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Database: UniProt
Entry: A0A022RMC1_ERYGU
LinkDB: A0A022RMC1_ERYGU
Original site: A0A022RMC1_ERYGU 
ID   A0A022RMC1_ERYGU        Unreviewed;      1895 AA.
AC   A0A022RMC1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=MIMGU_mgv1a000075mg {ECO:0000313|EMBL:EYU40120.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU40120.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU40120.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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}.
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DR   EMBL; KI630427; EYU40120.1; -; Genomic_DNA.
DR   STRING; 4155.A0A022RMC1; -.
DR   eggNOG; KOG0916; Eukaryota.
DR   Proteomes; UP000030748; 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   InterPro; IPR026899; FKS1-like_dom1.
DR   InterPro; IPR003440; Glyco_trans_48.
DR   PANTHER; PTHR12741:SF67; CALLOSE SYNTHASE 10; 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   SMART; SM01205; FKS1_dom1; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000030748};
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        495..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        524..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        561..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        594..617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        658..679
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        718..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1457..1482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1517..1540
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1606..1624
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1630..1653
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1735..1755
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1767..1790
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1802..1819
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1839..1859
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          346..459
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
SQ   SEQUENCE   1895 AA;  217082 MW;  19AA4FC02AE360AA CRC64;
     MARVTTPSDN WEKLVRAVLR SEQRAGHERT TSGIAGAVPD SLQRTTNINA ILQAADEIQS
     EDPNVARILC EQAYSMAQNL DPSSDGRGVL QFKTGLMSVI KQKLAKKEGG QIDRNRDIER
     LWEFYNQYKR RHRVDDIQRE EQKWREAGTF SADVGDLELR FSEMKKVFAT LRALVEVMEA
     LSKDATSDGV GRLIMEELRR IKKSSAAISG ELIPYNIVPL EAPSLTNAIG YFPEVRGAIS
     AIRYTEQFPR LPADFETPGQ RELDMFDLLE YVFGFQKDNI RNQREHVVLA LANAQSRLGI
     PIDADPKLDE RAVREVFLKS LDNYIKWCKY LRIRLVWNSL EAINKDRKLF LVSLYFCIWG
     EAANARFLPE CICYIFHQMA RELDAILDRA EATQAASCTG ENGSVSFLEQ IICPIYGALA
     AEAERNNNGK AAHSEWRNYD DFNEYFWSPA CFELSWPMKR NSSFLLKPKK GKRTGKSSFV
     EHRTFLHLFR SFHRLWMFLI IMFQALAIIA FHDGKLNLNT FKSLLSIGPT FAVMNFLESC
     LDVVLMFGAY STARGMAISR LVIRFFWCGL SSVFVLYVYV RLLQERNKNT SDSLYFRIYV
     LVLGVYAGLR VLFALLLKFP ACHRLSEMSD QSFFQFFKWI YEERYFVGRG LVEKTTDYMS
     YVFFWLVIFA CKFPFAYFLQ IKPLVGPTLI IIHLPRLQYS WHDFVSKNNN NMLTVASLWA
     PVVAIYIMDI HIWYTLLSAI YGAVMGARGR LGEIRSIEMV HKRFESFPEA FVKNLVSPQI
     KSPHDNNKTY AAIFSPFWNE IIKALREEDY ISNREMDLLS MPSNAGSLKL VQWPLFLLSS
     KILLAIDLAL DCKDTQADLW NRICKDEYMA YAVQECYSSI EKILHSLVDG EGRLWVERIF
     REINSSISEG SLVITLHLKK LQVVLSRFTA LTGLLIRDPT PELAKGAAKA VYDFYDVVTH
     ELLSSDLREQ LDTWQILLRA RNEGRLFSRI EWPKDPDIKE QVKRLHLLLT VKDNAVNIPK
     NLEARRRLQF FTNSLFMDMP SAKPVCEMMP FCVFTPYYSE TVLYSNSELR LENEDGISTL
     FYLQKIFPDE WENFLERIGQ GDIGYAEIQE NSTSALELRF WASYRGQTLA RTVRGMMYYR
     KALMLQSHLE RRSLEEDVSS RTSFTTQGFE LSREARAQAD IKFTYVVSCQ IYGQQKQRKA
     PEAADIALLL QRNEALRVAF IHVEESGAAD GNVTKEFYSK LVKADANGKD QEIFSIRLPG
     DPKLGEGKPE NQNHAIVFTR GEAVQTIDMN QDNYLEEAMK MRNLLEEFRA NHGLRPPTIL
     GVREHVFTGS VSSLAWFMSN QETSFVTLGQ RVLACPLKVR MHYGHPDVFD RIFHITRGGI
     SKSSRVINIS EDIYAGFNST LRQGNITHHE YIQVGKGRDV GLNQIALFEG KVAGGNGEQV
     LSRDVYRLGQ LFDFFRMLSF FFTTVGFYVC TMMTVLTVYV FLYGRAYLAF SGLDQGISDE
     ADVLGNTALD TVLNAQFLVQ IGIFTAVPMV MGFILELGLL QAVFSFITMQ LQLCSVFFTF
     SLGTRTHYFG RTILHGGAKY RATGRGFVVR HIKFAENYRL YSRSHFVKAL EVALLLIVYM
     AYGYSEGGAV TFVLLTISSW FLVFSWLFAP YIFNPSGFEW QKTVEDFDDW TNWLMYKGGV
     GVKGDNSWES WWEEEQTHIQ TLRGRILETI LSFRFIMFQY GIVYKLHLTG RDTSIAVYGF
     SWVVLAGLVM IFKIFTFSPK KSTNFQLVLR FMQGITCIGL IVALCLVVFF TDLSIPDLFA
     SFLAFIPTGW FILSLAIAWR SIVRSLGLWD SVKEFARMYD AGMGILIFSP IAVLSWFPFV
     STFQSRLLFN QAFSRGLEIS LILAGNKANV EASSF
//
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