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UD3A1_HUMAN
ID   UD3A1_HUMAN             Reviewed;         523 AA.
AC   Q6NUS8; G5E961; Q8IYS9; Q8NAW4; Q96DM6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=UDP-glucuronosyltransferase 3A1;
DE            Short=UDPGT 3A1;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT3A1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney, and Small intestine;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: UDP-glucuronosyltransferases catalyze phase II
CC       biotransformation reactions in which lipophilic substrates are
CC       conjugated with glucuronic acid to increase water solubility and
CC       enhance excretion. They are of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NUS8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NUS8-2; Sequence=VSP_044985, VSP_044986, VSP_044987;
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AK057066; BAB71358.1; -; mRNA.
DR   EMBL; AK091977; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC016612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC112204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471119; EAW55928.1; -; Genomic_DNA.
DR   EMBL; BC035012; AAH35012.1; -; mRNA.
DR   EMBL; BC068446; AAH68446.1; -; mRNA.
DR   CCDS; CCDS3913.1; -. [Q6NUS8-1]
DR   CCDS; CCDS54841.1; -. [Q6NUS8-2]
DR   RefSeq; NP_001165344.1; NM_001171873.1. [Q6NUS8-2]
DR   RefSeq; NP_689617.3; NM_152404.3. [Q6NUS8-1]
DR   AlphaFoldDB; Q6NUS8; -.
DR   SMR; Q6NUS8; -.
DR   BioGRID; 126370; 12.
DR   STRING; 9606.ENSP00000274278; -.
DR   DrugBank; DB01852; Kaempherol.
DR   DrugBank; DB04216; Quercetin.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyGen; Q6NUS8; 1 site.
DR   iPTMnet; Q6NUS8; -.
DR   PhosphoSitePlus; Q6NUS8; -.
DR   BioMuta; UGT3A1; -.
DR   DMDM; 74749002; -.
DR   EPD; Q6NUS8; -.
DR   jPOST; Q6NUS8; -.
DR   MassIVE; Q6NUS8; -.
DR   PaxDb; Q6NUS8; -.
DR   PeptideAtlas; Q6NUS8; -.
DR   PRIDE; Q6NUS8; -.
DR   ProteomicsDB; 33841; -.
DR   ProteomicsDB; 66710; -. [Q6NUS8-1]
DR   Antibodypedia; 22897; 41 antibodies from 15 providers.
DR   DNASU; 133688; -.
DR   Ensembl; ENST00000274278.8; ENSP00000274278.3; ENSG00000145626.12. [Q6NUS8-1]
DR   Ensembl; ENST00000333811.5; ENSP00000328033.4; ENSG00000145626.12. [Q6NUS8-2]
DR   Ensembl; ENST00000625798.2; ENSP00000487376.1; ENSG00000145626.12. [Q6NUS8-2]
DR   GeneID; 133688; -.
DR   KEGG; hsa:133688; -.
DR   MANE-Select; ENST00000274278.8; ENSP00000274278.3; NM_152404.4; NP_689617.3.
DR   UCSC; uc003jjv.3; human. [Q6NUS8-1]
DR   CTD; 133688; -.
DR   GeneCards; UGT3A1; -.
DR   HGNC; HGNC:26625; UGT3A1.
DR   HPA; ENSG00000145626; Group enriched (kidney, liver).
DR   MIM; 616383; gene.
DR   neXtProt; NX_Q6NUS8; -.
DR   OpenTargets; ENSG00000145626; -.
DR   PharmGKB; PA142670642; -.
DR   VEuPathDB; HostDB:ENSG00000145626; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000163740; -.
DR   InParanoid; Q6NUS8; -.
DR   OMA; VGPIMPV; -.
DR   PhylomeDB; Q6NUS8; -.
DR   TreeFam; TF315472; -.
DR   BRENDA; 2.4.1.17; 2681.
DR   PathwayCommons; Q6NUS8; -.
DR   Reactome; R-HSA-156588; Glucuronidation.
DR   Reactome; R-HSA-9749641; Aspirin ADME.
DR   BioGRID-ORCS; 133688; 9 hits in 1071 CRISPR screens.
DR   ChiTaRS; UGT3A1; human.
DR   GenomeRNAi; 133688; -.
DR   Pharos; Q6NUS8; Tdark.
DR   PRO; PR:Q6NUS8; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q6NUS8; protein.
DR   Bgee; ENSG00000145626; Expressed in kidney epithelium and 51 other tissues.
DR   ExpressionAtlas; Q6NUS8; baseline and differential.
DR   Genevisible; Q6NUS8; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IDA:MGI.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IDA:MGI.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:MGI.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..523
FT                   /note="UDP-glucuronosyltransferase 3A1"
FT                   /id="PRO_0000299150"
FT   TOPO_DOM        23..483
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..54
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_044985"
FT   VAR_SEQ         282..306
FT                   /note="DLDNFIANFGDAGFVLVAFGSMLNT -> NGQPALFTTPSLFSSGVYPEPLR
FT                   WL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_044986"
FT   VAR_SEQ         307..523
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_044987"
FT   VARIANT         121
FT                   /note="C -> G (in dbSNP:rs3756669)"
FT                   /id="VAR_034791"
FT   CONFLICT        139
FT                   /note="Y -> C (in Ref. 1; BAB71358)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="A -> T (in Ref. 1; BAB71358)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        475
FT                   /note="A -> V (in Ref. 1; BAB71358)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q6NUS8-2:251
FT                   /note="W -> R (in Ref. 2; AAH35012)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   523 AA;  59151 MW;  602AE3D75CE986BD CRC64;
     MVGQRVLLLV AFLLSGVLLS EAAKILTIST LGGSHYLLLD RVSQILQEHG HNVTMLHQSG
     KFLIPDIKEE EKSYQVIRWF SPEDHQKRIK KHFDSYIETA LDGRKESEAL VKLMEIFGTQ
     CSYLLSRKDI MDSLKNENYD LVFVEAFDFC SFLIAEKLVK PFVAILPTTF GSLDFGLPSP
     LSYVPVFPSL LTDHMDFWGR VKNFLMFFSF SRSQWDMQST FDNTIKEHFP EGSRPVLSHL
     LLKAELWFVN SDFAFDFARP LLPNTVYIGG LMEKPIKPVP QDLDNFIANF GDAGFVLVAF
     GSMLNTHQSQ EVLKKMHNAF AHLPQGVIWT CQSSHWPRDV HLATNVKIVD WLPQSDLLAH
     PSIRLFVTHG GQNSVMEAIR HGVPMVGLPV NGDQHGNMVR VVAKNYGVSI RLNQVTADTL
     TLTMKQVIED KRYKSAVVAA SVILHSQPLS PAQRLVGWID HILQTGGATH LKPYAFQQPW
     HEQYLIDVFV FLLGLTLGTM WLCGKLLGVV ARWLRGARKV KKT
 
 
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