FIS1B_ARATH
ID FIS1B_ARATH Reviewed; 167 AA.
AC Q94CK3;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Mitochondrial fission 1 protein B;
DE AltName: Full=FIS1 homolog B;
DE Short=AtFIS1b;
GN Name=FIS1B; OrderedLocusNames=At5g12390; ORFNames=T2L20;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
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 [7]
RP FUNCTION, INTERACTION WITH PEX11A; PEX11B; PEX11C; PEX11D AND PEX11E, AND
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [9]
RP 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. In association with PEX11C, PEX11D, PEX11E and DRP3A, is
CC involved in cell cycle-associated constitutive self-replication of
CC preexisting peroxisomes. {ECO:0000269|PubMed:18539750,
CC ECO:0000269|PubMed:18785999, ECO:0000269|PubMed:19825601}.
CC -!- SUBUNIT: Interacts with PEX11A, PEX11B, PEX11C, PEX11D and PEX11E.
CC {ECO:0000269|PubMed:18539750}.
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 -!- MISCELLANEOUS: Plants silencing FIS1B show reduced growth, increase in
CC the size of mitochondria and decrease in the number of mitochondria per
CC cell (PubMed:18785999). Overexpression of FIS1B increases the fission
CC of peroxisomes and mitochondria (PubMed:19825601).
CC {ECO:0000305|PubMed:18785999, ECO:0000305|PubMed:19825601}.
CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}.
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DR EMBL; AB195718; BAE47516.1; -; mRNA.
DR EMBL; AL592312; CAC42900.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91804.1; -; Genomic_DNA.
DR EMBL; AK118241; BAC42860.1; -; mRNA.
DR EMBL; BT005496; AAO63916.1; -; mRNA.
DR RefSeq; NP_568272.1; NM_121277.4.
DR AlphaFoldDB; Q94CK3; -.
DR SMR; Q94CK3; -.
DR BioGRID; 16392; 5.
DR IntAct; Q94CK3; 4.
DR STRING; 3702.AT5G12390.1; -.
DR PaxDb; Q94CK3; -.
DR PRIDE; Q94CK3; -.
DR ProteomicsDB; 230580; -.
DR EnsemblPlants; AT5G12390.1; AT5G12390.1; AT5G12390.
DR GeneID; 831114; -.
DR Gramene; AT5G12390.1; AT5G12390.1; AT5G12390.
DR KEGG; ath:AT5G12390; -.
DR Araport; AT5G12390; -.
DR TAIR; locus:505006607; AT5G12390.
DR eggNOG; KOG3364; Eukaryota.
DR HOGENOM; CLU_104368_0_0_1; -.
DR InParanoid; Q94CK3; -.
DR OMA; ADEFPLC; -.
DR OrthoDB; 1595957at2759; -.
DR PhylomeDB; Q94CK3; -.
DR PRO; PR:Q94CK3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94CK3; baseline and differential.
DR Genevisible; Q94CK3; AT.
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:TAIR.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
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 InterPro; IPR019734; TPR_repeat.
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.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 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..167
FT /note="Mitochondrial fission 1 protein B"
FT /id="PRO_0000422805"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 92..125
FT /note="TPR"
SQ SEQUENCE 167 AA; 17920 MW; 913A01523294BE84 CRC64;
MDAAIGKVFD SVSDFFSGAA SASADEFPLC DSDIISGCEK ELAEAQDEGR KKECIMRLSW
ALVHSKMPSD IQRGIAMLEA LVVNDTSAMK LREKLYLLAL GYYRSGDFSR SRDCIERCLE
VEPESGQAQA LKKAIEDRIV KDGVIGVGIA VTAVGVVAGI AAAILRS
