ID H0V5G3_CAVPO Unreviewed; 580 AA.
AC H0V5G3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Trehalase {ECO:0000256|ARBA:ARBA00019905, ECO:0000256|RuleBase:RU361180};
DE EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757, ECO:0000256|RuleBase:RU361180};
DE AltName: Full=Alpha-trehalose glucohydrolase {ECO:0000256|RuleBase:RU361180};
GN Name=TREH {ECO:0000313|Ensembl:ENSCPOP00000004893.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000004893.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000004893.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000004893.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001576,
CC ECO:0000256|RuleBase:RU361180};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC {ECO:0000256|ARBA:ARBA00005615, ECO:0000256|RuleBase:RU361180}.
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DR EMBL; AAKN02024813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003472700.1; XM_003472652.3.
DR AlphaFoldDB; H0V5G3; -.
DR STRING; 10141.ENSCPOP00000004893; -.
DR Ensembl; ENSCPOT00000005495.3; ENSCPOP00000004893.2; ENSCPOG00000005437.4.
DR GeneID; 100726401; -.
DR KEGG; cpoc:100726401; -.
DR CTD; 11181; -.
DR VEuPathDB; HostDB:ENSCPOG00000005437; -.
DR eggNOG; KOG0602; Eukaryota.
DR GeneTree; ENSGT00390000006949; -.
DR HOGENOM; CLU_006451_4_3_1; -.
DR InParanoid; H0V5G3; -.
DR OMA; NRYWDAS; -.
DR OrthoDB; 1329212at2759; -.
DR TreeFam; TF314239; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000005437; Expressed in adult mammalian kidney and 2 other cell types or tissues.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:Ensembl.
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; TREHALASE; 1.
DR PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR Pfam; PF01204; Trehalase; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00927; TREHALASE_1; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..580
FT /note="Trehalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003542483"
SQ SEQUENCE 580 AA; 66227 MW; 11E159CD50EA6CDC CRC64;
MAVRTWGLAL LLLLGLGSQE ALPPPCASQI YCYGELLHQV QMAKLYSDDK NFVDMSLSKD
PDQVLQSFRA LATAHNGSIP RQQLQEFVHQ HFRSVGQELL AWTPEDWKDS PQFLQRISDT
KLRAWAEDLH QIWKKLGKQI KPEVLSNPER FSLIYSKHPF IVPGGRFVEF YYWDSYWVME
GLLLSEMAET VKGMLQNFLD LVKTYGHIPN GGRIYYLQRS QPPLLTLMVD RYVAHTNNTA
FLRENIETLA LELDFWTVNR SVSVNLGGQN YTLNRYYVPY GGPRPESYSK DEELANTLPE
GDREALWSEL KAGAESGWDF SSRWLVESPN LDSLSSIQTS KRVPVDLNAF LCQAEELMSN
FYARLGDDVQ AARYKALRNQ RLTAMQAVLW DEQKGAWFDY DLENMKKNLE FYPSNLAPLW
AGCFSDPGVV DKAVKYLEDN QILTHQYGIP TSLHNTGQQW DFPNGWAPLQ DLVIRGLAKS
QSPQTQEVAF QLAQNWIRTN FDVYSQKSTM YEKYDVSRGQ AGGGGEYEVQ EGFGWTNGVA
LMLMDRYGDR LTSGTQLALL MPHCLAATFL FQLLLGFLSQ
//
