RBL10_ARATH
ID RBL10_ARATH Reviewed; 343 AA.
AC F4ICF4; F4ICF5; Q9FRH8;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=RHOMBOID-like protein 10, chloroplastic {ECO:0000303|PubMed:17181860};
DE Short=AtRBL10 {ECO:0000303|PubMed:17181860};
DE EC=3.4.21.- {ECO:0000305};
DE Flags: Precursor;
GN Name=RBL10 {ECO:0000303|PubMed:17181860};
GN Synonyms=RBL8 {ECO:0000303|PubMed:17938163};
GN OrderedLocusNames=At1g25290 {ECO:0000312|Araport:AT1G25290};
GN ORFNames=F4F7.32 {ECO:0000312|EMBL:AAG40087.1};
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 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 [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND INDUCTION BY COLD.
RX PubMed=22416142; DOI=10.1093/jxb/ers012;
RA Thompson E.P., Smith S.G., Glover B.J.;
RT "An Arabidopsis rhomboid protease has roles in the chloroplast and in
RT flower development.";
RL J. Exp. Bot. 63:3559-3570(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION 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 [8]
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 (PubMed:22416142, PubMed:22738221). Required for correct
CC root growth, floral development, fertility and photoprotection
CC (PubMed:22416142). May be involved in TIC22 processing during its
CC import and in AOS accumulation in the chloroplast membrane
CC (PubMed:22738221). {ECO:0000269|PubMed:22416142,
CC ECO:0000269|PubMed:22738221}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:22416142, ECO:0000269|PubMed:22738221}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes probably to the inner
CC membrane. {ECO:0000303|PubMed:22738221}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4ICF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4ICF4-2; Sequence=VSP_057732;
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, seedlings,
CC stems, flowers and immatures siliques. {ECO:0000269|PubMed:22416142}.
CC -!- INDUCTION: Up-regulated by cold during seedling germination.
CC {ECO:0000305|PubMed:22416142}.
CC -!- DISRUPTION PHENOTYPE: Longer roots and increased number of lateral
CC roots (PubMed:22416142). No effect on the appearance of plants or time
CC of flowering (PubMed:22416142, PubMed:22738221). Reduced fertility
CC (PubMed:22416142). Rbl10 and rbl11 double mutants have no visible
CC phenotype (PubMed:22738221). {ECO:0000269|PubMed:22416142,
CC ECO:0000269|PubMed:22738221}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG40087.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079374; AAG40087.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30602.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30603.1; -; Genomic_DNA.
DR RefSeq; NP_001185093.1; NM_001198164.2. [F4ICF4-2]
DR RefSeq; NP_173900.2; NM_102339.3. [F4ICF4-1]
DR AlphaFoldDB; F4ICF4; -.
DR SMR; F4ICF4; -.
DR STRING; 3702.AT1G25290.1; -.
DR MEROPS; S54.A08; -.
DR PaxDb; F4ICF4; -.
DR PRIDE; F4ICF4; -.
DR ProteomicsDB; 236510; -. [F4ICF4-1]
DR EnsemblPlants; AT1G25290.1; AT1G25290.1; AT1G25290. [F4ICF4-1]
DR EnsemblPlants; AT1G25290.2; AT1G25290.2; AT1G25290. [F4ICF4-2]
DR GeneID; 839113; -.
DR Gramene; AT1G25290.1; AT1G25290.1; AT1G25290. [F4ICF4-1]
DR Gramene; AT1G25290.2; AT1G25290.2; AT1G25290. [F4ICF4-2]
DR KEGG; ath:AT1G25290; -.
DR Araport; AT1G25290; -.
DR TAIR; locus:2032940; AT1G25290.
DR eggNOG; KOG2289; Eukaryota.
DR HOGENOM; CLU_055068_8_0_1; -.
DR InParanoid; F4ICF4; -.
DR OrthoDB; 1253228at2759; -.
DR BRENDA; 3.4.21.105; 399.
DR PRO; PR:F4ICF4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4ICF4; baseline and differential.
DR Genevisible; F4ICF4; AT.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0019374; P:galactolipid metabolic process; IMP:TAIR.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
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 Alternative splicing; Chloroplast; Hydrolase; Membrane; Plastid; Protease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..26
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 27..343
FT /note="RHOMBOID-like protein 10, chloroplastic"
FT /id="PRO_0000433331"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 240
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT ACT_SITE 293
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT VAR_SEQ 217..224
FT /note="KPILRVLG -> S (in isoform 2)"
FT /id="VSP_057732"
SQ SEQUENCE 343 AA; 38222 MW; FD535E23A4635082 CRC64;
MVSVSLSHHN LWPPESGSTA FRGFATAASV HACHHVSRHL RLDFHLRSSL KKLQHFSDDA
RMKFARYQRV FVFNGANFLK SRVDIRLSQS SPFVCFFNGG ESRLNPRGGE EGSSNPETSK
RNTVNGRRWT NVLLAINVIM YIAQIASDGK VLTWGAKINS LIERGQLWRL ATASVLHANP
MHLMINCYSL NSIGPTAESL GGPKRFLAVY LTSAVAKPIL RVLGSAMSYW FNKAPSVGAS
GAIFGLVGSV AVFVIRHKQM VRGGNEDLMQ IAQIIALNMA MGLMSRRIDN WGHIGGLLGG
TAMTWLLGPQ WKYEYTTRDG RRVFMDSAPI PLLLRWRNEQ RRL
