SHGR2_ARATH
ID SHGR2_ARATH Reviewed; 933 AA.
AC Q8W5R2; Q9C6U4; Q9C861;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Phospholipase SGR2;
DE EC=3.1.1.-;
DE AltName: Full=Protein SHOOT GRAVITROPISM 2;
GN Name=SGR2; OrderedLocusNames=At1g31480; ORFNames=F27M3.29, T8E3.1;
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP GLY-320 AND GLY-446, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11826297; DOI=10.1105/tpc.010215;
RA Kato T., Morita M.T., Fukaki H., Yamauchi Y., Uehara M., Niihama M.,
RA Tasaka M.;
RT "SGR2, a phospholipase-like protein, and ZIG/SGR4, a SNARE, are involved in
RT the shoot gravitropism of Arabidopsis.";
RL Plant Cell 14:33-46(2002).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8819871; DOI=10.1104/pp.110.3.945;
RA Fukaki H., Fujisawa H., Tasaka M.;
RT "SGR1, SGR2, SGR3: novel genetic loci involved in shoot gravitropism in
RT Arabidopsis thaliana.";
RL Plant Physiol. 110:945-955(1996).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12024223; DOI=10.1007/s003440010047;
RA Kato T., Morita M.T., Tasaka M.;
RT "Role of endodermal cell vacuoles in shoot gravitropism.";
RL J. Plant Growth Regul. 21:113-119(2002).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11826298; DOI=10.1105/tpc.010216;
RA Morita M.T., Kato T., Nagafusa K., Saito C., Ueda T., Nakano A., Tasaka M.;
RT "Involvement of the vacuoles of the endodermis in the early process of
RT shoot gravitropism in Arabidopsis.";
RL Plant Cell 14:47-56(2002).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16344262; DOI=10.1093/pcp/pci237;
RA Mano E., Horiguchi G., Tsukaya H.;
RT "Gravitropism in leaves of Arabidopsis thaliana (L.) Heynh.";
RL Plant Cell Physiol. 47:217-223(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21645145; DOI=10.1111/j.1365-313x.2011.04665.x;
RA Saito C., Uemura T., Awai C., Tominaga M., Ebine K., Ito J., Ueda T.,
RA Abe H., Morita M.T., Tasaka M., Nakano A.;
RT "The occurrence of 'bulbs', a complex configuration of the vacuolar
RT membrane, is affected by mutations of vacuolar SNARE and phospholipase in
RT Arabidopsis.";
RL Plant J. 68:64-73(2011).
CC -!- FUNCTION: Involved in vacuolar formation or function (e.g. formation of
CC vacuolar membrane 'bulbs'). Required for amyloplast sedimentation in
CC the endodermis during shoot gravitropism, which are thus acting as
CC statoliths. Particularly important for the negative gravitropism
CC leading to leaf movement observed in darkness.
CC {ECO:0000269|PubMed:11826297, ECO:0000269|PubMed:11826298,
CC ECO:0000269|PubMed:12024223, ECO:0000269|PubMed:16344262,
CC ECO:0000269|PubMed:21645145, ECO:0000269|PubMed:8819871}.
CC -!- SUBUNIT: Forms oligomers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11826298}.
CC Note=Detected in small organelles membranes.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, leaves, stems and
CC floral buds, and, at low levels, in siliques.
CC {ECO:0000269|PubMed:11826297}.
CC -!- DEVELOPMENTAL STAGE: Expressed in young seedlings and progressively
CC confined in the elongation zone of the root during seedlings growth.
CC {ECO:0000269|PubMed:11826298}.
CC -!- DISRUPTION PHENOTYPE: Abnormal amyloplast sedimentation and shoot
CC gravitropism. Abnormal gravitropism in both inflorescence stems and
CC hypocotyls accompanied by misshapen seeds and seedlings, including leaf
CC movement in darkness. Reduced formation of vacuolar membrane 'bulbs'.
CC The sgr2-1 mutant has no gravitropic response in inflorescence stems
CC but a reduced gravitropic response in hypocotyls.
CC {ECO:0000269|PubMed:11826297, ECO:0000269|PubMed:11826298,
CC ECO:0000269|PubMed:12024223, ECO:0000269|PubMed:16344262,
CC ECO:0000269|PubMed:21645145, ECO:0000269|PubMed:8819871}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51263.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG60149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB073133; BAB71959.1; -; mRNA.
DR EMBL; AC027135; AAG51263.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC074360; AAG60149.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31360.1; -; Genomic_DNA.
DR PIR; H86440; H86440.
