ID R0FMI3_9BRAS Unreviewed; 591 AA.
AC R0FMI3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU362027};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU362027};
GN ORFNames=CARUB_v10016785mg {ECO:0000313|EMBL:EOA23221.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA23221.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
RN [2] {ECO:0000313|EMBL:EOA23221.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., Prochnik S., Nordborg M., Weigel D., Rokhsar D., Wright S.;
RT "Genome sequencing of Capsella rubella.";
RL Nat. Genet. 0:0-0(2013).
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004877, ECO:0000256|RuleBase:RU362027}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU362027}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU362027}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000256|ARBA:ARBA00006351, ECO:0000256|RuleBase:RU362027}.
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; KB870809; EOA23221.1; -; Genomic_DNA.
DR EMBL; KB870809; EOA23222.1; -; Genomic_DNA.
DR RefSeq; XP_006290323.1; XM_006290261.1.
DR RefSeq; XP_006290324.1; XM_006290262.1.
DR AlphaFoldDB; R0FMI3; -.
DR UniPathway; UPA00845; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR029993; GAUT.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR32116; GALACTURONOSYLTRANSFERASE 4-RELATED; 1.
DR PANTHER; PTHR32116:SF4; POLYGALACTURONATE 4-ALPHA-GALACTURONOSYLTRANSFERASE; 1.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU362027};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362027};
KW Golgi apparatus {ECO:0000256|RuleBase:RU362027};
KW Membrane {ECO:0000256|RuleBase:RU362027};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|RuleBase:RU362027};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362027}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362027"
FT REGION 115..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..264
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 67379 MW; DE6035110AAB0600 CRC64;
MALKRGLSGV NRIRGSSGGS RSALVLLIFF CVFSPLVFFV GRGVYIDSSN DYSSASVKQN
LDWRERLAMQ SVRSLFSKEV LDVISTSTAD LGPLSLDSFK KKNLPASWRG AGVDTSLGYS
ENQTTPDVKS NILNEKRDST SKDGGHQKVE TPAKLHRRQL REKRREMRAN ELVQHNDDTI
LKLENAAIER SKSVDSAVLG KYSIWRRENE NDNSDSNIRL MRDQVIMARV YSGIAKLKNK
NDLLQELQAR LKDSQRVLGE STSDADLPRS AHEKLRAMGQ VLAKAKMQLY DCKLVTGKLR
AMLQTADEQV RSLKKQSTFL AQLAAKTIPN PIHCLSMRLT IDYYLLSPEK RKFPRSENLE
NPNLYHYALF SDNVLAASVV VNSTIMNAKD PSKHVFHLVT DKLNFGAMNM WFLLNPPGKA
TIHVENVDEF KWLNSSYCPV LRQLESAAMR EYYFKADHPT SGSSNLKYRN PKYLSMLNHL
RFYLPEVYPK LNKILFLDDD IIVQKDLTPL WEVNLNGKVN GAVETCGESF HRFDKYLNFS
NPHIARNFNP NACGWAYGMN MFDLKEWKKR DITGIYHKWQ NMVIISLTLC N
//
