FIS1A_ARATH
ID FIS1A_ARATH Reviewed; 170 AA.
AC Q9M1J1;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Mitochondrial fission 1 protein A;
DE AltName: Full=FIS1 homolog A;
DE Short=AtFIS1a;
DE AltName: Full=Protein BIGYIN 1;
GN Name=FIS1A; Synonyms=BGY1; OrderedLocusNames=At3g57090;
GN ORFNames=F24I3.1700;
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].
RC STRAIN=cv. Columbia;
RA Mori A., Fujimoto M., Tsutsumi N., Arimura S.;
RT "Arabidopsis AtFIS1a is involved in the mitochondrial fission.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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].
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16510519; DOI=10.1093/jxb/erj096;
RA Scott I., Tobin A.K., Logan D.C.;
RT "BIGYIN, an orthologue of human and yeast FIS1 genes functions in the
RT control of mitochondrial size and number in Arabidopsis thaliana.";
RL J. Exp. Bot. 57:1275-1280(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=19825601; DOI=10.1093/mp/ssn056;
RA Zhang X.C., Hu J.P.;
RT "FISSION1A and FISSION1B proteins mediate the fission of peroxisomes and
RT mitochondria in Arabidopsis.";
RL Mol. Plant 1:1036-1047(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18539750; DOI=10.1105/tpc.107.057679;
RA Lingard M.J., Gidda S.K., Bingham S., Rothstein S.J., Mullen R.T.,
RA Trelease R.N.;
RT "Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A
RT cooperate in cell cycle-associated replication of peroxisomes.";
RL Plant Cell 20:1567-1585(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18785999; DOI=10.1111/j.1365-313x.2008.03677.x;
RA Zhang X., Hu J.;
RT "Two small protein families, DYNAMIN-RELATED PROTEIN3 and FISSION1, are
RT required for peroxisome fission in Arabidopsis.";
RL Plant J. 57:146-159(2009).
RN [10]
RP INTERACTION WITH ARC5, AND SUBCELLULAR LOCATION.
RX PubMed=20179140; DOI=10.1105/tpc.109.071324;
RA Zhang X., Hu J.;
RT "The Arabidopsis chloroplast division protein DYNAMIN-RELATED PROTEIN5B
RT also mediates peroxisome division.";
RL Plant Cell 22:431-442(2010).
CC -!- FUNCTION: Component of the peroxisomal and mitochondrial division
CC machineries. Plays a role in promoting the fission of mitochondria and
CC peroxisomes. {ECO:0000269|PubMed:16510519, ECO:0000269|PubMed:18785999,
CC ECO:0000269|PubMed:19825601}.
CC -!- SUBUNIT: Interacts with ARC5. {ECO:0000269|PubMed:20179140}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC membrane protein. Peroxisome membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The C-terminus is necessary for mitochondrial or peroxisomal
CC targeting, while the N-terminus is necessary for mitochondrial or
CC peroxisomal fission. {ECO:0000269|PubMed:19825601}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant growth. Increase in the size of
CC mitochondria and decrease in the number of mitochondria per cell.
CC {ECO:0000269|PubMed:16510519, ECO:0000269|PubMed:18785999,
CC ECO:0000269|PubMed:19825601}.
CC -!- MISCELLANEOUS: Overexpression of FIS1A increases the fission of
CC peroxisomes and mitochondria. {ECO:0000305|PubMed:19825601}.
CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}.
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DR EMBL; AB195717; BAE47515.1; -; mRNA.
DR EMBL; AL138655; CAB72179.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79613.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65072.1; -; Genomic_DNA.
DR EMBL; AY050354; AAK91371.1; -; mRNA.
DR EMBL; AY097397; AAM19913.1; -; mRNA.
DR EMBL; AY087545; AAM65087.1; -; mRNA.
DR PIR; T47769; T47769.
DR RefSeq; NP_001327069.1; NM_001339841.1.
DR RefSeq; NP_567044.1; NM_115568.4.
DR AlphaFoldDB; Q9M1J1; -.
DR SMR; Q9M1J1; -.
DR BioGRID; 10192; 6.
DR IntAct; Q9M1J1; 7.
DR STRING; 3702.AT3G57090.1; -.
DR SwissPalm; Q9M1J1; -.
DR PaxDb; Q9M1J1; -.
DR PRIDE; Q9M1J1; -.
DR ProteomicsDB; 230099; -.
DR EnsemblPlants; AT3G57090.1; AT3G57090.1; AT3G57090.
DR EnsemblPlants; AT3G57090.2; AT3G57090.2; AT3G57090.
DR GeneID; 824876; -.
DR Gramene; AT3G57090.1; AT3G57090.1; AT3G57090.
DR Gramene; AT3G57090.2; AT3G57090.2; AT3G57090.
DR KEGG; ath:AT3G57090; -.
DR Araport; AT3G57090; -.
DR TAIR; locus:2080665; AT3G57090.
DR eggNOG; KOG3364; Eukaryota.
DR HOGENOM; CLU_104368_0_0_1; -.
DR InParanoid; Q9M1J1; -.
DR OMA; VTIQTKF; -.
DR OrthoDB; 1595957at2759; -.
DR PhylomeDB; Q9M1J1; -.
DR PRO; PR:Q9M1J1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1J1; baseline and differential.
DR Genevisible; Q9M1J1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:TAIR.
DR GO; GO:0016559; P:peroxisome fission; IMP:TAIR.
DR CDD; cd12212; Fis1; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR016543; Fis1.
DR InterPro; IPR033745; Fis1_cytosol.
DR InterPro; IPR028061; Fis1_TPR_C.
DR InterPro; IPR028058; Fis1_TPR_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13247; PTHR13247; 1.
DR Pfam; PF14853; Fis1_TPR_C; 1.
DR Pfam; PF14852; Fis1_TPR_N; 1.
DR PIRSF; PIRSF008835; TPR_repeat_11_Fis1; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Peroxisome;
KW Peroxisome biogenesis; Reference proteome; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..170
FT /note="Mitochondrial fission 1 protein A"
FT /id="PRO_0000422804"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 90..123
FT /note="TPR"
SQ SEQUENCE 170 AA; 18698 MW; 550FC38CAC4B5418 CRC64;
MDAKIGQFFD SVGTFFSGSD KIPWCDGDVI AGCEREVREA TDSGTEDLKK ECLMRLSWAL
VHSRQTEDVQ RGIAMLEASL ESSAPPLEDR EKLYLLAVGY YRSGNYSRSR QLVDRCIEMQ
ADWRQALVLK KTIEDKITKD GVIGIGITAT AFGAVGLIAG GIVAAMSRKK
