RBL11_ARATH
ID RBL11_ARATH Reviewed; 280 AA.
AC Q84MB5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Rhomboid-like protein 11, chloroplastic {ECO:0000303|PubMed:17181860};
DE Short=AtRBL11 {ECO:0000303|PubMed:17181860};
DE EC=3.4.21.- {ECO:0000305};
DE Flags: Precursor;
GN Name=RBL11 {ECO:0000303|PubMed:17181860};
GN Synonyms=RBL9 {ECO:0000303|PubMed:17938163};
GN OrderedLocusNames=At5g25752 {ECO:0000312|Araport:AT5G25752};
GN ORFNames=T5I5 {ECO:0000305};
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 {ECO:0000312|EMBL:AAP21234.1};
RN [1]
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16895613; DOI=10.1186/1471-2164-7-200;
RA Tripathi L.P., Sowdhamini R.;
RT "Cross genome comparisons of serine proteases in Arabidopsis and rice.";
RL BMC Genomics 7:200-200(2006).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17181860; DOI=10.1186/1471-2229-6-30;
RA Garcia-Lorenzo M., Sjodin A., Jansson S., Funk C.;
RT "Protease gene families in Populus and Arabidopsis.";
RL BMC Plant Biol. 6:30-30(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17938163; DOI=10.1101/gr.6425307;
RA Lemberg M.K., Freeman M.;
RT "Functional and evolutionary implications of enhanced genomic analysis of
RT rhomboid intramembrane proteases.";
RL Genome Res. 17:1634-1646(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18543065; DOI=10.1007/s11103-008-9359-8;
RA Kmiec-Wisniewska B., Krumpe K., Urantowka A., Sakamoto W., Pratje E.,
RA Janska H.;
RT "Plant mitochondrial rhomboid, AtRBL12, has different substrate specificity
RT from its yeast counterpart.";
RL Plant Mol. Biol. 68:159-171(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22738221; DOI=10.1111/j.1365-313x.2012.05090.x;
RA Knopf R.R., Feder A., Mayer K., Lin A., Rozenberg M., Schaller A., Adam Z.;
RT "Rhomboid proteins in the chloroplast envelope affect the level of allene
RT oxide synthase in Arabidopsis thaliana.";
RL Plant J. 72:559-571(2012).
RN [10]
RP REVIEW.
RX PubMed=22007993; DOI=10.1111/j.1399-3054.2011.01532.x;
RA Knopf R.R., Adam Z.;
RT "Rhomboid proteases in plants - still in square one?";
RL Physiol. Plantarum 145:41-51(2012).
CC -!- FUNCTION: Rhomboid-type serine protease that catalyzes intramembrane
CC proteolysis. May be involved in TIC22 processing during its import.
CC {ECO:0000269|PubMed:22738221}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000269|PubMed:17938163}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:18543065, ECO:0000269|PubMed:22738221}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Rbl10 and rbl11 double
CC mutants have no visible phenotype. {ECO:0000269|PubMed:22738221}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- CAUTION: Both termini are shown to be facing the stroma and hence a
CC sixth transmembrane domain should be present.
CC {ECO:0000269|PubMed:22738221}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT006426; AAP21234.1; -; mRNA.
DR EMBL; AK228048; BAF00010.1; -; mRNA.
DR AlphaFoldDB; Q84MB5; -.
DR IntAct; Q84MB5; 116.
DR STRING; 3702.AT5G25752.1; -.
DR MEROPS; S54.025; -.
DR PaxDb; Q84MB5; -.
DR PeptideAtlas; Q84MB5; -.
DR PRIDE; Q84MB5; -.
DR Araport; AT5G25752; -.
DR TAIR; locus:504956416; AT5G25752.
DR eggNOG; ENOG502QTDP; Eukaryota.
DR HOGENOM; CLU_055068_0_1_1; -.
DR InParanoid; Q84MB5; -.
DR PhylomeDB; Q84MB5; -.
DR PRO; PR:Q84MB5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84MB5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0080140; P:regulation of jasmonic acid metabolic process; IMP:TAIR.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Membrane; Plastid; Plastid inner membrane;
KW Protease; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..280
FT /note="Rhomboid-like protein 11, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433332"
FT TOPO_DOM 58..82
FT /note="Stromal"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..117
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..154
FT /note="Stromal"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..178
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..243
FT /note="Stromal"
FT /evidence="ECO:0000305"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..280
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305"
FT ACT_SITE 186
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT ACT_SITE 250
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54493"
SQ SEQUENCE 280 AA; 31593 MW; D599E046F9C65C4B CRC64;
MSQLLHLHRL SLPQSSLRFR FPPLHRRRAA SSPTNSTQPP LQFRPLTVSR SQITCRFSQS
DITPQFELDK AKDNRKPQKR ANGIFWIILI NLGIYLADHF FQVRGIKSLY LYHNFPAWYQ
FVTATFCHAN WNHLSSNLFF LYIFGKLVEE EEGNFGLWLS YLFTGVGANL VSWLVLPRNA
VSVGASGAVF GLFAISVLVK MSWDWRKILE VLILGQFVIE RVMEAAQASA GLSGTIYGGY
SLQTVNHIAH LSGALVGVVL VWLLSKFPSA SMDQDVKKSS
