TRET1_APILI
ID TRET1_APILI Reviewed; 502 AA.
AC A9ZSY2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000303|PubMed:20035867};
DE Short=AmTRET1 {ECO:0000303|PubMed:20035867};
GN Name=Tret1 {ECO:0000312|EMBL:BAF96743.1};
OS Apis mellifera ligustica (Common honeybee) (Italian honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7469;
RN [1] {ECO:0000312|EMBL:BAF96743.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20035867; DOI=10.1016/j.ibmb.2009.12.006;
RA Kanamori Y., Saito Y., Hagiwara-Komoda Y., Tanaka D., Mitsumasu K.,
RA Kikuta S., Watanabe M., Cornette R., Kikawada T., Okuda T.;
RT "The trehalose transporter 1 gene sequence is conserved in insects and
RT encodes proteins with different kinetic properties involved in trehalose
RT import into peripheral tissues.";
RL Insect Biochem. Mol. Biol. 40:30-37(2010).
CC -!- FUNCTION: Moderate-capacity facilitative transporter for trehalose.
CC Does not transport maltose, sucrose or lactose. Mediates the
CC bidirectional transfer of trehalose. Responsible for the transport of
CC trehalose synthesized in the fat body and the incorporation of
CC trehalose into other tissues that require a carbon source, thereby
CC regulating trehalose levels in the hemolymph.
CC {ECO:0000269|PubMed:20035867}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.42 mM for trehalose {ECO:0000269|PubMed:20035867};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20035867};
CC Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:20035867}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Trehalose transporter subfamily.
CC {ECO:0000255, ECO:0000269|PubMed:20035867}.
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DR EMBL; AB369549; BAF96743.1; -; mRNA.
DR RefSeq; NP_001107211.1; NM_001113739.1.
DR RefSeq; XP_006570642.1; XM_006570579.2.
DR AlphaFoldDB; A9ZSY2; -.
DR SMR; A9ZSY2; -.
DR GeneID; 551643; -.
DR KEGG; ame:551643; -.
DR CTD; 100141437; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051119; F:sugar transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015574; F:trehalose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015771; P:trehalose transport; IDA:UniProtKB.
DR CDD; cd17358; MFS_GLUT6_8_Class3_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR044775; MFS_ERD6/Tret1-like.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..502
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395539"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..83
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..433
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 502 AA; 55517 MW; C43F96A09779542E CRC64;
MGVENTKQTM SSQNIKPAKD SDDVLHTQFK EVKRSPMRYT MQLLAALAVS MASLMIGYSS
SYTSPALVSM RDNTTATFEV TMDMAMWIGS IMPLSALIGG IIGGPCIEYI GRRNTILSTA
LPFLAGWLFI ALATNVAMIL VGRSICGFCV GVASLSLPVY LGESIQPEVR GSLGLLPTVF
GNSGILMCFT AGMYLAWRNL ALLGACIPII FLILMFLIPE TPRWYISKGK IKEARKSLQW
LRGKTADISE ELDSIQKMHI ESERIATEGA LIELFRKNHI KPVFISLGLM FFQQFSGINA
VIFYTVQIFK DSGSTVDENL STIIVGLVNF ISTFVAAMII DRLGRKMLLY ISSILMCITL
FTFGTFFYVK ELMDVTAFGW IPLMSLIVYV IGFSFGFGPI PWLMMGEILP VKIRGTAASV
ATAFNWSCTF VVTKTYEDLV LHIGPYGTFW LFGTLVAVAF IFVIICVPET RGRSLEEIER
RFAGPVRRTS AIANLKPMPI TI
