FAO4B_ARATH
ID FAO4B_ARATH Reviewed; 748 AA.
AC Q94BP3; Q9M0H4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Long-chain-alcohol oxidase FAO4B;
DE EC=1.1.3.20;
DE AltName: Full=Long-chain fatty alcohol oxidase 4B;
GN Name=FAO4B; OrderedLocusNames=At4g28570; ORFNames=T5F17.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15358540; DOI=10.1016/j.febslet.2004.07.086;
RA Cheng Q., Liu H.T., Bombelli P., Smith A., Slabas A.R.;
RT "Functional identification of AtFao3, a membrane bound long chain alcohol
RT oxidase in Arabidopsis thaliana.";
RL FEBS Lett. 574:62-68(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC oxidation pathway of lipid degradation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain primary fatty alcohol + O2 = a long-chain fatty
CC aldehyde + H2O2; Xref=Rhea:RHEA:22756, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17176, ChEBI:CHEBI:77396; EC=1.1.3.20;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AJ316231; CAC87644.1; -; mRNA.
DR EMBL; AL161573; CAB81445.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85508.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67935.1; -; Genomic_DNA.
DR EMBL; AY039977; AAK64154.1; -; mRNA.
DR EMBL; BT001942; AAN71941.1; -; mRNA.
DR PIR; T10651; T10651.
DR RefSeq; NP_001320082.1; NM_001341924.1.
DR RefSeq; NP_194586.1; NM_118999.5.
DR AlphaFoldDB; Q94BP3; -.
DR SMR; Q94BP3; -.
DR STRING; 3702.AT4G28570.1; -.
DR PaxDb; Q94BP3; -.
DR PRIDE; Q94BP3; -.
DR ProteomicsDB; 230851; -.
DR EnsemblPlants; AT4G28570.1; AT4G28570.1; AT4G28570.
DR EnsemblPlants; AT4G28570.2; AT4G28570.2; AT4G28570.
DR GeneID; 828975; -.
DR Gramene; AT4G28570.1; AT4G28570.1; AT4G28570.
DR Gramene; AT4G28570.2; AT4G28570.2; AT4G28570.
DR KEGG; ath:AT4G28570; -.
DR Araport; AT4G28570; -.
DR TAIR; locus:2139895; AT4G28570.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_1_1_1; -.
DR InParanoid; Q94BP3; -.
DR OMA; HTVECDA; -.
DR OrthoDB; 626762at2759; -.
DR PhylomeDB; Q94BP3; -.
DR PRO; PR:Q94BP3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94BP3; baseline and differential.
DR Genevisible; Q94BP3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR012400; Long_Oxdase.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF028937; Lg_Ch_AO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..748
FT /note="Long-chain-alcohol oxidase FAO4B"
FT /id="PRO_0000395506"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 679
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 238..253
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 118
FT /note="K -> R (in Ref. 4; AAK64154)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 81959 MW; 13CD183F5940DAC3 CRC64;
MEDVRRRNRG HPLLRSKKRG EGYNHGFSPS QIQSLAVICQ TFLPPETTSE QQAVNSFHVA
SSTQPPFTDE VAEMIVKNGR SEAVKVLRII LMILSFRFGT LLLCGSLCLD KSWPFVLKFS
QLPLDKREAI LRNWSRQSGF LLPFRITFFL AKFYTLFYFF SQTDENLKNP ALEAIGYCID
GTERSSNKKS EADEKRRPLE KGIIETMHES DVTITQSLTE KGVHVARDDG DNVYRIRCDA
VVVGSGSGGG VAAANLAKAG LKVLVLEKGN YFTAHDYSGL EVPSMLELYE KGGLLTTVDG
KFMLLAGSAV GGGTAVNWSA SIRTPDHVLQ EWSEGSKIKF FGSQEYQSAM DEVTIRIGVT
ERCVKHGFQN QVLRKGCERL GLQVESVPRN SPEDHYCGLC GYGCRAGAKN GTDQTWLVDA
VENGAVILTG IKAERFVLVD NTSSSNERKK RCVGVFASSV GGKIGKKFII EARVTVSSAG
SLLTPPLMLS SGLKNPNIGR NLKLHPVLMT WGYFPEKDSE FSGKMYEGGI ITSVHHMNDT
ESGCKAILEN PLIGPASYAG LSPWVSGPDL KERMIKYGRT AHLFALVRDL GSGEVMMENE
VTYRTTKKDR ENLRAGLRQA LRVSVAAGAV EVGTYRSDGQ KMKCEAITKE AMEEFLDEVD
AVGGVGTKGE YWTTYFSAHQ MGSCRMGVTA EEGALDENGE SWEAEGLFVC DGSILPSAVG
VNPMITIQST AYCISSKIVD SLQNKTKV
