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CSLA3_ARATH
ID   CSLA3_ARATH             Reviewed;         556 AA.
AC   Q9LQC9; Q3ED64; Q9ZUE5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable glucomannan 4-beta-mannosyltransferase 3 {ECO:0000305};
DE            EC=2.4.1.32 {ECO:0000250|UniProtKB:Q9LZR3};
DE   AltName: Full=Cellulose synthase-like protein A3 {ECO:0000303|PubMed:11027699};
DE            Short=AtCslA3 {ECO:0000303|PubMed:11027699};
DE   AltName: Full=Glucomannan synthase {ECO:0000305};
DE   AltName: Full=Mannan synthase 3 {ECO:0000305};
GN   Name=CSLA3 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At1g23480;
GN   ORFNames=F28C11.11, F5O8.4;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11027699; DOI=10.1104/pp.124.2.495;
RA   Richmond T.A., Somerville C.R.;
RT   "The cellulose synthase superfamily.";
RL   Plant Physiol. 124:495-498(2000).
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:Q9LZR3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1.;
CC         EC=2.4.1.32; Evidence={ECO:0000250|UniProtKB:Q9LZR3};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LQC9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LQC9-2; Sequence=VSP_031472;
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC       cellulose synthase-like A subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC98005.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC005990; AAC98005.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC007945; AAF79586.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30391.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30392.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30393.1; -; Genomic_DNA.
DR   EMBL; AY099769; AAM20620.1; -; mRNA.
DR   EMBL; BT000203; AAN15522.1; -; mRNA.
DR   PIR; D86368; D86368.
DR   RefSeq; NP_001031084.1; NM_001036007.2. [Q9LQC9-2]
DR   RefSeq; NP_173762.4; NM_102197.5. [Q9LQC9-1]
DR   RefSeq; NP_850952.1; NM_180621.3. [Q9LQC9-1]
DR   AlphaFoldDB; Q9LQC9; -.
DR   STRING; 3702.AT1G23480.2; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PaxDb; Q9LQC9; -.
DR   PRIDE; Q9LQC9; -.
DR   ProteomicsDB; 224423; -. [Q9LQC9-1]
DR   EnsemblPlants; AT1G23480.1; AT1G23480.1; AT1G23480. [Q9LQC9-1]
DR   EnsemblPlants; AT1G23480.2; AT1G23480.2; AT1G23480. [Q9LQC9-1]
DR   EnsemblPlants; AT1G23480.3; AT1G23480.3; AT1G23480. [Q9LQC9-2]
DR   GeneID; 838956; -.
DR   Gramene; AT1G23480.1; AT1G23480.1; AT1G23480. [Q9LQC9-1]
DR   Gramene; AT1G23480.2; AT1G23480.2; AT1G23480. [Q9LQC9-1]
DR   Gramene; AT1G23480.3; AT1G23480.3; AT1G23480. [Q9LQC9-2]
DR   KEGG; ath:AT1G23480; -.
DR   Araport; AT1G23480; -.
DR   TAIR; locus:2028862; AT1G23480.
DR   eggNOG; ENOG502QR7J; Eukaryota.
DR   InParanoid; Q9LQC9; -.
DR   OMA; QTRIFVF; -.
DR   PhylomeDB; Q9LQC9; -.
DR   BioCyc; ARA:AT1G23480-MON; -.
DR   PRO; PR:Q9LQC9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LQC9; baseline and differential.
DR   Genevisible; Q9LQC9; AT.
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   Alternative splicing; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..556
FT                   /note="Probable glucomannan 4-beta-mannosyltransferase 3"
FT                   /id="PRO_0000319328"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000255"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_031472"
SQ   SEQUENCE   556 AA;  64402 MW;  A427612B7E849E1F CRC64;
     MSPFLKFFLF LYDYLSPSSF FLVQRNTLGA SLDTTDGVVR SGIIGEIIYI WKQTRIFVFI
     PILKCLVTIC LVMSLLLFIE RVYMSIVVVF VKLLRRTPEK VHKWEPINDD DLELANTNYP
     MVLIQIPMYN EKEVCQLSIG AACRLSWPLD RMIVQVLDDS TDPASKELVN AECDKWARKG
     INIMSEIRDN RIGYKAGALK AGMMHNYVKQ CEFVAIFDAD FQPDPDFLER TIPFLIHNHE
     ISLVQCRWKF VNANECLMTR MQEMSLNYHF VAEQESGSSI HAFFGFNGTA GVWRIAALNE
     AGGWKDRTTV EDMDLAVRAC LHGWKFVYVH DVEVKNELPS TFKAYRFQQH RWSCGPANLW
     RKMTMEILQN KKVSAWKKLY LIYNFFFIRK IVVHIFTFVF YCLILPTTVL FPELQVPKWA
     TVYFPTTITI LNAIATPRSL HLLVFWILFE NVMSMHRTKA TFIGLLEAGR VNEWVVTEKL
     GDTLKSKLIG KATTKLYTRF GQRLNWRELV VGLYIFFCGC YDFAYGGSYF YVYLFLQSCA
     FFVAGVGYIG TFVPTV
 
 
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