TRET1_BOMMO
ID TRET1_BOMMO Reviewed; 505 AA.
AC A9ZSY3;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000303|PubMed:20035867};
DE Short=BmTRET1 {ECO:0000303|PubMed:20035867};
GN Name=Tret1 {ECO:0000312|EMBL:BAF96744.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000312|EMBL:BAF96744.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=p50T;
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: High-capacity facilitative transporter for trehalose. Does
CC not transport maltose, sucrose or lactose. Mediates the bidirectional
CC transfer of trehalose. Responsible for the transport of trehalose
CC synthesized in the fat body and the incorporation of trehalose into
CC other tissues that require a carbon source, thereby regulating
CC trehalose levels in the hemolymph. {ECO:0000269|PubMed:20035867}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=71.58 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 -!- TISSUE SPECIFICITY: Expressed in many larval tissues at a low level,
CC moderate levels of expression are seen in testis and head and highest
CC expression in muscle. {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; AB369550; BAF96744.1; -; mRNA.
DR RefSeq; NP_001108344.1; NM_001114872.1.
DR AlphaFoldDB; A9ZSY3; -.
DR SMR; A9ZSY3; -.
DR STRING; 7091.BGIBMGA003739-TA; -.
DR PRIDE; A9ZSY3; -.
DR GeneID; 100141437; -.
DR KEGG; bmor:100141437; -.
DR CTD; 100141437; -.
DR eggNOG; KOG0254; Eukaryota.
DR InParanoid; A9ZSY3; -.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..505
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395540"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..437
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 505 AA; 55529 MW; FAB47959FDB4A887 CRC64;
MEMEIKDENL RNSVPFVRQL STDSVKTKTE YDNEDGTPYK STTQKLFLWT QLLAAFAVSV
GSMNVGFSSG YTSPAVLTMN ITLDITKEEI TWVGGLMPLA ALVGGIVGGP LIEYLGRKKT
IMGTAVPFTI GWMLIANAIN VVMVFAGRVI CGVCVGIVSL AFPVYIGETI QPEVRGALGL
LPTAFGNTGI LLAFLVGSYL DWSNLAFFGA AIPVPFFLLM ILTPETPRWY VSKARVQEAR
KSLRWLRGKN VNIEKEMRDL TISQTESDRT GGNAFKQLFS KRYLPAVMIS LGLMLFQQLT
GINAVIFYAA SIFQMSGSSV DENLASIIIG VVNFISTFIA TMLIDRLGRK VLLYISSVAM
ITTLLALGAY FYLKQNHIDV TAYGWLPLAC LVIYVLGFSI GFGPIPWLML GEILPSKIRG
TAASLATGFN WTCTFIVTKT FQNIIDAIYM HGTLWLFAVI CIGGLLFVIF FVPETKGKSL
EEIEMKLTSG SRRVRNISKQ PENIC
