ID A0A1F5LIU3_9EURO Unreviewed; 1477 AA.
AC A0A1F5LIU3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENARI_c008G09054 {ECO:0000313|EMBL:OGE53124.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE53124.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE53124.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE53124.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000256|ARBA:ARBA00006351}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGE53124.1}.
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DR EMBL; LXJU01000008; OGE53124.1; -; Genomic_DNA.
DR STRING; 1835702.A0A1F5LIU3; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
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 InterPro; IPR040525; UGGT_TRXL_4.
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; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1477
FT /note="UDP-glucose:glycoprotein glucosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009519634"
FT DOMAIN 43..225
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 274..402
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 409..652
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 667..864
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1184..1450
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
SQ SEQUENCE 1477 AA; 165726 MW; 87D88DF5F03B6148 CRC64;
MKLGSRISWR WYAAIGAFLP GCIANANASP AVNVALQASF DSAPYLVELL EAAAEENSTS
YFPLLDRIAD GTFEDLTTEQ ELYDRFLSVV QDGGHLRTPE SLSSFKLSLS VRSSAPRIEA
HYQFYNTSVQ QSLGAAQDAV CPVWVHLEGK QYCSSALERA QQDVLDAQDP RELPFDRILG
DISLPPAVLY ADISAPMFRD FHETLSGMAK QGQISYRVRY RPPQHWVSRP LFVSGYGVEL
ALKRTDYIVI DDRAAEKLDT ETGPDLEVKE DAPDDLRPLS SSEVARLGVN SAKYVMDSAD
PLEALIKLSQ NFPKYSSTVA AHNATGEMLQ EIRHNRAKML PGGYNVMWIN GVQIDMRQID
AFSLLEHLRR ERKLIEKFRG LGLSANDAVK ILSHQVLTEA QAGGEEQRYD YRDDSEENQV
IIWLNDLEKD SRYEGWSSEL DAYITSAYPG QLPPVRRDLH NVVVPVDLSD PENMMLIAGN
LHAFIKRGIP VRFGLVPLSS SLESVAQLKV AHYLFDAYGL DSLVKYFEAY ATKGKRGFPD
KSCFVTATKE HELIGDHPAL SLDQVLKSEK YNALVSHTAA YQRRLSLTGD APHFLVNGVP
VSSEGNWMQG MSMQISRDLK LVQQGIHEDL FEEDAWLPEF FLAGAFKRRN TFLMPEDPKS
VRIVDLANVL GSDENILNKI PRIASDKSAL DSVHMIVVGD FESEGVTLLT EALNLRKEHT
DVEVLLLHNA ASDDDALPKN LVMVYQSLAK GESIDQVLAR IRASDDDAEI PEIAVEELSS
VQALHQRLAK ELGFEPGTEG LVVNGRAVGP IDKDYPLTMD ELSQLIAYER LKRLDPVALA
VAQLGFQTKI SSPLDFAKLT SLVALSMISD VPEGIFENTP DFRMDVSDKW RTVHSVITVS
NSDDPAINVA VVLDPASEVA QRWLPIIKVL SELSGVQLKI FLNPKEDLKE LPVKRFYRYV
LESEPSFTEG GALARPQASF TGVPVEALLT LGMDVPSSWL VAPKDSIHDL DNIKLSSLKA
GTDVDAIYAL EHILIEGHSR DLTTKTPPRG VQLTLGTEKN PYFADTIIMA NLGYFQFKTQ
PGLWQINLKP GRSEKLFNID SVGGLGYRPQ TGDESNEVAL LTFQGRTLFP RLSRKPGHEE
EDVLETGIQP GSTKDYFAKG LNFASGVLSS VGVSTKSSDQ QADINIFSVA SGHLYERMLN
IMMVSVMRHT KHTVKFWFIE QFLSPSFRAF LPSLAREYNF SYEMVTYKWP HWLRAQKEKQ
REIWGYKMLF LDVLFPLSLD KVIFVDADQI VRTDMYDLVT HDLQDAPYGF TPMGDSRAEM
EGFRFWKQGY WSNFLRGKPY HISALYVVDL NRFRALAAGD RLRGQYQMLS SDPNSLSNLD
QDLPNHMQHH IPIHSLPQEW LWCETWCADE DLETARTIDL CNNPLTKEPK LERARRQIPE
WTIYDDEIAA LARRVAGVED AAGVEFVQSG EERKDEL
//
