ID A0A423SYE3_PENVA Unreviewed; 1539 AA.
AC A0A423SYE3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Putative UDP-glucose:glycoprotein glucosyltransferase {ECO:0000313|EMBL:ROT69290.1};
DE Flags: Fragment;
GN ORFNames=C7M84_012517 {ECO:0000313|EMBL:ROT69290.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT69290.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT69290.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT69290.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT69290.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT69290.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) 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:ROT69290.1}.
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DR EMBL; QCYY01002586; ROT69290.1; -; Genomic_DNA.
DR STRING; 6689.A0A423SYE3; -.
DR EnsemblMetazoa; XM_027367120.1; XP_027222921.1; LOC113815034.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000283509; 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: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:UP000283509};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ROT69290.1}.
FT DOMAIN 55..236
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 310..444
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 448..699
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 732..947
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1249..1515
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ROT69290.1"
SQ SEQUENCE 1539 AA; 174434 MW; BB8C5689B3312068 CRC64;
FKDIIILKVR QINAMREILG PLLGLLCFLL TGTTVKCQGK VKPVTTHLSA KWSHTPLLLE
TAEYMREESI ATFWEFVEAV SQKDFTLFTK GSDKAAYNEI LGTAGQFLSP SQVSILKLSL
SMRVYSPKIE MFRQIALDRN LPTGEDCIAV FDVNGELTCN IEAMKKLVEV GSGTKPVSYD
MDHHYPGGEN SKVGVTLYAE LGTKEFRIHH LAVKELVGLG KIDYVLRPYI KGNSKKKVRL
SGYGVELAIK STEYKAQDDT KVQDDGGRQE EDDEQEVEVE GFLFSKLESL HPEKMEELEQ
LRNHLVESRH EMAPMKVWQL QHLSMQAAQR IMTTPREEQL SVFVHTAQNF PMLARSLVRT
KVDDKMKREI LKNQNQLSAQ MDVNPSDAAL FINGMYFDMD FTDIYTLLDH IRTEDRVMGG
LYKLGVPGES LSTLLNIDLS ESKQDYGIDI RDTAIVWMND IENDRAYSKW SSSVGELLRP
TYPGMLRSIR KNFHNLVIVA EPEKATTADL IRLVEGFLTH NAPVRIGIVM SVNPDQTLRG
YDDAGVAMLC AFNYVAQNLE GREDANYKAL QFLVDLYSNV QGDITVDDVT SHFKSKYRSV
DLEDVFGEDS DYDVGRMLAQ EFVEKAGITS LPQALMNGVP LPEKHLNADE FEEVVLMDVM
RTTQTLQRAV YKGQLEDKHD VVDWLMSLPN IMPRLNERIL STKNSKFIDL TGTSGETLSS
VPVESFATQK APEMTATLAN SCRYITTKND HTLRPLTVWI VGDFDTYEGR AILLEGVKYL
RESNSIRICA IHNTDLSSES PKLFSRAVEV AQTTLPPAVA RQFLAKVLEK DNAKKIIAGT
KKWKDFEIAG LDIDAFTSRM NSFKDSVFKA HSVFCKKVLA LSPGQRTVVA NGRHLGTFKA
TEKFVMEDFG LLEKYVHSTF GEKLTEVLIG EDPPVNSDIS DLTMKVAGVL QTKPQSKGRT
TVNLRSDQYS VVKIPARNPN MPVFDIVAVC DPVSNAAQKI GPILMVLQEI VNAEIRVVLN
AREKHSEMPL RRFYRYVLEP EPQFTEAGDM TAGPYARFTG LPESSILTLN YHAPENWLVE
VVKSVYDLDN IKLDLVETGV HSEFELEHLL LEGHCFEQSS GNPPRGLQFT LGNRQQPVLV
DTIVMANLGY FQLKANPGAW LLRLRQGRSA DIYTIASHEG TDTPVGSEDV EIIISSFRSH
VVKVRVGKQP GKQHLELLAD ENEESGGLWN SITSTFSSSG AKEDETEKVN IFSVASGHLY
ERFLRIMMVS VRRHTKAPVK FWFLKNFLSP NFKDILPLLA KEYGFEYELV QYKWPRWLHQ
QTEKQRIIWG YKILFLDVLF PLDVKKIIFV DADQVVRADV KDLNNEELDG APYGFVPFCE
SRKEIEGFRF WKQGYWRNHL AGRKYHISAL FVVDLKKFRR IAAGDRLRGQ YQGLSQDPNS
LSNLDQDLPN NMIHQVRIKS LPQDWLWCES WCDDESKKSA KIIDLCNNPM TKEAKLVAAQ
RIIPEWTEYD NEIKAVLKGF KENKSYTEEQ PSQSPHIEL
//
