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RBL9_ARATH
ID   RBL9_ARATH              Reviewed;         434 AA.
AC   Q9FFX0;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=RHOMBOID-like protein 9, chloroplastic {ECO:0000303|PubMed:17181860};
DE            Short=AtRBL9 {ECO:0000303|PubMed:17181860};
DE            EC=3.4.21.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=RBL9 {ECO:0000303|PubMed:17181860};
GN   OrderedLocusNames=At5g38510 {ECO:0000312|Araport:AT5G38510};
GN   ORFNames=MBB18.4 {ECO:0000312|EMBL:BAB10141.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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].
RA   Kim C.J., Chen H., Cheuk R., Shinn P., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) 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.
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   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. {ECO:0000303|PubMed:22007993}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC   -!- CAUTION: Might be an inactive rhomboid-type serine protease due to
CC       mismatches with the consensus active sites.
CC       {ECO:0000303|PubMed:17938163}.
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DR   EMBL; AB005231; BAB10141.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94327.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94328.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68896.1; -; Genomic_DNA.
DR   EMBL; BT012562; AAS99706.1; -; mRNA.
DR   EMBL; AK226685; BAE98792.1; -; mRNA.
DR   RefSeq; NP_001078681.1; NM_001085212.2.
DR   RefSeq; NP_001330612.1; NM_001344253.1.
DR   RefSeq; NP_198667.1; NM_123212.3.
DR   AlphaFoldDB; Q9FFX0; -.
DR   STRING; 3702.AT5G38510.1; -.
DR   PaxDb; Q9FFX0; -.
DR   PRIDE; Q9FFX0; -.
DR   ProteomicsDB; 225971; -.
DR   EnsemblPlants; AT5G38510.1; AT5G38510.1; AT5G38510.
DR   EnsemblPlants; AT5G38510.2; AT5G38510.2; AT5G38510.
DR   EnsemblPlants; AT5G38510.3; AT5G38510.3; AT5G38510.
DR   GeneID; 833839; -.
DR   Gramene; AT5G38510.1; AT5G38510.1; AT5G38510.
DR   Gramene; AT5G38510.2; AT5G38510.2; AT5G38510.
DR   Gramene; AT5G38510.3; AT5G38510.3; AT5G38510.
DR   KEGG; ath:AT5G38510; -.
DR   Araport; AT5G38510; -.
DR   TAIR; locus:2159808; AT5G38510.
DR   eggNOG; KOG2289; Eukaryota.
DR   HOGENOM; CLU_043890_0_0_1; -.
DR   InParanoid; Q9FFX0; -.
DR   OMA; VGHEINR; -.
DR   OrthoDB; 1253228at2759; -.
DR   PhylomeDB; Q9FFX0; -.
DR   PRO; PR:Q9FFX0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FFX0; baseline and differential.
DR   Genevisible; Q9FFX0; AT.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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: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   Chloroplast; Hydrolase; Membrane; Plastid; Protease; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..68
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           69..434
FT                   /note="RHOMBOID-like protein 9, chloroplastic"
FT                   /id="PRO_0000433330"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   434 AA;  47727 MW;  E8951EDFC3CF60E6 CRC64;
     MALFPLHHEV PCKGEVLFDS NGLRRFSSGL KHRTMAEATT LGRDCRMKSY MKSIPYCRSP
     RRRLCLVRAS SENKITKQRL KLLDSYFGKL QNDDEKPSIS TGDDIDRKAE LNVNEELDSL
     SAYLDKLQKD AKSKGLVSST LDVVKSEGGS VASKLRKTGI ENNNSPFQQF DDEDQAEDTL
     NFYAVSILAS INVGVCLFEA AAPVRNNNMG LLSLPLLYGA KINDLILAGE WWRLVTPMFL
     HSGIPHVALS SWALLTFGPK VCRDYGLFTF CLIYILGGVS GNFMSFLHTA DPTVGGTGPA
     FALIGAWLVD QNQNKEMIKS NEYEDLFQKA IIMTGFGLIL SHFGPIDDWT NLGALIAGIV
     YGFFTCPVLQ LGSGGSERQE GIVTVGPEKQ NSADPCKSFL LFTIFVAVIV TSLLLIGDGP
     LDFPTYDDVV YSLI
 
 
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