ID D8SMF9_SELML Unreviewed; 1129 AA.
AC D8SMF9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Cellulose synthase-like D2-2, glycosyltransferase family 2 protein {ECO:0000313|EMBL:EFJ14485.1};
GN Name=CSLD2-2 {ECO:0000313|EMBL:EFJ14485.1};
GN ORFNames=SELMODRAFT_120069 {ECO:0000313|EMBL:EFJ14485.1};
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:EFJ14485.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; GL377627; EFJ14485.1; -; Genomic_DNA.
DR RefSeq; XP_002984435.1; XM_002984389.1.
DR AlphaFoldDB; D8SMF9; -.
DR STRING; 88036.D8SMF9; -.
DR EnsemblPlants; EFJ14485; EFJ14485; SELMODRAFT_120069.
DR GeneID; 9644283; -.
DR Gramene; EFJ14485; EFJ14485; SELMODRAFT_120069.
DR KEGG; smo:SELMODRAFT_120069; -.
DR eggNOG; ENOG502QU14; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; D8SMF9; -.
DR OMA; TWRITHQ; -.
DR OrthoDB; 1210919at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR GO; GO:0051753; F:mannan synthase activity; IBA:GO_Central.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13301:SF58; CELLULOSE SYNTHASE-LIKE PROTEIN D3; 1.
DR PANTHER; PTHR13301; X-BOX TRANSCRIPTION FACTOR-RELATED; 1.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF14570; zf-RING_4; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
PE 4: Predicted;
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, ECO:0000313|EMBL:EFJ14485.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 905..926
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 973..991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1028..1050
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1056..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 126019 MW; 2114A7F1E7AF6F67 CRC64;
MESPASSVSI SSSRRPFREL LSPRNLNTSI DSPRFLPPRS PRFLKSGTPS PTACSTPPSH
RSPGGSYVFM PREGNDPGRE AVSTAKNYTV LIPPTPDPGF LAAPKTGDMA SAMFTGGFQS
VTRGHVMDQM KEAKVVMTLS CAIAGCDGKA MKDEMGEDLS PCECAFRICR DCYFDAINNG
GKCPGCKEMY KVLDIEGPNA ETLPLPAPRR LSLLRSNQPG SMKQDFDHTR WLYETKGTYG
YGNALWPKDD TYFGDGMPSS FKDKARRPLT RKTNVSAAIL SPYRLLVFVR LAALGLFITW
RIRHPNPEAM WLWGLSIVCE LWFAFSWILD QLPKLCPVNR TTNLAVLKDE FERPTAKNPK
GRSDLPGIDI FVSTADPEKE PSLVTANTIL SILAAEYPVE KLCCYLSDDG GSLLTFEALA
EAASFSRIWV PFCRKHSIEP RNPEAYFMLK GDPTKNKVRA DFVKDRRRVK REYDEFKVRI
NGLGDAIRRR SDAYNAHEEI RAKRIQVDSG CNPGEPLNVP KATWMADGTH WPGTWLSSGS
EHGRGDHAGI IQVMLAPPST EHLMGSADND NNLIDTSDCD IRLPMLVYVS REKRAGYDHN
KKAGAMNALV RTSAIMSNGA FILNLDCDHY VYNSLAFREG MCFMMDNGGD RIGFVQFPQR
FEGIDHNDRY ANHNTVFFDV NMRALDGIQG PVYVGTGCLF RRVALYGFDP PRCKTRSCWN
RRKTRLTKKN TGISMEENED DLEAQTLLPK RYGTSTSFVA SISNAEFQGR PLSGQGVMLG
RPAASLISPR EPLDAATVAE AINVISCWYE DKTEWGQNVG WTYGSVTEDV VTGYTMHNKG
WKSVYCVTKR DAFRGTAPIN LTDRLHQVLR WATGSVEIFY SRNNALFAST RMKFLQRIAY
LNVGIYPFTS IFLTVYCFLP ALSLLTGKFI VQTLNVTFLV YLLIITVTIC LLAVLEIRWS
GITLDEWWRN EQFWVIGGTS AHLVAVFQGL LKVIAGIDIS FTLTSKNSGD EDDEFAELYM
VKWSALMIPP LTIMMVNLIA IAVAVSRTVY SPVPQWSKLL GGVFFSVWVL FHLYPFSKGL
MGRRRRTPTI IFVWSGLLAI VISLLWVSLS SSSLTPDKGM GIGGSFQFP
//
