ID   GCR2_ARATH              Reviewed;         410 AA.
AC   F4IEM5; Q9C929;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=LanC-like protein GCR2;
DE   AltName: Full=G-protein coupled receptor 2;
GN   Name=GCR2; Synonyms=GPCR; OrderedLocusNames=At1g52920; ORFNames=F14G24.19;
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=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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17894782; DOI=10.1111/j.1365-313x.2007.03291.x;
RA   Gao Y., Zeng Q., Guo J., Cheng J., Ellis B.E., Chen J.G.;
RT   "Genetic characterization reveals no role for the reported ABA receptor,
RT   GCR2, in ABA control of seed germination and early seedling development in
RT   Arabidopsis.";
RL   Plant J. 52:1001-1013(2007).
RN   [4]
RP   FUNCTION, INTERACTION WITH GPA1, AND DISRUPTION PHENOTYPE.
RX   PubMed=17347412; DOI=10.1126/science.1135882;
RA   Liu X., Yue Y., Li B., Nie Y., Li W., Wu W.H., Ma L.;
RT   "A G protein-coupled receptor is a plasma membrane receptor for the plant
RT   hormone abscisic acid.";
RL   Science 315:1712-1716(2007).
RN   [5]
RP   COMMENT ON PUBMED:17347412 RESULTS.
RX   PubMed=17991845; DOI=10.1126/science.1143230;
RA   Johnston C.A., Temple B.R., Chen J.G., Gao Y., Moriyama E.N., Jones A.M.,
RA   Siderovski D.P., Willard F.S.;
RT   "Comment on 'A G protein coupled receptor is a plasma membrane receptor for
RT   the plant hormone abscisic acid'.";
RL   Science 318:914-914(2007).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18714360; DOI=10.1371/journal.pone.0002982;
RA   Guo J., Zeng Q., Emami M., Ellis B.E., Chen J.G.;
RT   "The GCR2 gene family is not required for ABA control of seed germination
RT   and early seedling development in Arabidopsis.";
RL   PLoS ONE 3:E2982-E2982(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=19286934; DOI=10.1104/pp.109.135749;
RA   Risk J.M., Day C.L., Macknight R.C.;
RT   "Reevaluation of abscisic acid-binding assays shows that G-protein-coupled
RT   receptor2 does not bind abscisic acid.";
RL   Plant Physiol. 150:6-11(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH ZINC ION.
RA   Chen J.-H., Guo J., Chen J.-G., Nair S.K.;
RT   "Crystal structure of Arabidopsis GCR2 identifies a novel clade of
RT   lantibiotic cyclase-like proteins.";
RL   Submitted (JUL-2011) to the PDB data bank.
CC   -!- FUNCTION: May play a role in abscisic acid (ABA) signaling.
CC       {ECO:0000269|PubMed:17347412, ECO:0000269|PubMed:17894782,
CC       ECO:0000269|PubMed:18714360, ECO:0000269|PubMed:19286934}.
CC   -!- SUBUNIT: May interact (via C-terminus) with GPA1. {ECO:0000305|Ref.8}.
CC   -!- INTERACTION:
CC       F4IEM5; P18064: GPA1; NbExp=5; IntAct=EBI-1804974, EBI-443890;
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. However, in growth conditions described in PubMed:17347412
CC       mutant plants have decreased sensitivity to abscisic acid (ABA).
CC       {ECO:0000269|PubMed:17347412, ECO:0000269|PubMed:17894782,
CC       ECO:0000269|PubMed:18714360}.
CC   -!- SIMILARITY: Belongs to the LanC-like protein family. {ECO:0000305}.
CC   -!- CAUTION: Was originally described as a plasma membrane G-protein
CC       coupled receptor (GPCR) that binds ABA. Binding of ABA to GCR2 results
CC       in the release of G protein and dissociation of the heterotrimeric
CC       complex to activate downstream ABA effectors and to trigger the ABA
CC       responses (PubMed:17347412). However, GCR2 has been controversial with
CC       respect to the reproducibility of the results (PubMed:17894782,
CC       PubMed:18714360 and PubMed:19286934). Moreover, GCR2 lacks the
CC       prototypical seven transmembrane domains of GPCRs, and is homologous to
CC       mammalian lanthionine synthetase C-like (LANCL) proteins
CC       (PubMed:17991845). Intriguingly, it was shown that human granulocytes
CC       and insulin-producing rat insulinoma cells release ABA, and that LANCL2
CC       is necessary for ABA binding and signaling in these cells
CC       (PubMed:19667068). {ECO:0000305|PubMed:17347412,
CC       ECO:0000305|PubMed:17991845}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52264.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC019018; AAG52264.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE32868.1; -; Genomic_DNA.
