RBL6_ARATH
ID RBL6_ARATH Reviewed; 307 AA.
AC Q8VZ48; Q9LN72;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=RHOMBOID-like protein 6, mitochondrial {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
DE Short=AtRBL6 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
DE EC=3.4.21.- {ECO:0000305};
DE Flags: Precursor;
GN Name=RBL6 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
GN OrderedLocusNames=At1g12750 {ECO:0000312|Araport:AT1G12750};
GN ORFNames=T12C24.28 {ECO:0000312|EMBL:AAF88090.1};
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|EMBL:AAL38727.1};
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 GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16223493; DOI=10.1016/j.febslet.2005.09.049;
RA Kanaoka M.M., Urban S., Freeman M., Okada K.;
RT "An Arabidopsis Rhomboid homolog is an intramembrane protease in plants.";
RL FEBS Lett. 579:5723-5728(2005).
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 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. Might be involved in response to abiotic
CC stimuli. {ECO:0000303|PubMed:22007993}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Might be neither mitochondrial nor
CC chloroplastic. {ECO:0000305|PubMed:18543065}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF88090.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC025417; AAF88090.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE28921.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28923.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60285.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60286.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60288.1; -; Genomic_DNA.
DR EMBL; AY065251; AAL38727.1; -; mRNA.
DR EMBL; AY091318; AAM14257.1; -; mRNA.
DR PIR; G86260; G86260.
DR RefSeq; NP_001184975.1; NM_001198046.2.
DR RefSeq; NP_001322583.1; NM_001332051.1.
DR RefSeq; NP_001322584.1; NM_001332050.1.
DR RefSeq; NP_001322586.1; NM_001332048.1.
DR RefSeq; NP_172735.1; NM_101145.3.
DR AlphaFoldDB; Q8VZ48; -.
DR IntAct; Q8VZ48; 4.
DR STRING; 3702.AT1G12750.3; -.
DR MEROPS; S54.A04; -.
DR SwissPalm; Q8VZ48; -.
DR PaxDb; Q8VZ48; -.
DR PRIDE; Q8VZ48; -.
DR ProteomicsDB; 225970; -.
DR EnsemblPlants; AT1G12750.1; AT1G12750.1; AT1G12750.
DR EnsemblPlants; AT1G12750.3; AT1G12750.3; AT1G12750.
DR EnsemblPlants; AT1G12750.4; AT1G12750.4; AT1G12750.
DR EnsemblPlants; AT1G12750.6; AT1G12750.6; AT1G12750.
DR EnsemblPlants; AT1G12750.7; AT1G12750.7; AT1G12750.
DR GeneID; 837831; -.
DR Gramene; AT1G12750.1; AT1G12750.1; AT1G12750.
DR Gramene; AT1G12750.3; AT1G12750.3; AT1G12750.
DR Gramene; AT1G12750.4; AT1G12750.4; AT1G12750.
DR Gramene; AT1G12750.6; AT1G12750.6; AT1G12750.
DR Gramene; AT1G12750.7; AT1G12750.7; AT1G12750.
DR KEGG; ath:AT1G12750; -.
DR Araport; AT1G12750; -.
DR TAIR; locus:2195067; AT1G12750.
DR eggNOG; KOG2289; Eukaryota.
DR HOGENOM; CLU_011531_0_0_1; -.
DR InParanoid; Q8VZ48; -.
DR OMA; NIGNTQW; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; Q8VZ48; -.
DR PRO; PR:Q8VZ48; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VZ48; baseline and differential.
DR Genevisible; Q8VZ48; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR002610; Peptidase_S54_rhomboid.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR PANTHER; PTHR22936; PTHR22936; 1.
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..62
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 63..307
FT /note="RHOMBOID-like protein 6, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433327"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54493"
SQ SEQUENCE 307 AA; 34289 MW; 6A6A8EEF7E9F1147 CRC64;
MRSRDMERGR KHRGDTQWTA WLTPTIVVAN VSIFIVVMYT NDCPKTTTGA NGDCVAKLLR
RFSFQPLREN PFLGPSSSTL EKLGALDWKK VVQGNEKWRL ITAMWLHAGI IHLVMNMFDV
IIFGIRLEQQ FGFIRIGLIY LISGFGGSIL SALFLQKSIS VGASGALLGL MGAMLSELLT
NWTIYKSKLC ALLSFLFIIA INLAIGLLPW VDNFAHIGGL LTGFCLGFIL LMQPQSGWEE
FRNSSQYGAR ARSKYNPCQY VLFFVAAVLV VAGLTVGLVM LFDGENGNKH CKWCHRLDCY
PTSKWSC
