RBL12_ARATH
ID RBL12_ARATH Reviewed; 336 AA.
AC Q9FZ81;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=RHOMBOID-like protein 12, mitochondrial {ECO:0000303|PubMed:17181860};
DE Short=AtRBL12 {ECO:0000303|PubMed:17181860};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Presenilins-associated rhomboid-like protein {ECO:0000303|PubMed:17938163};
DE Flags: Precursor;
GN Name=RBL12 {ECO:0000303|PubMed:17181860};
GN Synonyms=PARL {ECO:0000303|PubMed:17938163};
GN OrderedLocusNames=At1g18600 {ECO:0000312|Araport:AT1G18600};
GN ORFNames=F25I16.6 {ECO:0000312|EMBL:AAF98414.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [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].
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 [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, AND FUNCTION.
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 SUBCELLULAR LOCATION.
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: Probable rhomboid-type serine protease that catalyzes
CC intramembrane proteolysis. Unable to cleave either of the yeast Pcp1
CC substrates in yeast cells. {ECO:0000269|PubMed:18543065}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:18543065, ECO:0000269|PubMed:22738221}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: The functional differences between RBL12 and the yeast
CC Pcp1 appear to be at least caused by differences in their transmembrane
CC domains. {ECO:0000305|PubMed:18543065}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; AC026238; AAF98414.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29733.1; -; Genomic_DNA.
DR EMBL; AY081685; AAM10247.1; -; mRNA.
DR EMBL; AY086276; AAM64348.1; -; mRNA.
DR EMBL; AF370504; AAK43881.1; -; mRNA.
DR PIR; F86319; F86319.
DR RefSeq; NP_564058.1; NM_101718.5.
DR AlphaFoldDB; Q9FZ81; -.
DR SMR; Q9FZ81; -.
DR STRING; 3702.AT1G18600.1; -.
DR MEROPS; S54.A07; -.
DR PaxDb; Q9FZ81; -.
DR PRIDE; Q9FZ81; -.
DR ProteomicsDB; 236472; -.
DR EnsemblPlants; AT1G18600.1; AT1G18600.1; AT1G18600.
DR GeneID; 838441; -.
DR Gramene; AT1G18600.1; AT1G18600.1; AT1G18600.
DR KEGG; ath:AT1G18600; -.
DR Araport; AT1G18600; -.
DR TAIR; locus:2027448; AT1G18600.
DR eggNOG; KOG2980; Eukaryota.
DR HOGENOM; CLU_048192_0_0_1; -.
DR InParanoid; Q9FZ81; -.
DR OMA; HFRTHYL; -.
DR OrthoDB; 1554324at2759; -.
DR PhylomeDB; Q9FZ81; -.
DR PRO; PR:Q9FZ81; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ81; baseline and differential.
DR Genevisible; Q9FZ81; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Hydrolase; Membrane; Mitochondrion; Protease; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..85
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 86..336
FT /note="RHOMBOID-like protein 12, mitochondrial"
FT /id="PRO_0000433333"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54493"
SQ SEQUENCE 336 AA; 37441 MW; 6F5C4E231BDBDA99 CRC64;
MKAIFNRRVV VDSSSRLTKL LANPTTHSHL NRQTFTSLYK PNQSRHFRTH YLPSSPSSPP
VSRFDPSQLW RSEKIRGFFA SALGNKAVKL GNLVESRVGF IGSQFPKKGF EFQRFSGFQR
RGWKHWLQGL SDRDVVLGLV IANAGVFVMW RVFNQQFMMN NFMISLDNFK SGRLHTLITS
AFSHIDIGHI VSNMIGLYFF GTSIARNFGP QFLLKLYLAG ALGGSVFYLI HHAYMAATSP
KGQGAFVRDP SRTPGLGASG AVNAIMLLDI FLHPRATLYL EFFIPVPAML LGIFLIGKDI
LRITEGNSNI SGSAHLGGAA VAAIAWARIR KGRFRF
