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Database: UniProt
Entry: CSLA1_ARATH
LinkDB: CSLA1_ARATH
Original site: CSLA1_ARATH 
ID   CSLA1_ARATH             Reviewed;         553 AA.
AC   Q84W54; F4JMI4; O23502; Q56X10; Q56ZJ0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-JUN-2019, entry version 96.
DE   RecName: Full=Probable glucomannan 4-beta-mannosyltransferase 1 {ECO:0000305};
DE            EC=2.4.1.32 {ECO:0000250|UniProtKB:Q9LZR3};
DE   AltName: Full=Cellulose synthase-like protein A1 {ECO:0000303|PubMed:11027699};
DE            Short=AtCslA1 {ECO:0000303|PubMed:11027699};
DE   AltName: Full=Glucomannan synthase {ECO:0000305};
DE   AltName: Full=Mannan synthase 1 {ECO:0000305};
GN   Name=CSLA1 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At4g16590;
GN   ORFNames=dl4320w, FCAALL.402;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L.,
RA   Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
RA   Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
RA   Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
RA   Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
RA   Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
RA   Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
RA   Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
RA   Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
RA   Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
RA   Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
RT   Arabidopsis thaliana.";
RL   Nature 391:485-488(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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
CC       beta-1,4-mannan product is the backbone for galactomannan
CC       synthesis by galactomannan galactosyltransferase. Galactomannan is
CC       a noncellulosic polysaccharides of plant cell wall.
CC       {ECO:0000250|UniProtKB:Q9LZR3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-mannose + (glucomannan)(n) = GDP +
CC         (glucomannan)(n+1).; EC=2.4.1.32;
CC         Evidence={ECO:0000250|UniProtKB:Q9LZR3};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
CC       Multi-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=BAD94168.1; Type=Frameshift; Positions=468; Evidence={ECO:0000305};
CC       Sequence=BAD94550.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAB10434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB10434.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC       Sequence=CAB78701.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78701.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
DR   EMBL; Z97341; CAB10434.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161544; CAB78701.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BT004213; AAO42230.1; -; mRNA.
DR   EMBL; AK220975; BAD94550.1; ALT_INIT; mRNA.
DR   EMBL; AK221869; BAD94168.1; ALT_FRAME; mRNA.
DR   PIR; H71432; H71432.
DR   STRING; 3702.AT4G16590.1; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PaxDb; Q84W54; -.
DR   PRIDE; Q84W54; -.
DR   Araport; AT4G16590; -.
DR   TAIR; locus:2130844; AT4G16590.
DR   eggNOG; COG1215; LUCA.
DR   HOGENOM; HOG000238309; -.
DR   InParanoid; Q84W54; -.
DR   OrthoDB; 559375at2759; -.
DR   PhylomeDB; Q84W54; -.
DR   BioCyc; ARA:AT4G16590-MONOMER; -.
DR   PRO; PR:Q84W54; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q84W54; baseline and differential.
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:0051753; F:mannan synthase activity; IBA:GO_Central.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Complete proteome;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    553       Probable glucomannan 4-beta-
FT                                mannosyltransferase 1.
FT                                /FTId=PRO_0000319326.
FT   TRANSMEM     64     84       Helical. {ECO:0000255}.
FT   TRANSMEM    395    415       Helical. {ECO:0000255}.
FT   TRANSMEM    431    451       Helical. {ECO:0000255}.
FT   TRANSMEM    510    530       Helical. {ECO:0000255}.
FT   TRANSMEM    531    551       Helical. {ECO:0000255}.
FT   ACT_SITE    163    163       {ECO:0000255}.
FT   ACT_SITE    316    316       {ECO:0000255}.
FT   BINDING     222    222       Substrate. {ECO:0000255}.
FT   BINDING     224    224       Substrate. {ECO:0000255}.
FT   CONFLICT    455    455       N -> D (in Ref. 5; BAD94550).
FT                                {ECO:0000305}.
SQ   SEQUENCE   553 AA;  64103 MW;  816F0FAE34D3ADB7 CRC64;
     MSLFLKPFLF LYDTTLSLLL LLFNGWSLED TAAAQKRREA DKNAAETEWI QLQYLWTKTR
     SVVLLPVFKG LVVMCLVLSI IVFFESFYMN FVILFVKLFK RKPHKVYKWE AMQEDVEVGP
     DNYPMVLIQI PMYNEKEVFQ LSIAAICSLV WPSSRLVVQV VDDSTDPAVR EGVDVEIAKW
     QSQGINIRCE RRDNRNGYKA GAMKEALTQS YVKQCDFVAV FDADFQPEPD YLIRAVPFLV
     HNPDVALVQA RWIFVNANKC LMTRMQEMSL NYHFKVEQES GSTRHAFFGF NGTAGVWRIS
     AMEAAGGWKS RTTVEDMDLA VRVGLHGWKF VYLNDLTVRN ELPSKFKAYR FQQHRWSCGP
     ANLFRKMTME IIFNKRVSIW KKFYVIYSFF FVRKVAVHFL TFFFYCIIVP TSVFFPEIHI
     PSWSTIYVPS LISIFHTLAT PRSFYLVIFW VLFENVMAMH RTKGTCIGLL EGGRVNEWVV
     TEKLGDALKS KLLSRVVQRK SCYQRVNSKE VMVGVYILGC ALYGLIYGHT WLHFYLFLQA
     TAFFVSGFGF VGT
//
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