CAND2_ARATH
ID CAND2_ARATH Reviewed; 300 AA.
AC Q94AH1; Q9CAW5;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 2 {ECO:0000303|PubMed:18671868};
DE Short=AtCand2 {ECO:0000303|PubMed:18671868};
DE AltName: Full=Protein PHYTOMELATONIN RECEPTOR 1 {ECO:0000303|PubMed:29702752};
GN Name=CAND2 {ECO:0000303|PubMed:18671868};
GN Synonyms=PMTR1 {ECO:0000303|PubMed:29702752};
GN OrderedLocusNames=At3g05010 {ECO:0000312|Araport:AT3G05010};
GN ORFNames=T9J14.4 {ECO:0000312|EMBL:AAG51409.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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.
RX PubMed=17064408; DOI=10.1186/gb-2006-7-10-r96;
RA Moriyama E.N., Strope P.K., Opiyo S.O., Chen Z., Jones A.M.;
RT "Mining the Arabidopsis thaliana genome for highly-divergent seven
RT transmembrane receptors.";
RL Genome Biol. 7:R96.1-R96.9(2006).
RN [5]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18671868; DOI=10.1186/gb-2008-9-7-r120;
RA Gookin T.E., Kim J., Assmann S.M.;
RT "Whole proteome identification of plant candidate G-protein coupled
RT receptors in Arabidopsis, rice, and poplar: computational prediction and
RT in-vivo protein coupling.";
RL Genome Biol. 9:R120.1-R120.26(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY N-ACYL-HOMOSERINE
RP LACTONES.
RC STRAIN=cv. Columbia;
RX PubMed=22206669; DOI=10.1016/j.bbrc.2011.12.066;
RA Jin G., Liu F., Ma H., Hao S., Zhao Q., Bian Z., Jia Z., Song S.;
RT "Two G-protein-coupled-receptor candidates, Cand2 and Cand7, are involved
RT in Arabidopsis root growth mediated by the bacterial quorum-sensing signals
RT N-acyl-homoserine lactones.";
RL Biochem. Biophys. Res. Commun. 417:991-995(2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH GPA1, INDUCTION BY
RP MELATONIN, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=29702752; DOI=10.1111/jpi.12500;
RA Wei J., Li D.-X., Zhang J.-R., Shan C., Rengel Z., Song Z.-B., Chen Q.;
RT "Phytomelatonin receptor PMTR1-mediated signaling regulates stomatal
RT closure in Arabidopsis thaliana.";
RL J. Pineal Res. 65:E12500-E12500(2018).
CC -!- FUNCTION: Plays a role in plants and microbes interactions
CC (PubMed:22206669). G-protein coupled receptor involved in root growth
CC mediated by the bacterial quorum-sensing signals N-acyl-homoserine
CC lactones (AHLs) (PubMed:18671868, PubMed:22206669). Binds to melatonin
CC (PubMed:29702752). Phytomelatonin receptor required, in collaboration
CC with GPA1, for melatonin-mediated stomatal closure involving H(2)O(2)
CC and Ca(2+) signals (PubMed:29702752). {ECO:0000269|PubMed:18671868,
CC ECO:0000269|PubMed:22206669, ECO:0000269|PubMed:29702752}.
CC -!- SUBUNIT: Interacts with GPA1. {ECO:0000269|PubMed:29702752}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29702752};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in seedlings.
CC {ECO:0000269|PubMed:29702752}.
CC -!- INDUCTION: Induced by the N-acyl-homoserine lactones (AHLs) N-3-oxo-
CC hexanoyl-homoserine lactone (3OC6-HSL) and N-3-oxo-octanoyl-homoserine
CC lactone (3OC8-HSL) (PubMed:22206669). Triggered by melatonin in leaves,
CC cotyledons, hypocotyls, roots and guard cells (PubMed:29702752).
CC {ECO:0000269|PubMed:22206669, ECO:0000269|PubMed:29702752}.
CC -!- DISRUPTION PHENOTYPE: Small leaf size phenotype (PubMed:29702752).
CC Abolished Gram-negative bacteria-mediated promotion of root elongation
CC triggered by the N-acyl-homoserine lactones (AHLs) N-3-oxo-hexanoyl-
CC homoserine lactone (3OC6-HSL) and N-3-oxo-octanoyl-homoserine lactone
CC (3OC8-HSL) (PubMed:22206669). Insensitivity to melatonin-induced
CC stomatal closure associated with abolished melatonin-induced H(2)O(2)
CC production and Ca(2+) influx (PubMed:29702752).
CC {ECO:0000269|PubMed:22206669, ECO:0000269|PubMed:29702752}.
CC -!- SIMILARITY: Belongs to the UPF0359 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009465; AAG51409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74175.1; -; Genomic_DNA.
DR EMBL; AY046040; AAK76714.1; -; mRNA.
DR RefSeq; NP_566244.1; NM_111373.3.
DR AlphaFoldDB; Q94AH1; -.
DR IntAct; Q94AH1; 1.
DR STRING; 3702.AT3G05010.1; -.
DR PaxDb; Q94AH1; -.
DR PRIDE; Q94AH1; -.
DR EnsemblPlants; AT3G05010.1; AT3G05010.1; AT3G05010.
DR GeneID; 819662; -.
DR Gramene; AT3G05010.1; AT3G05010.1; AT3G05010.
DR KEGG; ath:AT3G05010; -.
DR Araport; AT3G05010; -.
DR TAIR; locus:2114835; AT3G05010.
DR eggNOG; KOG4536; Eukaryota.
DR HOGENOM; CLU_078931_0_0_1; -.
DR InParanoid; Q94AH1; -.
DR OMA; GGMLFWF; -.
DR OrthoDB; 948626at2759; -.
DR PhylomeDB; Q94AH1; -.
DR PRO; PR:Q94AH1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94AH1; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:1904408; F:melatonin binding; IDA:UniProtKB.
DR GO; GO:0008502; F:melatonin receptor activity; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR GO; GO:0019236; P:response to pheromone; IMP:UniProtKB.
DR GO; GO:0010015; P:root morphogenesis; IMP:TAIR.
DR InterPro; IPR018781; TPRA1/CAND2/CAND8.
DR PANTHER; PTHR15876; PTHR15876; 1.
DR Pfam; PF10160; Tmemb_40; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..300
FT /note="Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 2"
FT /id="PRO_0000447635"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
SQ SEQUENCE 300 AA; 34063 MW; 4975BA386A438569 CRC64;
MRVLSEIAES PFVISRLSPD STATGGFIGG WVGKCHGFLH NTVLVLASIL FVAYLAYEAK
KSLSKLSNRR SYIMIAYYGF LWLVSLLNLA WCCLQAWECT PGKEVIWNLL TLFTTSGMLF
LEVSLVAFLF QGNYASGAEA LTRTFLISGL VIGLDLLLKA IYLFGFGVPL FIDNNEHIHK
FKWGLWVIHK LLLAGIYGMI FFMYNSKWRE RLPARPAFYK YITVMLALNG LSLFACALTA
NGAHFGLWLY GITSVCYHAF YLPLLYVTFL ADFFQEEDLN LENVYYSEMK DAGFFDADWE