DR   PIR; E96570; E96570.
DR   RefSeq; NP_175700.2; NM_104170.3.
DR   PDB; 3T33; X-ray; 2.25 A; A=1-410.
DR   PDBsum; 3T33; -.
DR   AlphaFoldDB; F4IEM5; -.
DR   SMR; F4IEM5; -.
DR   BioGRID; 26950; 1.
DR   IntAct; F4IEM5; 1.
DR   STRING; 3702.AT1G52920.1; -.
DR   PaxDb; F4IEM5; -.
DR   PRIDE; F4IEM5; -.
DR   ProteomicsDB; 222175; -.
DR   EnsemblPlants; AT1G52920.1; AT1G52920.1; AT1G52920.
DR   GeneID; 841725; -.
DR   Gramene; AT1G52920.1; AT1G52920.1; AT1G52920.
DR   KEGG; ath:AT1G52920; -.
DR   Araport; AT1G52920; -.
DR   TAIR; locus:2011466; AT1G52920.
DR   eggNOG; KOG2787; Eukaryota.
DR   HOGENOM; CLU_036244_0_1_1; -.
DR   InParanoid; F4IEM5; -.
DR   OMA; MAGTIHF; -.
DR   OrthoDB; 681208at2759; -.
DR   PRO; PR:F4IEM5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4IEM5; baseline and differential.
DR   Genevisible; F4IEM5; AT.
DR   GO; GO:0019898; C:extrinsic component of membrane; ISS:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0010427; F:abscisic acid binding; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0010231; P:maintenance of seed dormancy; IMP:TAIR.
DR   GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR007822; LANC-like.
DR   InterPro; IPR020464; LanC-like_prot_euk.
DR   Pfam; PF05147; LANC_like; 1.
DR   PRINTS; PR01951; LANCEUKARYTE.
DR   PRINTS; PR01950; LANCSUPER.
DR   SMART; SM01260; LANC_like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Abscisic acid signaling pathway; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..410
FT                   /note="LanC-like protein GCR2"
FT                   /id="PRO_0000424627"
FT   BINDING         283
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   HELIX           31..37
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           40..62
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   TURN            63..68
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           79..93
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           96..113
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           125..139
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           142..153
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   TURN            165..167
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           169..183
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           190..207
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           231..239
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           245..260
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   STRAND          270..273
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           286..300
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           303..319
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   STRAND          322..324
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           331..345
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           348..370
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   STRAND          373..375
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   STRAND          382..386
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           387..397
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   HELIX           400..402
FT                   /evidence="ECO:0007829|PDB:3T33"
FT   TURN            406..408
FT                   /evidence="ECO:0007829|PDB:3T33"
SQ   SEQUENCE   410 AA;  46451 MW;  DB8240DC0A60D6F9 CRC64;
     MGERFFRNEM PEFVPEDLSG EEETVTECKD SLTKLLSLPY KSFSEKLHRY ALSIKDKVVW
     ETWERSGKRV RDYNLYTGVL GTAYLLFKSY QVTRNEDDLK LCLENVEACD VASRDSERVT
     FICGYAGVCA LGAVAAKCLG DDQLYDRYLA RFRGIRLPSD LPYELLYGRA GYLWACLFLN
     KHIGQESISS ERMRSVVEEI FRAGRQLGNK GTCPLMYEWH GKRYWGAAHG LAGIMNVLMH
     TELEPDEIKD VKGTLSYMIQ NRFPSGNYLS SEGSKSDRLV HWCHGAPGVA LTLVKAAQVY
     NTKEFVEAAM EAGEVVWSRG LLKRVGICHG ISGNTYVFLS LYRLTRNPKY LYRAKAFASF
     LLDKSEKLIS EGQMHGGDRP FSLFEGIGGM AYMLLDMNDP TQALFPGYEL