ID A0A2T7NBA5_POMCA Unreviewed; 1378 AA.
AC A0A2T7NBA5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_21003 {ECO:0000313|EMBL:PVD18454.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD18454.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD18454.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD18454.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD18454.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 9A1,2,3B1,2,3) + UDP-alpha-D-glucose = H(+) + N(4)-
CC (alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:61304, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:59080, ChEBI:CHEBI:139493;
CC Evidence={ECO:0000256|ARBA:ARBA00034426};
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:PVD18454.1}.
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DR EMBL; PZQS01000014; PVD18454.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7NBA5; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg14.
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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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:UP000245119};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1378
FT /note="UDP-glucose:glycoprotein glucosyltransferase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015537462"
FT DOMAIN 70..118
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 192..321
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 342..537
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 569..785
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1082..1347
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
SQ SEQUENCE 1378 AA; 155637 MW; 1237E3704F43AD8C CRC64;
MQVLYLFLEL STLLWLIEGK QKPVTVKLDA KWSSTPVLLE ISEFLAKESN DVFWSFVQDV
MRISPQTFDA EAKSPVVILY GQLGTQDMLN FHRVLVTKAQ ERDIQYVLRH FVQEPAESNV
RLSGYGVELS LKSTEYKAKD DTKFEGGTDG ESIDFEDEEE DLQGFVFSKL RQLHPDLQKE
LKEFHSHLRE SATELAPLKA WELQDLSLQA AQRVLSSSPA DALQILTDIS QNFPTLAQSL
VKTVVPVELK EEIRQNQEFF ERNHNLFAGE SAFFLNGRAM DMEIYDVFTL LDIMLAEAKL
VEGLHTLGFK GEWLQKILQL DLSSGEDTGN ALDIRHSAVQ TFIINPAEDA SRELLKMAEA
FYVHSAPIRL GIVLQASADA SAKEDAGVAF ARAFDFIKID QSPAKALSFI TDVYEKVGSE
KITAESIIAE FNVQYPGEDL ELVFGSSSEY DDTRKAGIDY IQRSGLLGFP QVLVNGVPLD
KKYLSQEDFE EGVVGEILKQ TQVIQKAVYH GKLTDSDVVL DWLMEQDNVM PRLNSRVLSS
AAAQLDLTEN VDGSVLDDPA LFEMLNVREM SGAVAARLKY LTRRDEPAVR PVTMWVVCDL
QTPEGRDLLY NAIKQVKASN ELRVTWVPSS AAADNVDLVS RAAWVALRDL PGMLSKSFLT
KLVKEENYAE ISAGTKTLRD LEVNGMDMDS YLAAVEAETG GVLKSLSMFT RRVLGFTVGQ
RGVVANGKIY GPLGAQEDFT QDDFGLLEKV ISVQAGAKLR EQVKAVGIDG DRGSEMVMKV
SALLSSRSRS ESRSKVVFRE DKYSVVKIPA ADDLPAFTVE AIVDPASRAA QKMAPILQIL
HAVANVDIRI YMNSRQHLSE MPLTRFYRYV LEPELMFRSD GSAAEGPVAR FIALPHKSLL
TLGIDAPESW LVESVSSVYD LDNILLEEVN VAFLSMGGRM FEMFAGHCSD ATTMHPPRGL
QFILGTENKP DIVDTIVMAN LGYFQLKASP GLWRLRLREG RSQELYTIQS HEFTDTPAGS
SDVVVAMNSF KSKIIRIKVS KKPDKLHEKL LEDGQQESQG LWDSISSSFS GHKTEEDEDK
TLNIFSVASG HLYERFLRIM MLSVLKHTKS KVKFWFLKNY LSPTFKDFIP HMAKHYGFEY
ELVQYKWPRW LNQQKEKQRV IWGYKILFLD VLFPLDVKKI IFVDADQIVR TDLQELHDLD
LGGAPYGYTP FCDSRKEMDG FRFWKSGYWH SHLSGRKYHI SALYVVDLKK FRQIAAGDRL
RGQYQGLSQD PNSLANLDQD LPNNMIHQVA IKSLPQEWLY CETWCSETEK ARAKTIDLCN
NPLTKEPKLQ AAMRIVPEWK NYDYEIKLLW DQIYGTNTKA QIEYEPPNIA DFTTKTEL
//
