ID A0A1S2XMP8_CICAR Unreviewed; 1957 AA.
AC A0A1S2XMP8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=LOC101513869 {ECO:0000313|RefSeq:XP_004491686.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004491686.1};
RN [1] {ECO:0000313|RefSeq:XP_004491686.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004491686.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_004491686.1; XM_004491629.3.
DR STRING; 3827.A0A1S2XMP8; -.
DR PaxDb; 3827-XP_004491686-1; -.
DR GeneID; 101513869; -.
DR KEGG; cam:101513869; -.
DR eggNOG; KOG0916; Eukaryota.
DR OrthoDB; 211713at2759; -.
DR Proteomes; UP000087171; Chromosome Ca3.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
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:SF48; CALLOSE SYNTHASE 3; 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; 1.
DR Pfam; PF04652; Vta1; 1.
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:UP000087171};
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 523..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1517..1539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1568..1587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1599..1620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1662..1679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1686..1710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1764..1783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1795..1812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1832..1852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1859..1880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1900..1921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 319..435
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1957 AA; 226128 MW; A6D88ADF227B5ED6 CRC64;
MSSSSRGAGP SEPPQRRIIR TQTAGNLGES IFDSEVVPSS LVEIAPILRV ANEVEKTHPR
VAYLCRFYAF EKAHRLDPTS SGRGVRQFKT ALLQRLEREN DPTLKGRVKK SDAREMQSFY
QHYYKKYIQA LQNAADKADR AQLTKAYQTA NVLFEVLKAV NMTQSMEVDR EILETQDKVA
EKTEILVPYN ILPLDPDSAN QAIMRFPEIQ AAVFALRNTR GLLWPKDYKK KKDEDILDWL
GSMFGFQKHN VANQREHLIL LLANVHIRQF PKPDQQPKLD ERALTEVMKK LFKNYKKWCK
YLDRKSSLWL PTIQQEVQQR KLLYMGLYLL IWGEAANLRF MPECLCYIYH HMAFELYGML
AGNVSPMTGE NIKPAYGGEE EAFLRKVVTP IYNVIAEEAK KSKKGRSKHS QWRNYDDLNE
YFWSADCFRL GWPMRADADF FSLPSERVVF DKSNDDKPAN RDRWVGKVNF VEIRSFWHLF
RSFDRMWSFF ILSLQAMIIV AWNGSGDPTV IFNGDVFKKV LSVFITAAIL KLGQAVLDVI
VSWKARQSMS LYVKLRYILK VVSAAAWVIV LSVTYAYTWD NPPGFAQTIK SWFGSSSSAP
SLFILAVVVY LSPNMLAAIF FLFPFIRRYL ERSNYRIVML MMWWSQPRLY VGRGMHESTF
SLFKYTMFWF LLIVTKLAFS YYIEIKPLVG PTKAIMSVKI TTFQWHEFFP HARNNIGVVV
ALWAPIMLVY FMDTQIWYAI FSTLFGGIYG AFRRLGEIRT LGMLRSRFQT LPGAFNASLI
PEETTDEPRK KGLKATLSRR FTEVPSNKGK KAARFAQLWN QIITSFREED LISDREMDLL
LVPYWADTQL DLIQWPPFLL ASKIPIALDM AKDSNGKDRE LTKIIEADNY MFCAVRECYA
SFKSIMMQLV RGEREKPVIE FMFSEVDKHI AEGTLIKEFK MSALPSLYEQ FVQLIKYLLE
NNQKDRDQVV ILFQDMLEVM TRDIMMEDQD QIFRLVDSNH GGAGHEGMFP LEPEPQHQLF
ASEGAIRFPI EPVTAAWTEK IKRLFLLLTT KESAMDVPSN LEARRRISFF SNSLFMDMPL
APKVRNMLSF SVLTPYYTEE VLFSLHNLDS PNEDGVSILF YLQKIFPDEW NNFLQRVKCS
SEEELKGNEY EELEEELRLW ASYRGQTLTR TVRGMMYYRK ALELQAFLDM AKDEDLMEGY
KAMENLDDNS RGEKSLLTQC QAVADMKFTY VVSCQQYGID KRSGSLRAHD ILRLMTRYPS
LRVAYIDEVE EPIKDTKKKI NKVYYSCLVK AMPKSSSPSE PEQNLDQVIY KIKLPGPAIL
GEGKPENQNH AIIFTRGEGL QTIDMNQDNY MEEALKMRNL LQEFLKKHDG VRFPSILGLR
EHIFTGSVSS LAWFMSNQET SFVTIGQRLL ANPLRVRFHY GHPDVFDRLF HLTRGGVSKA
SKVINLSEDI FAGFNSTLRE GSVTHHEYIQ VGKGRDVGLN QISMFEAKIA NGNGEQTLSR
DVYRLGHRFD FFRMLSCYFT TVGFYFSTLI TVLTVYVFLY GRLYLVLSGL EEGLSTQKAI
RDNKPLQVAL ASQSFVQIGF LMALPMLMEI GLERGFRTAL SEFILMQLQL APVFFTFSLG
TKTHYFGRTL LHGGAKYRST GRGFVVFHAK FADNYRLYSR SHFVKGIELM ILLVIYQIFG
HSYRGAVAYV LITVSMWFMV GTWLFAPFLF NPSGFEWQKI VDDWTDWNKW ISNRGGIGVL
PEKSWESWWE EEQDHLQYSG IRGIIVEILL SLRFFIYQYG LVYHLNITKK GSKSFLVYGI
SWLVIFVILF VMKTVSVGRR KFSANFQLVF RLIKGMIFVT FVSILVILIA LPHMTLQDIV
VCVLAFMPTG WGILQIAQAL KPIVRRAGFW GSVKTLARGY EIVMGLLLFT PVAFLAWFPF
VSEFQTRMLF NQAFSRGLQI SRILGGQRKE RSSRNKE
//
