APO1_ARATH
ID APO1_ARATH Reviewed; 436 AA.
AC Q9XIR4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=APO protein 1, chloroplastic;
DE AltName: Full=Accumulation of photosystem I protein 1;
DE AltName: Full=Protein ACCUMULATION OF PHOTOSYSTEM ONE 1;
DE Flags: Precursor;
GN Name=APO1; OrderedLocusNames=At1g64810; ORFNames=F13O11.11;
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], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15494558; DOI=10.1105/tpc.104.024935;
RA Amann K., Lezhneva L., Wanner G., Herrmann R.G., Meurer J.;
RT "ACCUMULATION OF PHOTOSYSTEM ONE1, a member of a novel gene family, is
RT required for accumulation of [4Fe-4S] cluster containing chloroplast
RT complexes and antenna proteins.";
RL Plant Cell 16:3084-3097(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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).
CC -!- FUNCTION: Involved in the stable assembly of several 4Fe-4S cluster-
CC containing complexes of chloroplasts. May participate in 4Fe-4S
CC cofactor incorporation into psaA and/or psaB during translation.
CC {ECO:0000269|PubMed:15494558}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9XIR4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at low level. Expressed at higher level
CC in leaves. Expressed at lower level in roots, stems, siliques and
CC flowers. {ECO:0000269|PubMed:15494558}.
CC -!- INDUCTION: Up-regulated during photomorphogenesis.
CC {ECO:0000269|PubMed:15494558}.
CC -!- DOMAIN: The APO repeats may provide ligands for 4Fe-4S centers.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Plants fail to accumulate significant amounts of
CC the outer antenna subunits of PSI and PSII and to form grana stacks.
CC 2Fe-2S cluster-containing complexes appear to be unaffected.
CC {ECO:0000269|PubMed:15494558}.
CC -!- SIMILARITY: Belongs to the APO family. {ECO:0000255|PROSITE-
CC ProRule:PRU00832}.
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DR EMBL; AY466161; AAS45665.1; -; mRNA.
DR EMBL; AC006193; AAD38255.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34292.1; -; Genomic_DNA.
DR PIR; C96671; C96671.
DR RefSeq; NP_176661.1; NM_105155.4. [Q9XIR4-1]
DR AlphaFoldDB; Q9XIR4; -.
DR STRING; 3702.AT1G64810.2; -.
DR PaxDb; Q9XIR4; -.
DR ProteomicsDB; 240599; -. [Q9XIR4-1]
DR EnsemblPlants; AT1G64810.1; AT1G64810.1; AT1G64810. [Q9XIR4-1]
DR GeneID; 842789; -.
DR Gramene; AT1G64810.1; AT1G64810.1; AT1G64810. [Q9XIR4-1]
DR KEGG; ath:AT1G64810; -.
DR Araport; AT1G64810; -.
DR eggNOG; ENOG502QPNK; Eukaryota.
DR HOGENOM; CLU_033199_0_1_1; -.
DR InParanoid; Q9XIR4; -.
DR PhylomeDB; Q9XIR4; -.
DR PRO; PR:Q9XIR4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIR4; baseline and differential.
DR Genevisible; Q9XIR4; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR InterPro; IPR023342; APO_dom.
DR Pfam; PF05634; APO_RNA-bind; 2.
DR PROSITE; PS51499; APO; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Plastid; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..436
FT /note="APO protein 1, chloroplastic"
FT /id="PRO_0000001930"
FT DOMAIN 155..240
FT /note="APO 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00832"
FT DOMAIN 329..414
FT /note="APO 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00832"
SQ SEQUENCE 436 AA; 49627 MW; D6C78E8EAE6E19D6 CRC64;
MLLVSPACRG VYLQTIDPKP IDFSARASYA LCFQIPTSIP KRECLMRLGT VFCFNQKHRE
QTSFKKRYVS TQNVDLPPIL PKNKKKPYPI PFKQIQEEAR KDKKLAQMGI EKQLDPPKNG
LLVPNLVPVA DQVIDNWKLL IKGLAQLLHV VPVFACSECG AVHVANVGHN IRDCNGPTNS
QRRGSHSWVK GTINDVLIPV ESYHMYDPFG RRIKHETRFE YERIPALVEL CIQAGVEIPE
YPCRRRTQPI RMMGKRVIDR GGYHKEPEKP QTSSSLSSPL AELDTLGVFE RYPPPTPEDI
PKIAQETMDA YEKVRLGVTK LMRKFTVKAC GYCSEVHVGP WGHSVKLCGE FKHQWRDGKH
GWQDALVDEV FPPNYVWHVR DLKGNPLTGN LRRFYGKAPA LVEICMHSGA RVPQRYKAMM
RLDIIVPDSQ EADMVA