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RBL14_ARATH
ID   RBL14_ARATH             Reviewed;         334 AA.
AC   Q8RXW0; A8MS64; Q27GK6; Q682Z5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Rhomboid-like protein 14, mitochondrial {ECO:0000303|PubMed:17181860};
DE            Short=AtRBL14 {ECO:0000303|PubMed:17181860};
DE            EC=3.4.21.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=RBL14 {ECO:0000303|PubMed:17181860};
GN   Synonyms=RBL10 {ECO:0000303|PubMed:17938163};
GN   OrderedLocusNames=At3g17611 {ECO:0000312|Araport:AT3G17611};
GN   ORFNames=MKP6.17 {ECO:0000312|EMBL:BAB02051.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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] OF 196-334.
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 (SEP-2004) 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   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. May function in the heat-shock response
CC       pathway. {ECO:0000303|PubMed:22007993}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}. Note=Might be neither mitochondrial nor
CC       chloroplastic. {ECO:0000305|PubMed:18543065}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8RXW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8RXW0-2; Sequence=VSP_057724;
CC       Name=3;
CC         IsoId=Q8RXW0-3; Sequence=VSP_057723;
CC   -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB02051.1; Type=Erroneous gene model prediction; Note=The predicted gene At3g17610 has been split into 2 genes: At3g17609 and At3g17611.; Evidence={ECO:0000305};
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DR   EMBL; AB022219; BAB02051.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE75978.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75979.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75980.1; -; Genomic_DNA.
DR   EMBL; AY080647; AAL85014.1; -; mRNA.
DR   EMBL; AY117194; AAM51269.1; -; mRNA.
DR   EMBL; AK175222; BAD42985.1; -; mRNA.
DR   RefSeq; NP_001078170.1; NM_001084701.1. [Q8RXW0-3]
DR   RefSeq; NP_850606.1; NM_180275.3. [Q8RXW0-1]
DR   RefSeq; NP_974329.1; NM_202600.1. [Q8RXW0-2]
DR   AlphaFoldDB; Q8RXW0; -.
DR   BioGRID; 6361; 6.
DR   IntAct; Q8RXW0; 6.
DR   STRING; 3702.AT3G17611.1; -.
DR   PaxDb; Q8RXW0; -.
DR   PRIDE; Q8RXW0; -.
DR   ProteomicsDB; 236473; -. [Q8RXW0-1]
DR   EnsemblPlants; AT3G17611.1; AT3G17611.1; AT3G17611. [Q8RXW0-1]
DR   EnsemblPlants; AT3G17611.2; AT3G17611.2; AT3G17611. [Q8RXW0-2]
DR   EnsemblPlants; AT3G17611.3; AT3G17611.3; AT3G17611. [Q8RXW0-3]
DR   GeneID; 821028; -.
DR   Gramene; AT3G17611.1; AT3G17611.1; AT3G17611. [Q8RXW0-1]
DR   Gramene; AT3G17611.2; AT3G17611.2; AT3G17611. [Q8RXW0-2]
DR   Gramene; AT3G17611.3; AT3G17611.3; AT3G17611. [Q8RXW0-3]
DR   KEGG; ath:AT3G17611; -.
DR   Araport; AT3G17611; -.
DR   TAIR; locus:1005716534; AT3G17611.
DR   eggNOG; KOG2632; Eukaryota.
DR   HOGENOM; CLU_056643_0_0_1; -.
DR   InParanoid; Q8RXW0; -.
DR   OMA; HFFFNMS; -.
DR   PhylomeDB; Q8RXW0; -.
DR   PRO; PR:Q8RXW0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8RXW0; baseline and differential.
DR   Genevisible; Q8RXW0; 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:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   Pfam; PF01694; Rhomboid; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF144091; SSF144091; 1.
DR   SUPFAM; SSF90209; SSF90209; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW   Protease; Reference proteome; Transit peptide; Transmembrane;
KW   Transmembrane helix; Zinc; Zinc-finger.
FT   TRANSIT         1..87
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           88..334
FT                   /note="Rhomboid-like protein 14, mitochondrial"
FT                   /id="PRO_0000223928"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         273..302
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ACT_SITE        156
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P54493"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P54493"
FT   VAR_SEQ         1..161
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_057723"
FT   VAR_SEQ         1..95
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057724"
SQ   SEQUENCE   334 AA;  37150 MW;  8889A08D64484AD6 CRC64;
     MENFGEGRRS GGGMLPLLAL SAVAEYYRLP WKPPVTASLL AANTLVYLRP AFIDPVIPHI
     SEVWFNPHLI FKHKDLKRLF LSAFYHVNEP HLVYNMMSLL WKGIKLETSM GSSEFASMVF
     TLIGMSQGVT LLLAKSLLLL FDYDRAYYNE YAVGFSGVLF AMKVVLNSQA EDYSSVYGIL
     VPTKYAAWAE LILVQMFVPN ASFLGHLGGI LAGIIYLKLK GSYSGSDPVT MAVRGVSRLV
     TWPLRFLNGM VRSRRRRITG RGRVGRGQTG IAGPGIWRCQ SCTYDNSGWL SACEMCGSGR
     ARGNGWSLNQ GPALSSSNDL PLDELRRRRV ERFS
 
 
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