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Database: UniProt
Entry: R0ILR9_9BRAS
LinkDB: R0ILR9_9BRAS
Original site: R0ILR9_9BRAS 
ID   R0ILR9_9BRAS            Unreviewed;      1186 AA.
AC   R0ILR9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Cellulose synthase-like protein D5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CARUB_v10008123mg {ECO:0000313|EMBL:EOA39505.1};
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:EOA39505.1, 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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KB870805; EOA39505.1; -; Genomic_DNA.
DR   RefSeq; XP_006306607.1; XM_006306545.1.
DR   AlphaFoldDB; R0ILR9; -.
DR   STRING; 81985.R0ILR9; -.
DR   GeneID; 17897843; -.
DR   KEGG; crb:17897843; -.
DR   eggNOG; ENOG502QQG2; Eukaryota.
DR   OrthoDB; 1210919at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
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:SF183; CELLULOSE SYNTHASE-LIKE PROTEIN D5; 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:UP000029121};
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        968..990
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        996..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1093..1112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1118..1139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1151..1171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1186 AA;  132918 MW;  14FA5005B17A4054 CRC64;
     MVKTAASQSP SPVTITVTPC KGSGDRSLGL TSPIPRASVI NNQNSPLSSR ATRRTSVSGG
     DRRSSGGEGR YCSMSVEDLT AETTTNSDCV LSYTVHIPPT PDHQTVFASQ ESGMGEEDEL
     LKGNSNNRGF LSGTIFTGGF KSVTRGHVID CSMDRADPEK KSGQICWLKG CDEKVVHGRC
     ECGFRICRDC YFDCITSGGG NCPGCKEPYR DINDDVETEE EDEEDEAKPL PQMNESKLDK
     RLSVVKSFKA QNQAGDFDHT RWLFETKGTY GYGNAVWPKD GYGIGSGGNN GNGYETPPEF
     GERSKRPLTR KVSVSAAIIS PYRLLIALRL VALCLFLTWR IRHPNREAMW LWGMSTTCEL
     WFALSWLLDQ LPKLCPVNRL TDLGVLKERF ESPNLRNPKG RSDLPGIDVF VSTADPEKEP
     PLVTANTILS ILAVDYPVEK LACYLSDDGG ALLTFEALAQ TASFASTWVP FCRKHSIEPR
     NPEAYFGQKR NFLKNKVRLD FVRERRRVKR EYDEFKVRIN SLPEAIRRRS DAYNVHEELR
     AKKKQMEMMM VSNPEEAVKV PKATWMSDGS HWPGTWSSGE SDNSRGDHAG IIQAMLAPPN
     AEPVYGAEAD AENLIDTTDV DIRLPMLVYV SREKRPGYDH NKKAGAMNAL VRTSAIMSNG
     PFILNLDCDH YVYNSMALRE GMCFMLDRGG DRISYVQFPQ RFEGIDPNDR YANHNTVFFD
     VSMRALDGLQ GPMYVGTGCI FRRTALYGFS PPRATEHHGW LGRKKVKISL RKPKAVMKKD
     DEISLPMNGE FNEEENDDGD IESLLLPKRF GNSNSFVASI PVAEYQGRLL QDLQGKGKNS
     RPAGSLAVPR EPLDAATVAE AISVISCFYE DKTEWGKRVG WIYGSVTEDV VTGYRMHNRG
     WRSIYCVTKR DAFRGTAPIN LTDRLHQVLR WATGSVEIFF SRNNAIFATR RMKFLQRVAY
     FNVGMYPFTS LFLIIYCILP AVSLFSGQFI VQSLDITFLI FLLSITLTLC MLSLLEIKWS
     GITLHEWWRN EQFWVIGGTS AHPAAVLQGL LKVIAGVDIS FTLTSKSSTP EDGDDEFADL
     YVVKWSFLMV PPLTIMMVNM IAIAVGLART LYSPFPQWSK LVGGVFFSFW VLCHLYPFAK
     GLMGRRGKVP TIVFVWSGLL SIIVSLLWVY INPPSGKQDY MQFQFP
//
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