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CSLA2_ORYSJ
ID   CSLA2_ORYSJ             Reviewed;         580 AA.
AC   Q7PC67; Q0IXV9; Q7XEU7; Q8W1N9; Q948I4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Probable glucomannan 4-beta-mannosyltransferase 2 {ECO:0000305};
DE            EC=2.4.1.32 {ECO:0000250|UniProtKB:Q7PC76};
DE   AltName: Full=Cellulose synthase-like protein A2 {ECO:0000303|PubMed:11842136};
DE            Short=OsCslA2 {ECO:0000303|PubMed:11842136};
DE   AltName: Full=Glucomannan synthase {ECO:0000305};
DE   AltName: Full=Mannan synthase 2 {ECO:0000305};
GN   Name=CSLA2 {ECO:0000303|PubMed:11842136};
GN   OrderedLocusNames=Os10g0406400, LOC_Os10g26630; ORFNames=OSJNBa0060A14.12;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 317-580, IDENTIFICATION, GENE FAMILY, AND
RP   NOMENCLATURE.
RX   PubMed=11842136; DOI=10.1104/pp.010875;
RA   Hazen S.P., Scott-Craig J.S., Walton J.D.;
RT   "Cellulose synthase-like genes of rice.";
RL   Plant Physiol. 128:336-340(2002).
CC   -!- FUNCTION: Probable mannan synthase which consists of a 4-beta-
CC       mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-
CC       mannan product is the backbone for galactomannan synthesis by
CC       galactomannan galactosyltransferase. Galactomannan is a noncellulosic
CC       polysaccharides of plant cell wall. {ECO:0000250|UniProtKB:Q7PC76}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1.;
CC         EC=2.4.1.32; Evidence={ECO:0000250|UniProtKB:Q7PC76};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC       cellulose synthase-like A subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK98678.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAP53691.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF26478.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC021893; AAK98678.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000086; AAP53691.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008216; BAF26478.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF435640; AAL38525.1; -; mRNA.
DR   EMBL; BK000092; DAA01755.1; -; Genomic_DNA.
DR   RefSeq; XP_015612871.1; XM_015757385.1.
DR   AlphaFoldDB; Q7PC67; -.
DR   SMR; Q7PC67; -.
DR   STRING; 4530.OS10T0406400-00; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PaxDb; Q7PC67; -.
DR   PRIDE; Q7PC67; -.
DR   GeneID; 4348586; -.
DR   KEGG; osa:4348586; -.
DR   eggNOG; ENOG502SHF0; Eukaryota.
DR   InParanoid; Q7PC67; -.
DR   OrthoDB; 559375at2759; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0047259; F:glucomannan 4-beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0051753; F:mannan synthase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..580
FT                   /note="Probable glucomannan 4-beta-mannosyltransferase 2"
FT                   /id="PRO_0000319373"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        437..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        528..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        335
FT                   /evidence="ECO:0000255"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   580 AA;  65341 MW;  9D8ABF4975DBFA5B CRC64;
     MSTNGGAPSQ KRSWLPSRPL LTTTTQTYPP PLLPFKKLHA PPTAARRSLP PAASKPMASS
     SSSSLPAAWA AAVRAWAVAP ALRAAVWACL AMSAMLVAEA AWMGLASLAA AAARRLRGYG
     YRWEPMAAPP DVEAPAPAPA EFPMVLVQIP MYNEKEVYKL SIGAACALTW PPDRIIIQVL
     DDSTDPFVKE LVELECKEWA SKKINIKYEV RNNRKGYKAG ALRKGMEHTY AQLCDFVAIF
     DADFEPESDF LLKTMPYLLH NPKIALVQTR WEFVNYNVCL MTRIQKMSLD YHFKVEQESG
     SFMHAFFGFN GTAGVWRVSA INQSGGWKDR TTVEDMDLAV RASLKGWEFL YVGDIRVKSE
     LPSTFQAYRH QQHRWTCGAA NLFRKMAWEI ITNKEVSMWK KYHLLYSFFF VRRAIAPILT
     FLFYCIVIPL SAMVPEVTIP VWGLVYIPTA ITIMNAIRNP GSVHLMPFWI LFENVMAMHR
     MRAALSGLLE TARANDWVVT EKVGDQVKDE LDVPLLEPLK PTECAERIYI PELLLALYLL
     ICASYDFVLG NHKYYIYIYL QAVAFTVMGF GFVGTRTPCS
 
 
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