RBL8_ARATH
ID RBL8_ARATH Reviewed; 351 AA.
AC F4I8K2; F2Z6M1; Q1PFC3; Q9SH15;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=RHOMBOID-like protein 8 {ECO:0000305};
DE Short=AtRBL8 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000305};
DE AltName: Full=Protein KOMPEITO {ECO:0000303|PubMed:16223493};
GN Name=KOM {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
GN Synonyms=RBL8 {ECO:0000305};
GN OrderedLocusNames=At1g77860 {ECO:0000312|Araport:AT1G77860};
GN ORFNames=F28K19.7 {ECO:0000312|EMBL:AAF17700.1};
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 [GENOMIC DNA].
RA Kanaoka M.M., Shimizu K.K., Urban S., Freeman M., Hong Z., Okada K.;
RT "A plant Rhomboid responsible for the processing of multi-path membrane
RT protein and pollen-stigma adhesion.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-340.
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RA Kanaoka M., Shimizu K., Okada K.;
RT "KOMPEITO is important for callose accumulation and the exine pattern
RT formation in Arabidopsis.";
RL (In) Proceedings of the 14th international conference on Arabidopsis
RL research, abstract#360, Chapel Hill (2003).
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. {ECO:0000303|PubMed:22007993}.
CC -!- FUNCTION: Probably essential for the meiosis stage-specific callose
CC accumulation and pollen exine formation. {ECO:0000305|Ref.9}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|Ref.9};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen mother cell.
CC {ECO:0000305|Ref.9}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17700.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABE65782.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAK20219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB257405; BAK20219.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009243; AAF17700.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36036.1; -; Genomic_DNA.
DR EMBL; DQ446440; ABE65782.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001321009.1; NM_001334801.1.
DR RefSeq; NP_177909.2; NM_106435.2.
DR AlphaFoldDB; F4I8K2; -.
DR STRING; 3702.AT1G77860.1; -.
DR PaxDb; F4I8K2; -.
DR PRIDE; F4I8K2; -.
DR EnsemblPlants; AT1G77860.1; AT1G77860.1; AT1G77860.
DR GeneID; 844122; -.
DR Gramene; AT1G77860.1; AT1G77860.1; AT1G77860.
DR KEGG; ath:AT1G77860; -.
DR Araport; AT1G77860; -.
DR TAIR; locus:2029376; AT1G77860.
DR eggNOG; KOG2289; Eukaryota.
DR HOGENOM; CLU_011531_0_0_1; -.
DR InParanoid; F4I8K2; -.
DR OMA; FTSPWLH; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; F4I8K2; -.
DR PRO; PR:F4I8K2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I8K2; baseline and differential.
DR Genevisible; F4I8K2; AT.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Golgi apparatus; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="RHOMBOID-like protein 8"
FT /id="PRO_0000433329"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 351 AA; 39315 MW; EA540D01F1D03EAA CRC64;
MEVPTESKTT QIDEISHNLS FTTSNAGDSS WDKISFFRHR SRQIKRDTWL VSVFVLLQIV
LFAVTMGVND CSGNSHGHCS AKLLGRFSFQ SLSENPMLGP SASTLEHMGG LSWKALTENH
EIWRILTSPW LHSGLFHLFI NLGSLIFVGI YMEQQFGPLR IAVIYFLSGI MGSLFAVLFV
RNIPSISSGA AFFGLIGAML SALAKNWNLY NSKISALAII FTIFTVNFLI GFLPFIDNFA
NIGGFISGFL LGFVLLFKPQ LRQMPPSHKG KLFEDDMNRS TRLKEQFDRP VLRIICLLVF
CGILAGVLLA ACWGVNLNRH CHWCRYVDCV PTKKWSCSDM TTSCEVYSSK P
