ID   A0A444Z7V7_ARAHY        Unreviewed;      1139 AA.
AC   A0A444Z7V7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   10-JUN-2026, entry version 22.
DE   RecName: Full=Cellulose synthase domain-containing protein {ECO:0000259|Pfam:PF03552};
GN   ORFNames=Ahy_B05g078721 {ECO:0000313|EMBL:RYR10249.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR10249.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR10249.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738}, and
RC   GDAAS-fuhuasheng2018 {ECO:0000313|EMBL:RYR10249.1};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR10249.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004653}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC       cellulose synthase-like D subfamily. {ECO:0000256|ARBA:ARBA00061286}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RYR10249.1}.
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DR   EMBL; SDMP01000015; RYR10247.1; -; Genomic_DNA.
DR   EMBL; SDMP01000015; RYR10248.1; -; Genomic_DNA.
DR   EMBL; SDMP01000015; RYR10249.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A444Z7V7; -.
DR   SMR; A0A444Z7V7; -.
DR   STRING; 3818.A0A444Z7V7; -.
DR   Gramene; arahy.Tifrunner.gnm2.ann2.Ah15g149300.1; arahy.Tifrunner.gnm2.ann2.Ah15g149300.1-CDS; arahy.Tifrunner.gnm2.ann2.Ah15g149300.
DR   OrthoDB; 72851at2759; -.
DR   Proteomes; UP000289738; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR   GO; GO:0051753; F:mannan synthase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR   GO; GO:0009409; P:response to cold; IEA:UniProtKB-ARBA.
DR   FunFam; 3.30.40.10:FF:000229; Cellulose synthase-like protein D3; 1.
DR   FunFam; 3.90.550.10:FF:000040; cellulose synthase-like protein D3; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
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; 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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
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        278..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        912..935
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        947..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1045..1067
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1073..1091
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1103..1123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          369..1129
FT                   /note="Cellulose synthase"
FT                   /evidence="ECO:0000259|Pfam:PF03552"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..19
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-1"
FT   ACT_SITE        842
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-1"
FT   BINDING         374
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-2"
FT   BINDING         380
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-2"
FT   BINDING         381
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-2"
FT   BINDING         410
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-2"
FT   BINDING         602
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-2"
FT   BINDING         603
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-3"
FT   BINDING         627
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605150-3"
SQ   SEQUENCE   1139 AA;  127873 MW;  15B8305FD11C1745 CRC64;
     MASKSFKPSR LSQSSSTRSD VNESQKVTFA RRTSSGRYVS YSRDDLDSEL GSTDFANYTV
     HLPPTPDNQP MDPSISQKVE EQYVSNSLFT GGFNSVTRAH LMDKVIESEA NHPQMAGAKG
     SSCAIPGCDS KVMSDERGVD ILPCECDFKI CRDCYIDAVK AGGGICPGCK EPYKNTELDE
     VAVDNSRPLP LPPPSGMSKM ERRLSLMKST KSALMRSQTG DFDHNRWLFE TKGTYGYGNA
     IWPKEGGFGN EKEDGVAEPT ELMNRPWRPL TRKLKIPAAV LSPYRLLIFV RLVVLTLFLM
     WRVSHKNTDA IWLWGMSVVC EIWFAFSWLL DQLPKLCPIN RSTDLNVLKE KFETPTPNNP
     TGKSDLPGID VFVSTADPEK EPPLVTANTI LSILAADYPV EKLSCYVSDD GGALLTFEAM
     AEAASFANIW VPFCRKHDIE PRNPESYFSL KRDPYKNKVK PDFVKDRRRV KREYDEFKVR
     INSLPDSIRR RSDAYHAREE IKAMKLQRQN KEDEPIEPAK IPKATWMADG THWPGTWLSP
     TSEHTRGDHA GIIQVMLKPP SDEPLLGNAD DTKLIDVTNV DIRLPLLVYV SREKRPGYDH
     NKKAGAMNAL VRASAIMSNG PFILNLDCDH YIYNSKAMRE GMCFMMDRGG DRICYVQFPQ
     RFEGIDPSDR YANHNTVFFD VNMRALDGLQ GPVYVGTGCL FRRVALYGFD PPRSKEHNQG
     CCSCCFGRQK KLASMASTPE ENRALRMGES DDEEMNLSLF PKKFGNSTFL IDSIPVAEFQ
     GRPLADHPAV KNGRPPGALT IPRDLLDAST VAEAISVISC WYEDKTEWGQ RVGWIYGSVT
     EDVVTGYRMH NRGWKSVYCV TKRDAFRGTA PINLTDRLHQ VLRWATGSVE IFFSRNNALL
     ASPRMKFLQR IAYLNVGIYP FTSIFLIVYC FLPALSLFSG QFIVQTLNVT FLSYLLGITI
     TLCMLAVLEI KWSGIELEEW WRNEQFWLIG GTSAHLAAVL QGLLKVIAGI EISFTLTSKS
     AGDDVDDEFA DLYIVKWTSL MIPPITIMMV NLIAIAVGVS RTIYSVIPQW SRLIGGVFFS
     FWVLTHLYPF AKGLMGRRGR TPTIVFVWSG LIAITISLLW VAINPPAGSN QIGGSFQFP
//