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Identification
HMDB Protein ID HMDBP00374
Secondary Accession Numbers
  • 5611
Name Trehalase
Synonyms
  1. Alpha,alpha-trehalase
  2. Alpha,alpha-trehalose glucohydrolase
Gene Name TREH
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose.
Pathways
  • Starch and sucrose metabolism
  • Trehalose Degradation
Reactions
Trehalose + Water → D-Glucose + alpha-D-Glucose details
Trehalose + Water → D-Glucose details
GO Classification
Biological Process
small molecule metabolic process
trehalose catabolic process
polysaccharide digestion
Cellular Component
anchored to plasma membrane
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing o-glycosyl compounds
trehalase activity
alpha,alpha-trehalase activity
Molecular Function
alpha,alpha-trehalase activity
Process
metabolic process
primary metabolic process
carbohydrate metabolic process
oligosaccharide metabolic process
disaccharide metabolic process
trehalose metabolic process
Cellular Location
  1. Cell membrane
  2. Lipid-anchor
  3. GPI-anchor
Gene Properties
Chromosome Location 11
Locus 11q23.3
SNPs TREH
Gene Sequence
>1752 bp
ATGCCAGGGAGGACCTGGGAGCTGTGCCTGCTACTGCTGCTGGGGCTGGGACTGGGGTCC
CAGGAGGCCCTACCCCCACCCTGTGAGAGTGAGATTTACTGCCACGGGGAGCTCCTAAAC
CAAGTTCAAATGGCCAAGCTCTACCAGGATGACAAGCAGTTTGTGGACATGCCACTGTCT
ATAGCTCCAGAACAAGTCCTGCAGACCTTCACTGAGCTGTCCAGGGACCACAATCACAGC
ATCCCCAGGGAGCAGCTGCAGGCGTTTGTCCACGAACACTTCCAGGCCAAGGGGCAGGAG
CTGCAGCCCTGGACCCCTGCAGACTGGAAAGACAGCCCCCAGTTCCTGCAGAAGATTTCA
GATGCCAAACTGCGTGCCTGGGCAGGGCAGCTGCATCAGCTCTGGAAGAAGCTGGGGAAG
AAGATGAAGCCAGAGGTTCTCAGCCACCCTGAGCGGTTCTCTCTCATATACTCAGAACAT
CCTTTCATTGTGCCTGGCGGTCGCTTTGTTGAGTTCTACTACTGGGACTCCTACTGGGTC
ATGGAGGGTCTGCTCCTCTCAGAGATGGCTGAGACGGTGAAGGGCATGCTGCAGAACTTC
TTGGACCTGGTGAAAACCTATGGGCATGTCCCCAATGGTGGGCGCGTGTACTACTTGCAG
CGGAGCCAGCCCCCACTCTTGACCCTCATGATGGATTGCTACTTGACTCACACCAATGAC
ACCGCCTTTCTACAGGAAAACATTGAAACACTAGCCTTGGAATTGGACTTTTGGACCAAG
AACAGGACTGTCTCTGTGAGCTTGGAGGGAAAGAACTACCTCCTGAATCGCTATTATGTC
CCTTATGGGGGACCCAGGCCTGAGTCCTACAGCAAAGATGTGGAGTTGGCTGACACCTTG
CCAGAAGGAGACCGGGAGGCTCTGTGGGCTGAGCTCAAGGCTGGGGCTGAGTCTGGCTGG
GACTTCTCTTCACGCTGGCTCATTGGAGGCCCAAACCCCAACTCGCTTAGCGGCATCCGA
ACAAGCAAACTGGTGCCTGTTGACCTGAATGCCTTCCTATGCCAAGCAGAGGAGCTGATG
AGCAACTTCTATTCCAGGCTGGGGAACGACTCCCAGGCCACGAAGTACAGAATCCTGCGG
TCGCAGCGCTTGGCCGCCCTGAACACAGTCCTGTGGGATGAGCAGACCGGAGCCTGGTTC
GATTACGACCTTGAGAAGAAGAAGAAAAACCGGGAGTTTTACCCATCCAACCTCACTCCA
CTCTGGGCCGGGTGTTTCTCTGACCCTGGCGTGGCGGACAAGGCTCTGAAATACCTGGAG
GACAACCGGATCCTGACTTACCAGTATGGGATCCCGACCTCTCTCCAGAAGACAGGCCAG
CAGTGGGATTTCCCCAATGCCTGGGCCCCCCTGCAGGACTTGGTCATCAGAGGCCTGGCC
AAGGCACCTTTACGTCGGGCCCAGGAAGTGGCTTTCCAGCTGGCTCAGAATTGGATCCGA
ACCAATTTTGATGTCTACTCGCAGAAGTCAGCCATGTATGAGAAGTATGACGTCAGCAAC
GGTGGACAGCCCGGTGGGGGAGGAGAATATGAAGTTCAGGAGGGATTTGGCTGGGACGAA
GGTGTGGTCCTGATGCTGCTGGACCGCTATGGTGACCGGCTGACCTCAGGGGCCAAGCTG
GCTTTCCTGGAGCCCCACTGCCTGGCGGCCACCCTTCTGCCCAGCCTCCTGCTCAGCCTC
CTGCCATGGTGA
Protein Properties
Number of Residues 583
Molecular Weight 66567.26
Theoretical pI 5.678
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Trehalase
MPGRTWELCLLLLLGLGLGSQEALPPPCESEIYCHGELLNQVQMAKLYQDDKQFVDMPLS
IAPEQVLQTFTELSRDHNHSIPREQLQAFVHEHFQAKGQELQPWTPADWKDSPQFLQKIS
DAKLRAWAGQLHQLWKKLGKKMKPEVLSHPERFSLIYSEHPFIVPGGRFVEFYYWDSYWV
MEGLLLSEMAETVKGMLQNFLDLVKTYGHVPNGGRVYYLQRSQPPLLTLMMDCYLTHTND
TAFLQENIETLALELDFWTKNRTVSVSLEGKNYLLNRYYVPYGGPRPESYSKDVELADTL
PEGDREALWAELKAGAESGWDFSSRWLIGGPNPNSLSGIRTSKLVPVDLNAFLCQAEELM
SNFYSRLGNDSQATKYRILRSQRLAALNTVLWDEQTGAWFDYDLEKKKKNREFYPSNLTP
LWAGCFSDPGVADKALKYLEDNRILTYQYGIPTSLQKTGQQWDFPNAWAPLQDLVIRGLA
KAPLRRAQEVAFQLAQNWIRTNFDVYSQKSAMYEKYDVSNGGQPGGGGEYEVQEGFGWTN
GVVLMLLDRYGDRLTSGAKLAFLEPHCLAATLLPSLLLSLLPW
GenBank ID Protein 2789461
UniProtKB/Swiss-Prot ID O43280
UniProtKB/Swiss-Prot Entry Name TREA_HUMAN
PDB IDs Not Available
GenBank Gene ID AB000824
GeneCard ID TREH
GenAtlas ID TREH
HGNC ID HGNC:12266
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Ishihara R, Taketani S, Sasai-Takedatsu M, Kino M, Tokunaga R, Kobayashi Y: Molecular cloning, sequencing and expression of cDNA encoding human trehalase. Gene. 1997 Nov 20;202(1-2):69-74. [PubMed:9427547 ]
  3. Sasai-Takedatsu M, Taketani S, Nagata N, Furukawa T, Tokunaga R, Kojima T, Kobayashi Y: Human trehalase: characterization, localization, and its increase in urine by renal proximal tubular damage. Nephron. 1996;73(2):179-85. [PubMed:8773341 ]