RBL15_ARATH
ID RBL15_ARATH Reviewed; 403 AA.
AC Q8LB17; C0Z2U1; Q8L7A1; Q9M2H0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Rhomboid-like protein 15 {ECO:0000303|PubMed:17181860};
DE Short=AtRBL15 {ECO:0000303|PubMed:17181860};
DE EC=3.4.21.- {ECO:0000305};
GN Name=RBL15 {ECO:0000303|PubMed:17181860};
GN Synonyms=RBL11 {ECO:0000303|PubMed:17938163};
GN OrderedLocusNames=At3g58460 {ECO:0000312|Araport:AT3G58460};
GN ORFNames=F14P22.50 {ECO:0000312|EMBL:CAB68184.1};
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 [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 [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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH57020.1};
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 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 [7]
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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).
RN [11]
RP STRUCTURE BY NMR OF 342-401.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-014, a UBA domain of Arabidopsis thaliana
RT cDNA.";
RL Submitted (JAN-2004) to the PDB data bank.
CC -!- FUNCTION: Probable rhomboid-type serine protease that catalyzes
CC intramembrane proteolysis. May function in senescence.
CC {ECO:0000303|PubMed:22007993}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LB17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LB17-2; Sequence=VSP_057725, VSP_057726;
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB68184.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL137082; CAB68184.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79784.1; -; Genomic_DNA.
DR EMBL; AY136386; AAM97052.1; -; mRNA.
DR EMBL; BT000186; AAN15505.1; -; mRNA.
DR EMBL; AK318905; BAH57020.1; -; mRNA.
DR EMBL; AY087480; AAM65024.1; -; mRNA.
DR PIR; T45666; T45666.
DR RefSeq; NP_567064.1; NM_115708.4. [Q8LB17-1]
DR PDB; 1VG5; NMR; -; A=342-401.
DR PDBsum; 1VG5; -.
DR AlphaFoldDB; Q8LB17; -.
DR SMR; Q8LB17; -.
DR BioGRID; 10330; 8.
DR IntAct; Q8LB17; 8.
DR STRING; 3702.AT3G58460.2; -.
DR iPTMnet; Q8LB17; -.
DR PaxDb; Q8LB17; -.
DR PRIDE; Q8LB17; -.
DR ProteomicsDB; 236512; -. [Q8LB17-1]
DR EnsemblPlants; AT3G58460.1; AT3G58460.1; AT3G58460. [Q8LB17-1]
DR GeneID; 825015; -.
DR Gramene; AT3G58460.1; AT3G58460.1; AT3G58460. [Q8LB17-1]
DR KEGG; ath:AT3G58460; -.
DR Araport; AT3G58460; -.
DR eggNOG; KOG2632; Eukaryota.
DR HOGENOM; CLU_036445_1_0_1; -.
DR InParanoid; Q8LB17; -.
DR OMA; QWWENIP; -.
DR PhylomeDB; Q8LB17; -.
DR EvolutionaryTrace; Q8LB17; -.
DR PRO; PR:Q8LB17; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LB17; baseline and differential.
DR Genevisible; Q8LB17; AT.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Membrane; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..403
FT /note="Rhomboid-like protein 15"
FT /id="PRO_0000220607"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 361..401
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 282..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT VAR_SEQ 358..362
FT /note="GRVAA -> VTFLL (in isoform 2)"
FT /id="VSP_057725"
FT VAR_SEQ 363..403
FT /note="Missing (in isoform 2)"
FT /id="VSP_057726"
FT CONFLICT 237
FT /note="R -> Q (in Ref. 3; AAM65024)"
FT /evidence="ECO:0000305"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1VG5"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:1VG5"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1VG5"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:1VG5"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:1VG5"
SQ SEQUENCE 403 AA; 44145 MW; FF6CD14E5582CB16 CRC64;
MRPNIVTEAG VQTRVGQWWN AIPFLTSSVV VVCGVIYLIC LLTGYDTFYE VCFLPSAIIS
RFQVYRFYTA IIFHGSLLHV LFNMMALVPM GSELERIMGS VRLLYLTVLL ATTNAVLHLL
IASLAGYNPF YQYDHLMNEC AIGFSGILFS MIVIETSLSG VTSRSVFGLF NVPAKLYPWI
LLIVFQLLMT NVSLLGHLCG ILSGFSYSYG LFNFLMPGSS FFTTIESASW MSSFIRRPKF
IMCTGGNPSS YIPTYSAQNT TSSGFSTGNA WRSLSSWLPQ REASNQSSED SRFPGRGRTL
STARDPTAPA GETDPNLHAR LLEDSSSPDR LSDATVNTVA DSRQAPIANA AVLPQSQGRV
AASEEQIQKL VAMGFDRTQV EVALAAADDD LTVAVEILMS QQA
