TREA_RABIT
ID TREA_RABIT Reviewed; 578 AA.
AC P19813;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Trehalase {ECO:0000303|PubMed:1697585};
DE EC=3.2.1.28 {ECO:0000269|PubMed:1697585};
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE Flags: Precursor;
GN Name=TREH; Synonyms=TREA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white;
RX PubMed=1697585; DOI=10.1016/s0021-9258(18)77220-7;
RA Ruf J., Wacker H., James P., Maffia M., Seiler P., Galand G.,
RA von Kieckebusch A., Semenza G., Mantei N.;
RT "Rabbit small intestinal trehalase. Purification, cDNA cloning, expression,
RT and verification of glycosylphosphatidylinositol anchoring.";
RL J. Biol. Chem. 265:15034-15039(1990).
CC -!- FUNCTION: Intestinal trehalase is probably involved in the hydrolysis
CC of ingested trehalose. {ECO:0000269|PubMed:1697585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC Evidence={ECO:0000269|PubMed:1697585};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:1697585}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1697585};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1697585}.
CC -!- TISSUE SPECIFICITY: Expressed in small intestine, kidney, and to a
CC lesser extent in liver. {ECO:0000269|PubMed:1697585}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; M55299; AAA63460.1; -; mRNA.
DR PIR; A35810; A35810.
DR RefSeq; NP_001075759.1; NM_001082290.1.
DR AlphaFoldDB; P19813; -.
DR SMR; P19813; -.
DR STRING; 9986.ENSOCUP00000008775; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR GeneID; 100009126; -.
DR KEGG; ocu:100009126; -.
DR CTD; 11181; -.
DR eggNOG; KOG0602; Eukaryota.
DR InParanoid; P19813; -.
DR OrthoDB; 417479at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:UniProtKB.
DR GO; GO:0005993; P:trehalose catabolic process; IDA:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001661; Glyco_hydro_37.
DR InterPro; IPR018232; Glyco_hydro_37_CS.
DR PANTHER; PTHR23403; PTHR23403; 1.
DR Pfam; PF01204; Trehalase; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS00927; TREHALASE_1; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..555
FT /note="Trehalase"
FT /id="PRO_0000012055"
FT PROPEP 556..578
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012056"
FT ACT_SITE 321
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT ACT_SITE 514
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 175..176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 221..223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 286..288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 528
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT LIPID 555
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 578 AA; 65517 MW; 9014B1189818CEAC CRC64;
MPGSTWELHL LLLLGLGLGS EQALPPPCES QIYCHGELLH QVQMARLYPD DKQFVDMPLS
TAPDQVLQSF AELAATYNNT VPREQLEKFV QEHFQAVGQE LESWTPGDWK ESPQFLQKIS
DPKLRAWAEQ LHLLWKKLGK KIKPEVLSQP ERFSLIYSQH PFIVPGGRFV EFYYWDSYWV
MEGLLLSEMA ETVKGMLQNF LDLVTAYGHI PNGGRVYYLQ RSQPPLLTLM MDRYVAHTGD
LAFLRENIET LALELDFWAE NRTISVSSGG NSHTLNRYHV PYGGPRPESY SKDTELAHTL
PEGSWETLWA ELKAGAESGW DFSSRWLVGS PNPDSLGSIR TSKLVPVDLN AFLCQAEELL
SGFYSRLGNE SQATKYRNLR AQRIAALTAL LWDEDKGAWF DYDLENQKKN HEFYPSNLTP
LWAGCFSDPA IADKALQYLQ DSQILNHRHG IPTSLQNTGQ QWDFPNAWAP LQDLVIRGLA
KSPSARTQEV AFQLAQNWIR TNFDVYSQRS AMYEKYDISN AQPGGGGEYE VQEGFGWTNG
VALMLLDRYG DRLSSGTQLA LLEPHCLAAA LLLSFLTR
