ID A0A3P9AUS8_9CICH Unreviewed; 1538 AA.
AC A0A3P9AUS8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=UDP-glucose glycoprotein glucosyltransferase 1 {ECO:0000313|Ensembl:ENSMZEP00005001378.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005001378.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005001378.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005001378.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR RefSeq; XP_004540359.1; XM_004540302.1.
DR STRING; 106582.ENSMZEP00005001378; -.
DR Ensembl; ENSMZET00005001466.1; ENSMZEP00005001378.1; ENSMZEG00005001047.1.
DR GeneID; 101467633; -.
DR KEGG; mze:101467633; -.
DR CTD; 56886; -.
DR GeneTree; ENSGT00390000004600; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000265160; LG19.
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:SF3; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 1; 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:UP000265160};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1538
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018129034"
FT DOMAIN 50..228
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 303..432
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 442..690
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 721..946
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1248..1515
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
SQ SEQUENCE 1538 AA; 174159 MW; 17CCEC98FBB981C1 CRC64;
MNSGSYRAGF GVGLRMWLLW IVLLSLLSVA SGGADSKAVT TTLTTKWADT PLLLEASEFM
AEESQEKFWD FVEANQNIEG EHDDTDQAYY DLIMKRASAL LSSVQLNMLK FALSLRAYSA
TVHSFQQIAS TEPPPSGCSA FLSIHGEKTC DAEKLEALLK SAPQRTKPYL FKGDHKYPGS
NPDAPVVILY AQFGTADFQK LHQVILSKVN EGSVTYVLRH YLPKSRGKKV YLSGYGVELA
IKSQEYKAKD DTQVQGAEVN ATMIGENDPV DEVQGFLFGK LKTLYPELKE QLKELRKHLV
ESTNEMAPLK VWQMQDLSFQ TAARILAAPA VDALNVMKDL SQNFPTKARS ITKTVVNSEI
RKEIGENQKF FKGTLGLQPG DSALFINGLH IDLDAQDIFS VFEVLRSEAR VMEGLRSLLI
ETPFIHDILK LNVQPSDSDY AVDIRSPAIS WINNLETDYR YSSWPSNVQE LLRPTFPGVI
RQIRKNFHNL VIILDPTQEN TVELLSVAEM FYANNIPLRI GLVFVVSDED DIDGMQDAGV
ALVRAYNYIT EEVDSQNAFE AVMSMFNRVP VGGRLSVGDV VKVLEKKFPY VEVSSVLGAD
SSYDSNRKEG RAYYEQTGVG PLPVVMYNGI PYQREQLDPD ELETVTMQKI LETTSFYQRA
VYLGELATDH DVVDFIMNQP SVVPRINPRV LSTSRTYLDL SDTNNYFIDD YARFSTLDTV
EKNTAVANSM NYMTKKGMTT TNRHDDAYIR PVTFWVVGDF DKPSGRQLLY DAIKHMKTSN
NVRLGMINNP SADVSAETTR VTRAIWSAMQ TQTANNAKNF ITKMAKEETA AALQKGVDVG
EFAVGGMDLS LFKSAYEASK FNFLLSHAAY CRDVLKLKKG QRAVISNGRI IGPLEEAEVF
NQDDFLLLES IILKTSGERI KSKVQNFGIE EDRASDLVMK VDALLSSQPK GEARVEYGFA
DDRYSAVKIR PKEGDVYFDV VAVVDPVTRE AQKLAPLLLV IKQLVNVNLR VFMNCQSKLS
EMPLKSFYRY VLEPEVAFQA DGSFSPGPIA KFLDMPQSPL FTLNLNTPES WMVESVHTRY
DLDNIYLQEV ENIVAAEYEL EHLLLEGHCF DVSSGQPPRG LQFTLGTESE PVIVDTIVMA
NLGYFQLKAN PGAWILKLRK GRSDEIYKIY SHDGTDSPAD SDDIVVVLNN FKSRIIKVKV
QKKPDKFSEE LLSDGTEEND TGFWNSLTRG FTGGGKTEEP KQDKEDTINI FSVASGHLYE
RFLRIMMLSV LKHTKTPVKF WFLKNYLSPT FKEFIPHMAK EYGFQYELVQ YKWPRWLHQQ
TEKQRIIWGY KILFLDVLFP LAVDKILFVD ADQIVRTDLK ELRDFDLEGA PYGYTPFCES
RREMDGYRFW KSGYWASHLA GRKYHISALY VVDLKKFRKI AAGDRLRGQY QGLSQDPNSL
SNLDQDLPNN MIHQVPIKSL PQEWLWCETW CDDSSKKSAK TIDLCNNPMT KEPKLQAAVR
IVAEWTDYDQ EIKRLQARIQ DRANHMAKQQ DTDAHTEL
//
