GenomeNet

Database: UniProt
Entry: D8S8L5_SELML
LinkDB: D8S8L5_SELML
Original site: D8S8L5_SELML 
ID   D8S8L5_SELML            Unreviewed;      1896 AA.
AC   D8S8L5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE            EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE   AltName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00032165};
GN   Name=Gsl2 {ECO:0000313|EMBL:EFJ19064.1};
GN   ORFNames=SELMODRAFT_177798 {ECO:0000313|EMBL:EFJ19064.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ19064.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC         beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC         COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC         Evidence={ECO:0000256|ARBA:ARBA00000192};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC       {ECO:0000256|ARBA:ARBA00009040}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL377607; EFJ19064.1; -; Genomic_DNA.
DR   RefSeq; XP_002979662.1; XM_002979616.1.
DR   STRING; 88036.D8S8L5; -.
DR   EnsemblPlants; EFJ19064; EFJ19064; SELMODRAFT_177798.
DR   Gramene; EFJ19064; EFJ19064; SELMODRAFT_177798.
DR   KEGG; smo:SELMODRAFT_177798; -.
DR   eggNOG; KOG0916; Eukaryota.
DR   HOGENOM; CLU_000742_1_1_1; -.
DR   InParanoid; D8S8L5; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR   InterPro; IPR026899; FKS1-like_dom1.
DR   InterPro; IPR003440; Glyco_trans_48.
DR   InterPro; IPR039431; Vta1/CALS_N.
DR   InterPro; IPR023175; Vta1/CALS_N_sf.
DR   PANTHER; PTHR12741:SF29; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 1.
DR   PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR   Pfam; PF14288; FKS1_dom1; 1.
DR   Pfam; PF02364; Glucan_synthase; 2.
DR   Pfam; PF04652; Vta1; 1.
DR   SMART; SM01205; FKS1_dom1; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        454..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        491..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        525..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        567..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        629..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        703..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1465..1488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1508..1530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1542..1562
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1629..1648
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1737..1757
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1777..1795
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1801..1821
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1842..1862
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          299..416
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
SQ   SEQUENCE   1896 AA;  218843 MW;  5973FF573D89B3CF CRC64;
     MTTRLPRTFT TGTFPTEFDS EVVPSSLGPI AAILRVANEV EQDSQRVAYL CRFYAFERAH
     YDDPSSSGRG VRQFKTALLQ RLEKDEEPSR LARRERSDAR EMQRFYQNYY DKYVKALEAD
     HQDRASLAKA YQTAGILFDV LTSVTRQDGA EVDSEMQAMN TDVTKKKKDI KHYNILPLDA
     AGASQAIMKL EEVRAAHDAI ANVRGLPKRK EAPSDILEWL QVMFGFQKDN VANQREHLIL
     LLANVHVSLD PEPSPLYKLD QRATEIVMKR MFKNYRTWCK FLGRSDKLEL PEIQLEVQQR
     MILYMALYLL IWGEAANVRF MPECLCYIFH HMASELSGML SGRVSYVTGE NIKPAYGSED
     EAFLKKVVTP IYNVIFKKES NRNESGGKPH SSWRNYDDLN EYFWSKTCFR LGWPMRKDDE
     FFVGAAEEAH SRSSKTNFVE ARSFWHLFRT FDRMWTFFIL WLQAMIIIAW NGSGSLGALF
     EGSVFKKVLS VFITAAVLRF FQALLDIIFS FKALHSLGYV GSIRLVLKVL VSAFWIVILS
     TSYVHSWEHP TGLTRTIKNL LGHNGGPSVY LVAVILYLVP NAIAAIFFLL PCVRRVAEES
     DAIPVRILLW WSQPPCYIGR GMHEEPLHLF SYTFFWIVLI TCKLLFSYYV EIKPLVEPTK
     FILDFTNVRF AWHEFFPHAR GNIGVLIALW TPVILVYFMD IQIWYSIMST IWGGVVGAFM
     RLGEIRTLSM LRSRFRALPT TFNWNLIPLE SSVKRKYQIL RKFKAHNKLE EARFAHLWNA
     VIESLREEDF LDDKEKELML LPYSADPYPS NNIIQWPPFL LASMAPMAIE MAKEYAEVQG
     ENVEDARLWN KIKENEYMRC AVEECYEFLK NILLRVVTGD TEKRLIHDLL KELEDRKAEG
     KLLENFRMND LPLLAGHFVR FLEFLDKPDP SDTARDKVVL LLQDMLEVFM HDMMKFESSH
     GLNMKPTDNQ SVMGGKGKIQ FFAGKDSILY PLPEDHAWSE QIKRVLLLLT ETESAMDVPK
     NLDARRRITF FTNSLFMKMP PAPRVRKMIP FSVLTPFYEE EVLYSKNVIE EPNEDGVSIL
     FYLQNVYPDE WNKFLERVNC STEEEVEEAA LRDWTSYRGQ TLSRTVRGMM YYRTALELQA
     FLDLAPDEDV YTGFKEVSKR RKEEKGQDSF WAKLDAIVDM KFTFVATCQK FGQQKHSKDL
     KEASKAQDIQ KLMTKYPSLR VAYVLEEEPS KGKPQKSYYS VLSKAVDGRD EEIYKIRLPG
     PVNIGEGKPE NQNHAIIFTR GLGLQTIDMN QENYLEEAFK VRNLLEEFKS RHGARFPTIL
     GVREHIFTGS VSSLAWFMSN QETSFVTIGQ RVLATPLKVR FHYGHPDVFD RIFHITRGGV
     SKASKGINLS EDIFAGFNST LRRGLVTHHE YIQVGKGRDV GLNQISIFEA KVANGNGEQT
     LSRDVYRLGH RFDFFRMLSF YITTVGYYFS TMIVILTVYV FLYGRLYLAL SGLERSFVRA
     AQQNTDSALQ SALASQSLIQ LGLLMALPMV MEIGLERGFR MALSDLIVMQ LQLASVFFTF
     TLGSKVHYYG RTIFHGGAKY RATGRGFVVR HEKFPDNYRL YSRSHFVKGF ELMILLIIYD
     VYGSQTRNAV SYVLITFSMW FLVGTWLFSP FLFNPSGFEW QKIVEDWNDW NKWISSKGRI
     GVPANKSWES WWEEEQDHLQ NTGFRGRVFE VILALRFVLY QYGIVYQLNI MRGNKSLSMY
     GLSWVVICVV LFTLKAVSLG RKKFKANFQL VFRMLKGVIF VAVLSVIAVL FRFAHLTVGD
     LFASILAFVP TGWGLLQIFQ ACRPVIVTYG MWDSVQALAR TYEYVMGLLL FAPVAILAWF
     PFVSEFQTRL LFNQAFSRGL QISRILAGKR KKVADD
//
DBGET integrated database retrieval system