ID A0A194RI37_PAPMA Unreviewed; 808 AA.
AC A0A194RI37;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Beta-1,4-glucuronyltransferase 1 {ECO:0000256|ARBA:ARBA00017962};
DE AltName: Full=I-beta-1,3-N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00030723};
DE AltName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00033291};
DE AltName: Full=Poly-N-acetyllactosamine extension enzyme {ECO:0000256|ARBA:ARBA00032175};
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1 {ECO:0000256|ARBA:ARBA00032181};
GN ORFNames=RR48_13955 {ECO:0000313|EMBL:KPJ17099.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ17099.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ17099.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ17099.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ17099.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-
CC alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-
CC ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-
CC alpha-D-Man)]-Thr-[protein] + H(+) + UDP; Xref=Rhea:RHEA:46860,
CC Rhea:RHEA-COMP:15023, Rhea:RHEA-COMP:17482, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:142405,
CC ChEBI:CHEBI:177336; Evidence={ECO:0000256|ARBA:ARBA00029363};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 49 family.
CC {ECO:0000256|ARBA:ARBA00008539}.
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DR EMBL; KQ460205; KPJ17099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194RI37; -.
DR STRING; 76193.A0A194RI37; -.
DR InParanoid; A0A194RI37; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00761; Glyco_tranf_GTA_type; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR043189; B4GAT1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR46420; BETA-1,4-GLUCURONYLTRANSFERASE 1; 1.
DR PANTHER; PTHR46420:SF1; BETA-1,4-GLUCURONYLTRANSFERASE 1; 1.
DR Pfam; PF13896; Glyco_transf_49; 1.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 583..807
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 56..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 89371 MW; 7EBDC93EFEDF266C CRC64;
MRYITLQRAM VRSRRDKIWR WRCQWCFISV VAVALVLYNA AANIWLLHPS CAQSGPTSRP
APTAPTAHSP PPTEPPCEPC LEAAPSAAAD DDPIGRLDLR LGRWDGSRSY RLFDYATLGD
VYAEVSASRR VCLATQSSIE RLHELMRIAA HWSGPMSVAV FVAGDELRLL RAFATWLLRC
RPEIYGRLAL HAATPAERPG TQGAAPSWAR DCEAKPLPPA ERRADTVAWR ARHPYPQNHL
RNLARRNCHT PYVFLVDVDI VPSRGMAEAL DAFLARAPKC PLCAYVVPTY ELDKRVAEFP
ANKSELLRLS KNKLAIPFHR KVFIYNQYAS NFSRWEASGG NESCETHVSH DVTNFELLYE
PFYVATDAVP AHDERFLGYG FTRNTQFCLL TEGINRGRAR INIYCMNGPA RPIKYHDHRH
EVEVCEGGLI LVLFHFRPFY ARVDVDLTVE GTHRKGNSIP VHPLLRRLKE AVEGECCKEE
GDNPSTDVEL QDVDLQEACP ELSGQIIGGR PSSVTRHPYQ VSMVMNGNSF CGGFIISPDY
VLTAAHCVQK TYASSGSNSA NTLYVELQDV DLQEACPELS GQIIGGRPSS VTRHPYQVSM
VMNGNSFCGG FIISPDYVLT AAHCVQNTAA GAIRLRVGST RRDSGGRIVN VANVTVHAQY
GRPRFDNDIA ALRLARPLVF SNAVRAIRLP QPRQPVPLVR LTVTGWGLTA PRGRRIPRTM
MEARVPVVPH WLCRLSYGDA LTDNMFCGGH FLIGGVSSCQ GDSGGPAVFR GTAYGVVSFA
RGCALPLSPT VFTNLAALRD WVSQNTGV
//
