LAF3_ARATH
ID LAF3_ARATH Reviewed; 583 AA.
AC A0A1I9LN01; F4IY42; Q7Y048; Q7Y049; Q93ZE1; Q9LY60;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Protein LONG AFTER FAR-RED 3 {ECO:0000303|PubMed:14645728};
DE EC=3.5.-.- {ECO:0000305};
GN Name=LAF3 {ECO:0000303|PubMed:14645728};
GN OrderedLocusNames=At3g55850 {ECO:0000312|Araport:AT3G55850};
GN ORFNames=F27K19.30 {ECO:0000312|EMBL:CAB87839.1};
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] (ISOFORMS 1 AND 2), FUNCTION, DISRUPTION
RP PHENOTYPE, INDUCTION BY GERMINATION AND FAR-RED LIGHT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14645728; DOI=10.1104/pp.103.028480;
RA Hare P.D., Moller S.G., Huang L.-F., Chua N.-H.;
RT "LAF3, a novel factor required for normal phytochrome A signaling.";
RL Plant Physiol. 133:1592-1604(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] (ISOFORM 3).
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: Required for phyA-controlled responses to continuous far-red
CC light (FRc) conditions, including the inhibition of hypocotyl
CC elongation and the regulation of XTH15/XTR7 expression.
CC {ECO:0000269|PubMed:14645728}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:14645728}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=LAF3(ISF1) {ECO:0000303|PubMed:14645728};
CC IsoId=A0A1I9LN01-1; Sequence=Displayed;
CC Name=2; Synonyms=LAF3(ISF2) {ECO:0000303|PubMed:14645728};
CC IsoId=A0A1I9LN01-2; Sequence=VSP_059756;
CC Name=3;
CC IsoId=A0A1I9LN01-3; Sequence=VSP_059755;
CC -!- TISSUE SPECIFICITY: Expressed at low level in seedlings, roots, leaves,
CC stems, flowers, and siliques. {ECO:0000269|PubMed:14645728}.
CC -!- INDUCTION: Induced during germination. Accumulates slightly in
CC seedlings upon de-etiolation; triggered slowly after irradiation with
CC far-red light (FRc). {ECO:0000269|PubMed:14645728}.
CC -!- DISRUPTION PHENOTYPE: Reduced inhibition of hypocotyl elongation in
CC continuous far-red light (FRc), associated with a strongly attenuated
CC disappearance of XTH15/XTR7 transcripts. {ECO:0000269|PubMed:14645728}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY295343; AAP55749.1; -; mRNA.
DR EMBL; AY295344; AAP55750.1; -; mRNA.
DR EMBL; AL163832; CAB87839.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79448.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63958.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63959.1; -; Genomic_DNA.
DR EMBL; AY057597; AAL14392.1; -; mRNA.
DR EMBL; BT000585; AAN18154.1; -; mRNA.
DR PIR; T49197; T49197.
DR RefSeq; NP_001326017.1; NM_001339751.1. [A0A1I9LN01-2]
DR RefSeq; NP_567027.2; NM_115443.4. [A0A1I9LN01-2]
DR RefSeq; NP_974445.2; NM_202716.3. [A0A1I9LN01-1]
DR AlphaFoldDB; A0A1I9LN01; -.
DR SMR; A0A1I9LN01; -.
DR STRING; 3702.AT3G55850.2; -.
DR ProteomicsDB; 250750; -. [A0A1I9LN01-1]
DR EnsemblPlants; AT3G55850.1; AT3G55850.1; AT3G55850. [A0A1I9LN01-2]
DR EnsemblPlants; AT3G55850.5; AT3G55850.5; AT3G55850. [A0A1I9LN01-1]
DR EnsemblPlants; AT3G55850.6; AT3G55850.6; AT3G55850. [A0A1I9LN01-2]
DR GeneID; 824751; -.
DR Gramene; AT3G55850.1; AT3G55850.1; AT3G55850. [A0A1I9LN01-2]
DR Gramene; AT3G55850.5; AT3G55850.5; AT3G55850. [A0A1I9LN01-1]
DR Gramene; AT3G55850.6; AT3G55850.6; AT3G55850. [A0A1I9LN01-2]
DR KEGG; ath:AT3G55850; -.
DR Araport; AT3G55850; -.
DR eggNOG; ENOG502QSHE; Eukaryota.
DR HOGENOM; CLU_009942_6_0_1; -.
DR OMA; VAWVGSE; -.
DR OrthoDB; 776380at2759; -.
DR PRO; PR:A0A1I9LN01; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A0A1I9LN01; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0009704; P:de-etiolation; IEP:UniProtKB.
DR GO; GO:0010218; P:response to far red light; IMP:UniProtKB.
DR GO; GO:0009845; P:seed germination; IEP:UniProtKB.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..583
FT /note="Protein LONG AFTER FAR-RED 3"
FT /id="PRO_0000445026"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 3)"
FT /id="VSP_059755"
FT VAR_SEQ 1..13
FT /note="MTGWYEFPVMIGF -> MNLFVI (in isoform 2)"
FT /id="VSP_059756"
FT CONFLICT 41
FT /note="L -> P (in Ref. 1; AAP55749/AAP55750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 63785 MW; DE5BEA965BC57F2C CRC64;
MTGWYEFPVM IGFVSAAVFL LISVAYLPLL NDLYWSTLKS LTPPAGIVAD LLVTNGTIFT
SDSSLPFADS MAIRNGRILK VGSFATLKGF IGDGTMEVNL EGKIVVPGLI DSHVHLISGG
LQMAQVGLRG VSQKDEFCKM VKDAVQNAKE GSWILGGGWN NDFWGGELPS ASWIDEISPR
NPVWLIRMDG HMALANSLAL KIAGVISLTE DPVGGTIMRM PSGEPTGLLI DAAMELVTPW
VKEISVDERR EALFRASKYA LTRGVTTVID LGRYFPGTTD ELSWKDFQDV YLYADSSKKM
MIRTCLFFPI TTWSRLLDLK LQKGSVLSEW LYLGGVKAFI DGSLGSNSAL FYEEYIDTPN
NYGLEVMDPE KLSNFTMAAD KSGLQVAIHA IGDKANDMIL DMYESVAAAN GDRDRRFRIE
HAQHLAPGSA NRFGQLHIVA SVQPDHLLDD ADSVAKKLGS ERAVKESYLF QSLLNGNALL
ALGSDWPVAD INPLHSIRTA VKRIPPKWDH AWIPSERISF TDALIAQTIS AARAAFLDHH
LGSLSPGKLA DFVILSTNSW DEFSKDVSAS VLATYVGGKQ LYP
