TPS1_CAEEL
ID TPS1_CAEEL Reviewed; 1331 AA.
AC Q7YZT6; Q23515; Q2L6W2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1;
DE EC=2.4.1.15;
DE AltName: Full=Trehalose-6-phosphate synthase 1;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase 1;
GN Name=tps-1; Synonyms=tps1; ORFNames=ZK54.2;
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] (ISOFORM A), DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=13678635; DOI=10.1016/s0020-7519(03)00173-5;
RA Pellerone F.I., Archer S.K., Behm C.A., Grant W.N., Lacey M.J.,
RA Somerville A.C.;
RT "Trehalose metabolism genes in Caenorhabditis elegans and filarial
RT nematodes.";
RL Int. J. Parasitol. 33:1195-1206(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=15935281; DOI=10.1016/j.biochi.2005.01.010;
RA Goyal K., Browne J.A., Burnell A.M., Tunnacliffe A.;
RT "Dehydration-induced tps gene transcripts from an anhydrobiotic nematode
RT contain novel spliced leaders and encode atypical GT-20 family proteins.";
RL Biochimie 87:565-574(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC -!- FUNCTION: Catalyzes the production of trehalose from glucose-6-
CC phosphate and UDP-alpha-D-glucose in a 2 step process.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q7YZT6-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q7YZT6-2; Sequence=VSP_038112;
CC -!- DEVELOPMENTAL STAGE: Expressed in all development stages.
CC {ECO:0000269|PubMed:13678635}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:13678635}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the gob-1 trehalose
CC phosphatase family. {ECO:0000305}.
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DR EMBL; AJ512332; CAD54506.1; -; mRNA.
DR EMBL; AJ811573; CAH18875.1; -; mRNA.
DR EMBL; FO080803; CCD66907.1; -; Genomic_DNA.
DR EMBL; FO080803; CCD66908.1; -; Genomic_DNA.
DR RefSeq; NP_001041302.1; NM_001047837.2. [Q7YZT6-1]
DR RefSeq; NP_001041303.1; NM_001047838.2. [Q7YZT6-2]
DR AlphaFoldDB; Q7YZT6; -.
DR SMR; Q7YZT6; -.
DR BioGRID; 46653; 2.
DR STRING; 6239.ZK54.2a.3; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EPD; Q7YZT6; -.
DR PaxDb; Q7YZT6; -.
DR PeptideAtlas; Q7YZT6; -.
DR EnsemblMetazoa; ZK54.2a.1; ZK54.2a.1; WBGene00006602. [Q7YZT6-1]
DR EnsemblMetazoa; ZK54.2b.1; ZK54.2b.1; WBGene00006602. [Q7YZT6-2]
DR GeneID; 181778; -.
DR KEGG; cel:CELE_ZK54.2; -.
DR UCSC; ZK54.2b.3; c. elegans.
DR CTD; 181778; -.
DR WormBase; ZK54.2a; CE07617; WBGene00006602; tps-1. [Q7YZT6-1]
DR WormBase; ZK54.2b; CE30330; WBGene00006602; tps-1. [Q7YZT6-2]
DR eggNOG; KOG1050; Eukaryota.
DR GeneTree; ENSGT00940000167933; -.
DR InParanoid; Q7YZT6; -.
DR OMA; HYLAMDI; -.
DR OrthoDB; 772297at2759; -.
DR PRO; PR:Q7YZT6; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006602; Expressed in larva and 3 other tissues.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IBA:GO_Central.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProt.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd03788; GT20_TPS; 1.
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; PF00982; Glyco_transf_20; 1.
DR Pfam; PF18572; T6PP_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..1331
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 1"
FT /id="PRO_0000385176"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_038112"
SQ SEQUENCE 1331 AA; 150819 MW; 80A59C0D37783E75 CRC64;
MTDTATGVHS NANGVEKVPT PVFSIEGEPT QETAPTRMDP FDRPKNDNDP FEDALKRCHK
ILEKLDCPFV TGKEKDLDES DDMTENEDHD EMANEDDGIP SNEKKVETRK MDCTSGQLLA
PKLPEKAESI SSASESSEDS ESVAILKYTV RTCYAIWKKR QKNSEIALKG LMIVLELCLS
QPSARDDAFS ALLETLGYNT VTFWKAVVPQ IYNSDLSYAT QYREALLFSL VLYDVNHSKN
RLRELYAAVP GVRQSMLGIR AKQFGERYRH LQMKIARSRA SSRMSSKMGS EENLPAMASM
MNDVVFDEEP HTQSPLVDMS HDKQRVINVS NAPPVSISRK TSGSWEIKQG SGGLVACVDP
VMSADKKNIW LSNLGVNMQE ELKEHSTSTN SLGLPLIKQA CAGEVFCVLE RNEKKEELTP
KQQAVESDMS LLSVLNTYNK HSYQLNPVVV NQDDYNTYYG GISNGLLWPA LHNLPQYISP
CFDDPELLRE QWCAYVRVNY LFAINAARNS RAQDFIWIHD YHLMLCGQIM RSLESSLDIG
FFIHIPFQPP ANFMTKYKTV ADPIMRALLR FTKVGFQTSR DRDTFVKLVA KHIKRTKIEY
DSRLDRYTIE HDGWTCSLGV FPVSIKIADF VNIAKNPQTI IEAEEIKKQI MGRSADGGQL
FFSVERFDYT KGISEKLRAW QRYFEKYPDR IGKDVLFQVA VTNRRSVDSY RQYQDDVLAV
ADLINQKFKS EDYPEWKPVI FETDGLPRTR LIAHYLAMDI GVVTPSKDGM NLVAKEMLVC
NPTASLVLST GAGTEVQLSN AQFYSEQEGK CYHRVEEISN TEAFADNFFA AATESKETRT
KHGEKINQFL CVHDIDEWSD QFLDPKWTHE VISQCEVKQL GQFYGLMSRT AQVRRQIVEC
VLKGLPIRPH FRYSLENAKN SLESSCKSGT KLSLEADEES GEEKGFEITY DIHDELSEME
KDLAFLAFIQ SDEYENAEEF IKTLGSFYEG GPVLFKNEVK QAAEMLQQGI HYNTFFTDRD
GTLKSYACSY PTSVQPAYSA VIQAQFARRC ATFCAIVTTA PLLHTGILEV ATIPEGYYAY
GASAGREWYL NPAQQFKDRS FSAIDLNLMN KVFDIIEELL ERPEFRIFKW IGSGIQKHCG
HITIAKQDVN GTIPSRKVIR LYEQLVKIVN DFDPNGTTLT MRESDLDFKI YVKAKLKGRI
FNKGHGIRLV RERLKPNMSK GNCLVCGDNE SDIPMLEECL KLAGSKVYTI WVTADTNLQE
KVTQLCDRFS CSNIHFVSCP QVLLGAMAYA TAHTLVDERN RKLDYYYDSD TPMDQEESST
LGASLGTSFG N