DR RefSeq; NP_174433.2; NM_102887.5.
DR AlphaFoldDB; Q8W5R2; -.
DR STRING; 3702.AT1G31480.1; -.
DR iPTMnet; Q8W5R2; -.
DR PaxDb; Q8W5R2; -.
DR PRIDE; Q8W5R2; -.
DR ProteomicsDB; 234502; -.
DR EnsemblPlants; AT1G31480.1; AT1G31480.1; AT1G31480.
DR GeneID; 840038; -.
DR Gramene; AT1G31480.1; AT1G31480.1; AT1G31480.
DR KEGG; ath:AT1G31480; -.
DR Araport; AT1G31480; -.
DR TAIR; locus:2028641; AT1G31480.
DR eggNOG; KOG2308; Eukaryota.
DR HOGENOM; CLU_006932_1_0_1; -.
DR InParanoid; Q8W5R2; -.
DR OMA; WQNENIV; -.
DR OrthoDB; 777968at2759; -.
DR PhylomeDB; Q8W5R2; -.
DR PRO; PR:Q8W5R2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W5R2; baseline and differential.
DR Genevisible; Q8W5R2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008970; F:phospholipase A1 activity; ISS:TAIR.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0009660; P:amyloplast organization; IMP:TAIR.
DR GO; GO:0009590; P:detection of gravity; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009959; P:negative gravitropism; IMP:TAIR.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004177; DDHD_dom.
DR Pfam; PF02862; DDHD; 2.
DR SMART; SM01127; DDHD; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS51043; DDHD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Reference proteome; Vacuole.
FT CHAIN 1..933
FT /note="Phospholipase SGR2"
FT /id="PRO_0000429059"
FT DOMAIN 669..868
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..631
FT /evidence="ECO:0000255"
FT COMPBIAS 489..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 444
FT /evidence="ECO:0000250"
FT MUTAGEN 320
FT /note="G->S: In sgr2-6; altered shoot gravitropism."
FT /evidence="ECO:0000269|PubMed:11826297"
FT MUTAGEN 446
FT /note="G->A: In sgr2-3; altered shoot gravitropism."
FT /evidence="ECO:0000269|PubMed:11826297"
SQ SEQUENCE 933 AA; 106316 MW; 5014BB7731A4D053 CRC64;
MEDRETHLGT REVNETSPDL LKNTPSNIAR LEDVIEQCHG RQKYLAQTRS PSDGSDVRWY
FCKVPLAENE LAASVPRTDV VGKSEYFRFG MRDSLAIEAS FLQREDELLS LWWKEYAECS
EGPKLQVNSK KKSIETPSEA SVSSSLYEVE EERVGVPVKG GLYEVDLVRR HCFPVYWNGD
NRRVLRGHWF ARKGGLDWLP IPETVSEQLE VAYRNKVWRR RSFQPSGLFA ARIDLQGSSL
GLHALFTGED DTWEAWLNVD PSGFSGIVGY TGNGIKLRRG YAGSYSPKPT QEELRQQKEE
EMDDYCSQVP VRHLVFMVHG IGQKGEKSNL VDDVGNFRQI TAALAERHLT SHQLSTQRVL
FIPCQWRKGL KLSGEAAVDK CTLDGVRRFR EMLSATVHDV LYYMSPIYCQ AIIDSVSKQL
NRLYLKFLKR NPDYVGKISI YGHSLGSVLS YDILCHQHNL SSPFPMDSVY KKFFPDEESP
PTPAKADKPC SSHPSSNFEP EKSDQLNNPE KITGQDNNTM AKEPTVLEHH DVIQEDPSLI
SDSVVANVGL ERRGGQEDDH HDSSGAISSQ DVPDGADCRT PDSPSCSQEQ SWDKESVNSN
NEERIKLLQD EVNSLRSKVA QLLSENARIL SDEKAKTSVA PKELNNEKVQ TEDADAPTSF
TPFIKYQKLE FKVDTFFAVG SPLGVFLALR NIRLGIGKGK DYWEEENAIE EMPACRRMFN
IFHPYDPVAY RVEPLVCKEY LPERPVIIPY HRGGKRLHIG LQDFREDFAA RSQRIMNHFD
SVRTRVLTIC QSKSADNLDE MEETDDEKDD RSYGSLMIER LTGTRDGRID HMLQEKTFEH
PYLQAIGAHT NYWRDQDTAL FIIKHLYREL PDGPNSPTES TEGDDSPKDS SRPHSWIDRR
EADYDDEELP LTFSDKQITR SFSAEAKKYL KKP
