ID V9KVQ7_CALMI Unreviewed; 469 AA.
AC V9KVQ7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:AFP02741.1};
RN [1] {ECO:0000313|EMBL:AFP02741.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Intestine {ECO:0000313|EMBL:AFP02741.1};
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: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167, ECO:0000256|RuleBase:RU362059}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167,
CC 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; JW870223; AFP02741.1; -; mRNA.
DR AlphaFoldDB; V9KVQ7; -.
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; 2.
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:SF147; UDP GLUCURONOSYLTRANSFERASE 1 FAMILY, POLYPEPTIDE A7; 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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU003718}; Signal {ECO:0000256|RuleBase:RU362059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU362059"
FT CHAIN 26..469
FT /note="UDP-glucuronosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU362059"
FT /id="PRO_5005149352"
FT NON_TER 469
FT /evidence="ECO:0000313|EMBL:AFP02741.1"
SQ SEQUENCE 469 AA; 52655 MW; 51050B642A8E3E5B CRC64;
MAFRLNHPAV CLLACLPSLW SVADSGNLLV VPVDGSHWLN IRTLIQELGR RGHSIVVVAP
AVNMNISPGP HYTTKLYPVP YNQSDIQAVK PHVLVKQTFY NTVTTTFKKV NKLKHFLLVT
CESLLYNTGL MRELAESAFD ALLTDPFTSC GAIVAESLSL PSVHILRGLP CGLDYTSAQC
PRPVSYVPRM FTGNSDRMNF LQRTANFLMS VTEPLLCYLI YSPFDELAAR FLQKEVTVKE
LLSRGAIWLL RFDFVFEYPR PLMPNMILVG GMNCKDRKPL PEELEEFMNS SGEYGAVIFS
LGSMVSDVPI ETADQIAEAL GQIPQKVLWR HTGVKPSTLA PNTKLMKWMP QNDLLRHPKT
RAFISHGGMH GIYEAICAGV PMVLVPLFAD QLENVLRIKN QNAGVLIDLK NMSSRDLVEA
LNTVINDTRY KENMMRLSSL HKDQPVKPLD LSVHWVEFVM KHKGAEHLR
//