ID E9AE73_LEIMA Unreviewed; 1757 AA.
AC E9AE73;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LMJF_29_2110 {ECO:0000313|EMBL:CBZ12552.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CBZ12552.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CBZ12552.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CBZ12552.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR796425; CBZ12552.1; -; Genomic_DNA.
DR RefSeq; XP_003722294.1; XM_003722246.1.
DR STRING; 5664.E9AE73; -.
DR EnsemblProtists; CBZ12552; CBZ12552; LMJF_29_2110.
DR GeneID; 12981073; -.
DR KEGG; lma:LMJF_29_2110; -.
DR VEuPathDB; TriTrypDB:LmjF.29.2110; -.
DR VEuPathDB; TriTrypDB:LMJFC_290030600; -.
DR VEuPathDB; TriTrypDB:LMJLV39_290029100; -.
DR VEuPathDB; TriTrypDB:LMJSD75_290029200; -.
DR eggNOG; KOG1879; Eukaryota.
DR HOGENOM; CLU_002668_1_0_1; -.
DR InParanoid; E9AE73; -.
DR OMA; TYRWPWW; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000542; Chromosome 29.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR CDD; cd06432; GT8_HUGT1_C_like; 1.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11226:SF0; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 28..280
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 405..518
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 583..836
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 1473..1748
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 134..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1757 AA; 192407 MW; B579FFD70DF51038 CRC64;
MLLILGPTAQ TTLGKGIWAA VEASWNETSL YQEGCEWVAR SFGDEAFYSC LDALWLPSPS
QDCGSSSADS EGAREATSAR FLTQQLQYMR LLEVLFRLPE TRGANRALFE AEMAARVYSP
AVEAHYALAD KALRETTPPP SLSERDDSDQ GERGSGNRLT CGDPFAVVYT RTAPGAPLRA
LRVKTPAALK RAAGGAGPQH RDAVVSIDEL AFASFDHRHP APLLAAVREV PAVVVLYGLP
GSPAAHALHR VAVELSNPSD VASATVSGAP AYFWRHLPVS VSRLCAAAGV REQSLAAAMT
SLWDSPLAVQ GYGVTVDIKN MEYKVLDEKA AAQQRSKEQS STAADKGSSH DGTDAPAAAK
RVPETQVGRI AGGFHVGRLK ERYPGLAASL DEFAILLDEE MGSDDVKVNF DVRELQKIGL
AATQYISEVE NHSRRLHVLT DMVMRFPTYA AALSRIAALP GRLVEVQKTL LILHQRMRPG
QSAFFVDGWR VEEKELTLFG VLQALHEEER LIRRMKTVLT TCAVAAADAD SAAEDAVHEA
RTVPLAPAVL EKVADYVKRT THRTIVSLED NADTEAAYAI PSEHIIWINN VETDPRFKRL
PPVLSILLAR GYVKTPLPRR NVLNFVFLWN PVSRSSLQMI FHMFRFHQEG LIARYGLALA
DQTWSPVFEA GVQGGGGGFK GESAGSQAAL QVFALVYHLV ATGKTNNVLV FLMELLEEAK
QARADTIPDA VISRVCTRTA RAKLNSDIGE LTSKANFLSH YHETQAALRR FRVPEYPATF
LNGVQLKNSM AGMSTALQRE MTLLRAWVAS GALRDGMKDM YSAILKQRGA ADHLQPALVR
GPVTMRWSDT PTTVAYIESL PYVYSASYAE EVPALTQLVT LPCKFTTAML QQLQTVMEAL
EECGVAAKSQ GAIHEVCGTL RLSLVSCPAA TSLFHRHIGA LQQQLARSST PKAARYTTLR
RYLSHIAEAM TSANVGVNAV LGTETVAAAL AAAPLPADLQ ALVGVSRSTD ANTSPQWARA
KVQFWSVFAD AYHGSAGNVA LVTNGRIVAM DASFSAADVL SAAGLVAPIT KAVQRAVMSV
RFDEMSTADG GYAADELDNN FFASKAACLS SVFGDDISQH MAKQSSSAPA LMREESILGP
ENDWKPLQAV LFTVSNVARN AGEEAGTASG AVAQPLHHVT VVVDPSSRDA QVIVSLAHYL
VQSSLHIRLT FLLNPSLDVK FPIRNFYQYV GSPALAFEET SGRVVAPHAT FSQMPSSTLL
TLGVDEPPSW TVFSQDAEVD LDNIMLSSLP RSTLFVTAVY RIHSVLVTGG TTDVQTGVAP
DGLPLSLLHS SRARGALEVA SAARTTDTQV MANQGGYYQL QANPGLWYLS IKEGPVAAAF
CIKAIEGHAV RGCAEGANGS LLTNWTQGQR IPLVIDSFRG RYLSLQVGHT PTSDATADLH
TILQQMASDV RLEWPPSHSV RDATPALPEK PTLNIFSVAS GHLYERFLRM MMYSVHKTSS
DQHGANTTRI KFWVIENFLS PQFKRYIPLL AERLGFEVGF VTYRWPWWLP RQTEKQRKIW
AYKILFLDVL FPLDVDRIIF VDADQTAQAD LHELYNMEID GKPIAMTPFC LKFKNKATKS
FRFWERGFWK DHLRGKPYHI SAIFLVDLRR FRAMLAGDQY RGTYASLEGD PNSLQNLDQD
LPNYLQPSVP IFSLPEEWLW CETWCSEKSK SKAKTIDLCN NPRTKMPKLE NAKMIIPGWE
ELDNKLQNLS DSVLASL
//
