ID A0A3Q3B0A6_KRYMA Unreviewed; 1526 AA.
AC A0A3Q3B0A6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=UDP-glucose glycoprotein glucosyltransferase 2 {ECO:0000313|Ensembl:ENSKMAP00000022873.1};
GN Name=UGGT2 {ECO:0000313|Ensembl:ENSKMAP00000022873.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000022873.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000022873.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
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 RefSeq; XP_017278228.1; XM_017422739.1.
DR STRING; 37003.ENSKMAP00000022873; -.
DR Ensembl; ENSKMAT00000023163.1; ENSKMAP00000022873.1; ENSKMAG00000016954.1.
DR GeneID; 108239796; -.
DR KEGG; kmr:108239796; -.
DR CTD; 55757; -.
DR GeneTree; ENSGT00390000004600; -.
DR OMA; FQTHQLF; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000264800; Unplaced.
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:SF1; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 2; 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:UP000264800};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1526
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018674591"
FT DOMAIN 34..213
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 286..415
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 427..674
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 704..923
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1230..1497
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1502..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1526 AA; 173404 MW; 018638BD9538E7BB CRC64;
MRQVLLLALL LNVRPGTQTP KGVTASLKAK WSMTPFLLET SEFVGEDGSE KFWQFVETVK
ELTVYKQGES VRSYYNLIIK KAGQFLTELQ VHLLRFALSM RSYSPAVHAF QQIASDEPPP
EACPAFVSVH GELSCSTKDI KKLLKAAAGR PKPYLYKNDH TYPGANKTDV PVVILYAEIG
TKKFSVFHKV LSEKAEEGAL IYVLRHFVAD PKPQKILLSG YGVELAIKST EYKAVDDTKV
KDSKTVLNAE DDDNDEVQGF VFETLKKSHP ELQEQLGELR KHLLESTNDM APLKVWEMQD
LSFQAAARIM SVPKFDALKV MRDLSQNFPS KARSLTRVAV KKEMRKEIEE NQKHLSETIA
VHPGDGELFI NGLHIDLDIH NPFSILDILR TEARILEGLH NLGIKGEHQG KLLRLPVNSM
DDSYALDIRH PAIMWMNDIE NDSMYRSWPA SVQELLRATF PGVIRQIRRN FFNLVLFLDP
LQEETAELVK LAELFYKHKI PLRIGFVFVV NTKDEIDGFS DAGVGFYRLL NYIADEYDLS
QAVMSIVSMY SKVDVGEMLS ADTIAAYLKK KYPKANAERI LGVDSEYDYK RKDGSLFYRK
SGLGALPLAL FNGVPLNPDE MDPEDLETII LQRIMDTTTA FQRAAFLGQL ADSSDVVDYL
MEQANVVPRM NPLVLSTDRK YLDFTGTPVV DDWEDTSMFS FLDARDKTAV VAKRMKYFTN
NDEDGMTSVT MWIVGDLEKV SGRKLLLNAL KHVKSRPGVR VGVINNPSGR PREDNTAVYR
AVWATLLTQK NKAAAEFVQK LLKEESSQLL QQGTKMKDLL MQGMDVDAFE KKFNTLEVDF
VHSQQLFCRD VLKLHPGLRA VISNGRILGP FEEQEEFTVE DFHLLERITL SSSAEKVKTK
VKQMGMKPKH ASDLVMKVDA LLAAAPKGEV RRDVHFKDTH SVLHLSPREN EVFFDVVAIV
DPLTREAQKI SQLLIVLSQV VNVRLQVFMN CRAKLSEMPL KSFYRFVLES DVAFLANETA
SPGPVARFLE LPEAPLLTLN MITPESWMVQ AVSSPHDLDN IHLQEVNGVV AAEFELEHLL
LEGHCFDLST GQPPRGLQFT LGMSRDPLMY DTIVMANLGY FQLKANPGAW ILRLRKGRSE
EIYQILTHDG TDSPADAGDV IVVLNNFHSK IIKVRVQKKA EKINEDLLSE TSESKGIWDS
IVSVWSTFEK SITGGGSKKD GGEKKKEDVL NIFSVASGHL YERFLRIMML SVLRHTNTPV
KFWFLKNYLS PSFKETISHM ATSYGFQYEL VQYKWPRWLH QQTEKQRIIW GYKILFLDVL
FPLAVDKIIF VDADQIVRAD LKELKDFDLE GAPYGYTPFC DSRREMEGYR FWKTGYWASH
LGHRKYHISA LYVVDLKKFR KIAAGDRLRG QYQALSQDPN SLSNLDQDLP NNMIHQVAIK
SLPQEWLWCE TWCDDASKVT AKTIDLCNNP KTKEPKLMAA VRIVPEWVEY DNEIKQLLGQ
IQEGAAQKQT PPSTQHKKAD KQRDEL
//
