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Database: UniProt
Entry: F1L2H6_ASCSU
LinkDB: F1L2H6_ASCSU
Original site: F1L2H6_ASCSU 
ID   F1L2H6_ASCSU            Unreviewed;       577 AA.
AC   F1L2H6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=UDP-glucuronosyltransferase 2B13 {ECO:0000313|EMBL:ADY44330.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY44330.1};
RN   [1] {ECO:0000313|EMBL:ADY44330.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC         beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000301};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   EMBL; JI170122; ADY44330.1; -; mRNA.
DR   AlphaFoldDB; F1L2H6; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48043:SF18; GLUCURONOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADY44330.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          545..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  65208 MW;  B5CF21019578DE65 CRC64;
     MRVIIFFLCL FSEVSAINIL LFLIGTTHFE RGVFEYLAQQ LALRNHYTVT VKPILIPEES
     RLVKQKLHLV HEKTLNNLLP RHLFEPLEAI GNDFPWRRGY ETEQHLFPYY AAHVHACKKM
     LNSNLMETLK KDQIDVAIVY AGNPCQLAIV HALHIPFIYF DVEGFTDETR VASGTPLNAD
     IPPSQCHPPT SPVIQRIANG LCILREYAAQ SGFSWLASRV SERYARMDGP IGRLFVEDYE
     LKKKFPNFPD VNEIKQNAEL YFINSDRLIE YEHALLPHVI PIAGLHIDQV KPLFHPWNTS
     IASAEKGTIV VSLGTQANSS SMTLHQARSI LGALSRLTAY RIYWRIGPTL YIPGVNLDHI
     PSYINVTSFI PQNDLLADRR TRLLITNGGM QSIIEAIVHG VPIVGIPLYG TNRQNLDKVY
     SKGFGLIVTK DRLSESTLYT AIKEVLESSK YKTVAKNMAR EWKGRPQNAF QTALHYIEHV
     GRHRRALFIG VPHRSMHWAR MMNIDLLAVL FLAATAPLLL AYRLVATSIT ASYRYKGELQ
     NSCGSRKPIG DLKESDSAEG CQFGTKQNGR SQPSSRN
//
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