey T.B., Ali-Reynolds A., Saltzberg D.J., Carlow C.K.,
RA Dunaway-Mariano D., Allen K.N.;
RT "Structure of the trehalose-6-phosphate phosphatase from Brugia malayi
RT reveals key design principles for anthelmintic drugs.";
RL PLoS Pathog. 10:E1004245-E1004245(2014).
CC -!- FUNCTION: Catalyzes the hydrolysis of trehalose 6-phosphate to
CC trehalose and phosphate; prevents the accumulation of toxic levels of
CC trehalose 6-phosphate. {ECO:0000269|PubMed:16197937,
CC ECO:0000269|PubMed:24992307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC Evidence={ECO:0000269|PubMed:16197937};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A8NS89};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:A8NS89};
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in
CC intestine.
CC -!- DEVELOPMENTAL STAGE: Expression first seen at the 8E cell stage in the
CC embryonic intestine. Expression continues to and includes adulthood.
CC Beginning at the comma stage, additional expression is seen in the head
CC and possibly in the hypodermis. By the twofold stage and continuing
CC into adulthood, expression becomes increasingly widespread, with strong
CC staining in the intestine, pharynx, hypodermis, body wall muscle, tail,
CC and unidentified head neurons. {ECO:0000269|PubMed:16197937}.
CC -!- DISRUPTION PHENOTYPE: Lethal at early larval stage. Mutant larvae show
CC intestinal defects, and a high proportion exhibit gut obstruction
CC (gob). No visible phenotype when gob-1 is down-regulated together with
CC the trehalose phosphate synthases tps-1 and tps-2.
CC {ECO:0000269|PubMed:16197937, ECO:0000269|PubMed:24992307}.
CC -!- SIMILARITY: Belongs to the gob-1 trehalose phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB17072.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX284606; CAB17072.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX284606; CAC70091.2; -; Genomic_DNA.
DR PIR; T23091; T23091.
DR RefSeq; NP_510559.1; NM_078158.5.
DR RefSeq; NP_510560.2; NM_078159.3.
DR AlphaFoldDB; Q9XTQ5; -.
DR SMR; Q9XTQ5; -.
DR STRING; 6239.H13N06.3a; -.
DR EPD; Q9XTQ5; -.
DR PaxDb; Q9XTQ5; -.
DR PeptideAtlas; Q9XTQ5; -.
DR EnsemblMetazoa; H13N06.3.1; H13N06.3.1; WBGene00001649.
DR GeneID; 181637; -.
DR KEGG; cel:CELE_H13N06.3; -.
DR UCSC; H13N06.3a; c. elegans.
DR CTD; 181637; -.
DR WormBase; H13N06.3; CE40416; WBGene00001649; gob-1.
DR eggNOG; ENOG502RY87; Eukaryota.
DR InParanoid; Q9XTQ5; -.
DR OrthoDB; 766517at2759; -.
DR PhylomeDB; Q9XTQ5; -.
DR PRO; PR:Q9XTQ5; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001649; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IDA:UniProtKB.
DR GO; GO:1901136; P:carbohydrate derivative catabolic process; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0005992; P:trehalose biosynthetic process; IDA:WormBase.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR041064; T6PP_helical.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF18572; T6PP_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..439
FT /note="Trehalose-phosphatase"
FT /id="PRO_0000450613"
FT ACT_SITE 165
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:A8NS89"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8NS89"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8NS89"
FT BINDING 282..284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A8NS89"
FT BINDING 373
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A8NS89"
SQ SEQUENCE 439 AA; 48721 MW; CD96BC4778E555DA CRC64;
MNCEKESQMT IASQSIEDFK ECLYQMQEAR KSVTNEILET GHIKADQVQI FKSTLEEMND
ERTSKNHIRD IHSRGTTFGI NIQDEIKGLQ KDHHFLDAFA VESDKENNSF ANVLKLCDLP
GLLSKFVDDE IRFEKEVAEC KAFLMDLIDT STTGGIKPLF ITDWDGTMKD YCSQYATNLQ
PAYSAIVMGV FSRLFTRAFA VLTAGPLRHP GILDLTALPI NGPVLFSGSW GREWWLGGRR
IVHDDGIPEE GSVAIGQLCE QLDEILHEGE FVQFALVGSG VQRKVDRLTL GVQTVFKQVP
EDLSARYIDA VRERIHRVDP NSQYLVLENC SPLEIEVCVH SSGAVWNKGD GVAALVESLH
DSLKVGKVCV AGDTASDVPM LKKAADENPE NVRALFVNIN KQLQENITNI VGDAKRVCFI
SSPDVAHAAF AQIISEFSG
