ID D8T892_SELML Unreviewed; 1614 AA.
AC D8T892;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Glycosyltransferase in CAZY family GT24 {ECO:0000313|EMBL:EFJ07070.1};
GN Name=GT24A1 {ECO:0000313|EMBL:EFJ07070.1};
GN ORFNames=SELMODRAFT_186368 {ECO:0000313|EMBL:EFJ07070.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ07070.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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 EMBL; GL377689; EFJ07070.1; -; Genomic_DNA.
DR RefSeq; XP_002991808.1; XM_002991762.1.
DR STRING; 88036.D8T892; -.
DR EnsemblPlants; EFJ07070; EFJ07070; SELMODRAFT_186368.
DR Gramene; EFJ07070; EFJ07070; SELMODRAFT_186368.
DR KEGG; smo:SELMODRAFT_186368; -.
DR eggNOG; KOG1879; Eukaryota.
DR HOGENOM; CLU_002668_1_0_1; -.
DR InParanoid; D8T892; -.
DR OMA; KNFYRYV; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
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; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFJ07070.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1614
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003123374"
FT TRANSMEM 784..806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 958..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..241
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 330..446
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 459..720
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 876..950
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1296..1493
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT DOMAIN 1508..1579
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1586..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1614 AA; 183241 MW; 202650F5FF24B15F CRC64;
MSKALLPLLA WVAILVLAAA AAHRLHKNVI VELHAKWSGT SLLLEMGELV AKERDDNFWK
FIDSWIEREE KESQSSSNST SNCLEQILSQ GSALLDGHLA SLLDLSLSLR SASPKLVVYA
QLAQESLSAF NLHSGGSDRP RPPRQKCCWV DVGSSLLLEE SELLHWLKSL SGEPLLDKAL
NLFEFDHVYP QSASFAYTAI LYGALGTPCF KRFHSILSDS SKTQDLVRYV ARPFLPDGCE
ESCSACSKAG VGEPLNLAGY GVELALKNME YKAIDDSEVK AGGSSEDTSA EDPLAQEVRG
FIFSRLLERK PHLEGELMTF RDQLLSSEIS DSMNVWEVKD LGYQAAQRIV GASEPLRLMQ
ELNQNFPNLV SSLSRMKINE TIKQEIVSNQ QMISPGRNLL AINGALVNPE SLDLFTLIHM
VHQELSFADK ILKMKVPSSS VSKLLRLPEP VESVAVRVDF RSKDFVHYLN DLEEDNKYNR
WRTNLNELLM PAFPGQLRYI RKNLYHAVYV LDPVSVRGLR TVEMILHYYH NNLPMRFGLI
LLSAADLHSL DEENGAREKD DLSSLMIRLF LYVKNTGGVY NAFEFLKNVR VLDSYSEDSE
ENYTEARHIE EGFVKSLGTM TKTSAMEVFS KLKNGEDYRR EAFESSQFVY RLGLSEVYPC
LLMNGLVYGE SQPQFSVMAA MNEELPKIQE MVYFGQIHSR TDVLDKFLAE EGLKRYNPKI
AGTGKDSKYV SVALVVSESH PVVCSLQYLH TPGTEDDVKP VTHWLLVDLT KESGIRLLTQ
GVRYIVSCIK VLNTKVLLSL FSYGFLFSSR RAKYLRLLHS FLTHYKSGTF GEVLHLYLST
AKEMGLDIAK EAILESSTLS TQLLQFHKVM DFVSISMLTN SLQEKKFVAE LFGIRPGINA
VVTNGRISIQ DSKPFIAEDL MLLESLMYRR RIKDVREIIE DVKWEGLEPD DITRYVNLIN
VAFLSYFVVL SAYLSTVIMA VSSTMASRTR SSETAQFELL KADHSAIVRH VDGSPIQIDA
VINPLSALAQ RLTPLLLMLE EWLHPSIRIV LNPMSSLGDV PLKNFYRYVL PSKEEFLSGG
IGPHARFSNM PPSKTLTLNL DVPEPWLVEP VVAIHDLDNI VLEKLDDERT LHAVFELEAL
MITGHCYEHN EPPRGLQLIL GTKQHAHVVD TIVMANLGYF QLKAAPGVWT LGLARGRSSE
LYTLQGHKQG TDEGPISKQI LVADMRGELV HLEVVKRRGM EDEKLLVVDD DNGKKTSLSV
CFFEWAANIM GTGEKKTSKQ NTSVKFYFTT RHGETINIFS VASGHLYERF LKIMMLSVLK
NTRRPVKFWF IKNYLSPQFK NLIPHMAVEY GFEYELVTYK WPTWLHKQTE KQRIIWAYKI
LFLDVIFPLS LKKVIFVDAD QIVRADMGEL YDMDIKGRPL AYTPFCDNNK DMDGYRFWSQ
GFWKEHLQGK PYHISALYVV DLDKFRQTAA GDNLRVFYEN LSKDPNSLSN LDQVRFEVEL
FLIFFSHNLK QDLPNYAQHT VPIYSLPQEW LWCESWCGNA TKGRAKTIDL CNNPMTKEPK
LQGARRIVQE WPALDEEAQL FTKRILGKGR DEENTMQVPK EPSSTNDADV KDEL
//