RBL3_ARATH
ID RBL3_ARATH Reviewed; 346 AA.
AC Q9LYP1; B3H7G3;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=RHOMBOID-like protein 3 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
DE Short=AtRBL3 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
DE EC=3.4.21.- {ECO:0000305};
GN Name=RBL3 {ECO:0000303|PubMed:16223493, ECO:0000303|PubMed:17181860};
GN OrderedLocusNames=At5g07250 {ECO:0000312|Araport:AT5G07250};
GN ORFNames=T28J14.190 {ECO:0000312|EMBL:CAB87281.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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=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 [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. {ECO:0000303|PubMed:22007993}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:22738221}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Not localized in cytosol, mitochondria or
CC chloroplast. {ECO:0000269|PubMed:22738221}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LYP1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LYP1-2; Sequence=VSP_057730;
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; AL163652; CAB87281.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91127.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91128.1; -; Genomic_DNA.
DR EMBL; AY058157; AAL25572.1; -; mRNA.
DR EMBL; AY098983; AAM19993.1; -; mRNA.
DR PIR; T48496; T48496.
DR RefSeq; NP_001119182.1; NM_001125710.1. [Q9LYP1-2]
DR RefSeq; NP_196342.1; NM_120807.4. [Q9LYP1-1]
DR AlphaFoldDB; Q9LYP1; -.
DR IntAct; Q9LYP1; 3.
DR STRING; 3702.AT5G07250.1; -.
DR MEROPS; S54.A02; -.
DR PaxDb; Q9LYP1; -.
DR PRIDE; Q9LYP1; -.
DR ProteomicsDB; 236511; -. [Q9LYP1-1]
DR EnsemblPlants; AT5G07250.1; AT5G07250.1; AT5G07250. [Q9LYP1-1]
DR EnsemblPlants; AT5G07250.2; AT5G07250.2; AT5G07250. [Q9LYP1-2]
DR GeneID; 830616; -.
DR Gramene; AT5G07250.1; AT5G07250.1; AT5G07250. [Q9LYP1-1]
DR Gramene; AT5G07250.2; AT5G07250.2; AT5G07250. [Q9LYP1-2]
DR KEGG; ath:AT5G07250; -.
DR Araport; AT5G07250; -.
DR TAIR; locus:2182925; AT5G07250.
DR eggNOG; KOG2289; Eukaryota.
DR HOGENOM; CLU_011531_0_0_1; -.
DR InParanoid; Q9LYP1; -.
DR OMA; CTWCHYL; -.
DR PhylomeDB; Q9LYP1; -.
DR PRO; PR:Q9LYP1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYP1; baseline and differential.
DR Genevisible; Q9LYP1; 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:0009506; C:plasmodesma; HDA:TAIR.
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 Alternative splicing; Golgi apparatus; Hydrolase; Membrane; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..346
FT /note="RHOMBOID-like protein 3"
FT /id="PRO_0000433324"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT ACT_SITE 253
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54493"
FT VAR_SEQ 226..272
FT /note="Missing (in isoform 2)"
FT /id="VSP_057730"
SQ SEQUENCE 346 AA; 38491 MW; A5BE199ABB0C54FF CRC64;
MAVGDDDLEN RMSAKDRGIG SRGGDRNRIG PPPLPVALSS STEFGDNALS SRWTSWLVPM
FVVANVAVFV VAMFVNNCPN HFESHRLRGH CVAKFLGRLS FEPLRTNPLF GPSSHTLEKL
GALEWSKVVE KKEGWRLLTC IWLHAGVIHL GANMLSLVFI GIRLEQQFGF VRIGVIYLLS
GIGGSVLSSL FIRNSISVGA SGALFGLLGS MLSELFTNWT IYSNKIAALL TLLFVILINL
AIGILPHVDN FAHVGGFVTG FLLGFILLAR PQFKWLAREH MPQGTPLRYK YKTYQYLLWL
LSLVLLIAGF VVALLMLFRG ENGNDHCRWC HYLRCVPTSS WRCDDV
