GLO15_ORYSI
ID GLO15_ORYSI Reviewed; 621 AA.
AC B8BHF1; Q9XH51;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-5 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein ECERIFERUM 1 {ECO:0000303|Ref.1};
DE Short=Os-CER1 {ECO:0000303|Ref.1};
DE AltName: Full=Protein GLOSSY 1-5 {ECO:0000305};
GN Name=GL1-5 {ECO:0000305}; Synonyms=CER1 {ECO:0000303|Ref.1};
GN ORFNames=OsI_33995 {ECO:0000312|EMBL:EEC67150.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Anther;
RA Yau C.P., Zhuang C.X., Zee S.Y.;
RT "Isolation of a full length cDNA encoding a CER1 homolog in rice. (PGR99-
RT 104).";
RL Plant Physiol. 120:935-935(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Aldehyde decarbonylase involved in the conversion of
CC aldehydes to alkanes. Core component of a very-long-chain alkane
CC synthesis complex. {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-
CC chain alkane + formate + H2O + 2 NADP(+); Xref=Rhea:RHEA:21440,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17176, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:83563; EC=4.1.99.5;
CC Evidence={ECO:0000250|UniProtKB:F4HVY0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:F4HVY0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during the pollen mother cell meiotic
CC stage. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AF143746; AAD29719.1; -; mRNA.
DR EMBL; CM000135; EEC67150.1; -; Genomic_DNA.
DR AlphaFoldDB; B8BHF1; -.
DR STRING; 39946.B8BHF1; -.
DR EnsemblPlants; BGIOSGA031709-TA; BGIOSGA031709-PA; BGIOSGA031709.
DR Gramene; BGIOSGA031709-TA; BGIOSGA031709-PA; BGIOSGA031709.
DR HOGENOM; CLU_017842_1_0_1; -.
DR OMA; SYRWFMR; -.
DR Proteomes; UP000007015; Chromosome 10.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043668; C:exine; IEA:EnsemblPlants.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990465; F:aldehyde oxygenase (deformylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009924; F:octadecanal decarbonylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0048658; P:anther wall tapetum development; IEA:EnsemblPlants.
DR GO; GO:0042335; P:cuticle development; IEA:EnsemblPlants.
DR GO; GO:0010143; P:cutin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0010584; P:pollen exine formation; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR GO; GO:0010025; P:wax biosynthetic process; IEA:EnsemblPlants.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR021940; Uncharacterised_Wax2_C.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR Pfam; PF12076; Wax2_C; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..621
FT /note="Very-long-chain aldehyde decarbonylase GL1-5"
FT /id="PRO_0000445876"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 138..272
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT CONFLICT 358..370
FT /note="KKIRMQSWAIPRY -> RDQDAVMGHYQDT (in Ref. 1;
FT AAD29719)"
FT /evidence="ECO:0000305"
FT CONFLICT 555..589
FT /note="MAVPKTLQNVHSCENWLPRRVMSAWRIAGILHALE -> IGCTKNAAECAFM
FT RELAAKEGYGRMANGGNSSCVG (in Ref. 1; AAD29719)"
FT /evidence="ECO:0000305"
FT CONFLICT 602..619
FT /note="DMDKVWSAAIMHGFCPVA -> GMAKVWTDTIEHGLCPVD (in Ref. 1;
FT AAD29719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 71191 MW; 562E33F00EB661FC CRC64;
MATNPGLFTE WPWKKLGSFK YVLLAPWVAH GWYEVATKGR REVDLGYIAI LPSLLLRMLH
NQAWITISRL QNARGRRQIV RRGIEFDQVD RERNWDDQII LSGILLYLGA LYVPGGQHLP
LWRTDGAGLI ALLHAGPVEF LYYWFHRALH HHFLYTRYHS HHHSSIVTEP ITSVIHPFAE
LVAYELLFSI PLIACALTGT ASIIAFEMYL IYIDFMNNMG HCNFELVPSW LFTWFPPLKY
LMYTPSFHSL HHTQFRTNYS LFMPFYDYIY NTMDKSSDTL YENSLKNNDE EEAVDVVHLT
HLTTLHSIYH MRPGFAEFAS RPYVSRWYMR MMWPLSWLSM VLTWTYGSSF TVERNVMKKI
RMQSWAIPRY SFHYGLDWEK EAINDLIEKA VCEADKNGAK VVSLGLLNQA HTLNKSGEQY
LLKYPKLGAR IVDGTSLAAA VVVNSIPQGT DQVILAGNVS KVARAVAQAL CKKNIKVTMT
NKQDYHLLKP EIPETVADNL SFSKTGTAKV WLIGDGLDSA EQFRAQKGTL FIPYSQFPPK
MVRKDSCSYS TTPAMAVPKT LQNVHSCENW LPRRVMSAWR IAGILHALEG WNEHECGDKV
LDMDKVWSAA IMHGFCPVAQ G
