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MSR2_ARATH
ID   MSR2_ARATH              Reviewed;         423 AA.
AC   Q0WPA5; Q9C8H5;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Protein MANNAN SYNTHESIS-RELATED 2 {ECO:0000303|PubMed:22966747};
DE            Short=AtMSR2 {ECO:0000303|PubMed:22966747};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase 12 {ECO:0000305};
DE            Short=O-FucT-12 {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:ARJ31412.1};
GN   Name=MSR2 {ECO:0000303|PubMed:22966747, ECO:0000312|EMBL:ARJ31412.1};
GN   Synonyms=OFUT12 {ECO:0000305};
GN   OrderedLocusNames=At1g51630 {ECO:0000312|Araport:AT1G51630};
GN   ORFNames=F19C24.14 {ECO:0000312|EMBL:AAG50891.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Zeng W., Gluza P., Heazlewood J.;
RT   "Arabidopsis glycosyltransferases: an update.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND REVIEW.
RX   PubMed=22629278; DOI=10.3389/fpls.2012.00059;
RA   Hansen S.F., Harholt J., Oikawa A., Scheller H.V.;
RT   "Plant glycosyltransferases beyond CAZy: a perspective on DUF families.";
RL   Front. Plant Sci. 3:59-59(2012).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=23272088; DOI=10.1371/journal.pone.0051129;
RA   Voxeur A., Andre A., Breton C., Lerouge P.;
RT   "Identification of putative rhamnogalacturonan-II specific
RT   glycosyltransferases in Arabidopsis using a combination of bioinformatics
RT   approaches.";
RL   PLoS ONE 7:E51129-E51129(2012).
RN   [7]
RP   GENE FAMILY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=22966747; DOI=10.1111/tpj.12019;
RA   Wang Y., Mortimer J.C., Davis J., Dupree P., Keegstra K.;
RT   "Identification of an additional protein involved in mannan biosynthesis.";
RL   Plant J. 73:105-117(2013).
RN   [8]
RP   WEB RESOURCE.
RX   PubMed=24905498; DOI=10.1111/tpj.12577;
RA   Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA   Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA   Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA   Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA   Loque D., Scheller H.V., Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional genomics.";
RL   Plant J. 79:517-529(2014).
CC   -!- FUNCTION: Glycosyltransferase involved in mannan biosynthesis.
CC       {ECO:0000269|PubMed:22966747}.
CC   -!- PATHWAY: Glycan biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:22966747}; Single-pass type II membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22966747}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG50891.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC       URL="http://gt.jbei.org/arabidopsis.html";
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DR   EMBL; KY906048; ARJ31412.1; -; mRNA.
DR   EMBL; AC025294; AAG50891.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32693.1; -; Genomic_DNA.
DR   EMBL; AK229174; BAF01044.1; -; mRNA.
DR   PIR; A96555; A96555.
DR   RefSeq; NP_175574.2; NM_104041.5.
DR   AlphaFoldDB; Q0WPA5; -.
DR   STRING; 3702.AT1G51630.1; -.
DR   PaxDb; Q0WPA5; -.
DR   PRIDE; Q0WPA5; -.
DR   ProteomicsDB; 239009; -.
DR   EnsemblPlants; AT1G51630.1; AT1G51630.1; AT1G51630.
DR   GeneID; 841588; -.
DR   Gramene; AT1G51630.1; AT1G51630.1; AT1G51630.
DR   KEGG; ath:AT1G51630; -.
DR   Araport; AT1G51630; -.
DR   TAIR; locus:2017652; AT1G51630.
DR   eggNOG; ENOG502QUE8; Eukaryota.
DR   HOGENOM; CLU_018420_3_0_1; -.
DR   InParanoid; Q0WPA5; -.
DR   OMA; LAYSCYC; -.
DR   OrthoDB; 695946at2759; -.
DR   PhylomeDB; Q0WPA5; -.
DR   PRO; PR:Q0WPA5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q0WPA5; baseline and differential.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0051753; F:mannan synthase activity; IMP:UniProtKB.
DR   GO; GO:0052325; P:cell wall pectin biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010412; P:mannan metabolic process; IMP:UniProtKB.
DR   GO; GO:0097502; P:mannosylation; IMP:UniProtKB.
DR   CDD; cd11299; O-FucT_plant; 1.
DR   InterPro; IPR024709; FucosylTrfase_pln.
DR   InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR   PANTHER; PTHR31288; PTHR31288; 1.
DR   Pfam; PF10250; O-FucT; 1.
DR   PIRSF; PIRSF009360; UCP009360; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Fucose metabolism; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..423
FT                   /note="Protein MANNAN SYNTHESIS-RELATED 2"
FT                   /id="PRO_0000442075"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        7..26
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        27..423
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   BINDING         264..266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H488"
SQ   SEQUENCE   423 AA;  47142 MW;  8D3572073C10C134 CRC64;
     MGVDLRQVVA GILTITMFVM LGQMLHRDYF DAVQEKVQGD AHDIEFHGSK VAVEDGLVRA
     FEAGTKGPWM EDSHELKPCW SISQSDEAVS SKGYVTFSLT NGPEYHVSQI TDAVMVAKHL
     GATLVLPDIR GSKPGDEMKF EDIYDVDKLI KTLESVVKVV RKLPSHVSLR DIAIVKVPTR
     VAEDYIKEHI DPIFKSKGNI RVTTYFPSVN LRKSSQGAET DPVSCLAMFG SLELQPAVNE
     LVESMIQRLK THSKKSGGRF IAIDLRVEIL EKKNCHETGA VGSKTCYNAQ EIALFLRKLG
     FDSDTTIYLT QPRWESSLNI LKDIFPKTYT KEAIMPSDKK TKYLELENSE YENVIDFYIS
     SRSDVFVPAI PGLFYANTVG KRIALGKPQV LVPAEISGTS GLPANYISPY ISKKNHLAYS
     CFC
 
 
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