ID V9KMW8_CALMI Unreviewed; 392 AA.
AC V9KMW8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO99503.1};
RN [1] {ECO:0000313|EMBL:AFO99503.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gills {ECO:0000313|EMBL:AFO99503.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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|RuleBase:RU362059};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362059}; Single-
CC pass membrane protein {ECO:0000256|RuleBase:RU362059}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}.
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DR EMBL; JW866986; AFO99503.1; -; mRNA.
DR AlphaFoldDB; V9KMW8; -.
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 InterPro; IPR035595; UDP_glycos_trans_CS.
DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR PANTHER; PTHR48043:SF140; UDP-GLUCURONOSYLTRANSFERASE 2A1; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU003718}; Membrane {ECO:0000256|RuleBase:RU362059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718};
KW Transmembrane {ECO:0000256|RuleBase:RU362059};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362059}.
FT TRANSMEM 355..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362059"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFO99503.1"
SQ SEQUENCE 392 AA; 44646 MW; 6779A8EE18C99859 CRC64;
ENLRLAKYDI IIADPVTVGA ELLALKFKIP FVYIFRFSPA SAMERFCGQI PSPASYVPAT
LSELGPTMSF AQRLTNLLSY IIQDFFFSTI WGRWDSYYSD ILGEPTTFCE TMGKADIWLI
RTYWDFDYPR PFLPNFVFVG GIHCRPAKSL PQEMEEFVQS SGEHGIVVFT LGSMIKNLTA
ERADVIAAAL GQIPQKVLWR YAGEKPKTLA PNTKLYDWLP QNDLLGHPKT RAFITHGGTN
GIYEAIYHAV PLIGIPIFAD QPDNMSHMKE KGMAVVLNFN TMTTLDLVDA LNTVINDPRY
KENAIRLSSI QHDQPMTPLD TAVFWIEFVM RHKGAKHLRP ASHSLTWYQY HSLDVIAFLC
FCLAVALYIP IKCCMYCFRR CRSKLKRKGK KD
//
