ID   ROSY1_ARATH             Reviewed;         160 AA.
AC   Q9AST8; Q8L8M3;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=MD-2-related lipid-recognition protein ROSY1 {ECO:0000305};
DE   AltName: Full=Protein INTERACTOR OF SYNAPTOTAGMIN 1 {ECO:0000303|PubMed:27044028};
DE   Flags: Precursor;
GN   Name=ROSY1 {ECO:0000303|PubMed:27044028};
GN   OrderedLocusNames=At2g16005 {ECO:0000312|Araport:AT2G16005};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, INTERACTION WITH SYT1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   INDUCTION BY GRAVITY STIMULATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27044028; DOI=10.1016/j.jplph.2016.03.011;
RA   Dalal J., Lewis D.R., Tietz O., Brown E.M., Brown C.S., Palme K.,
RA   Muday G.K., Sederoff H.W.;
RT   "ROSY1, a novel regulator of gravitropic response is a stigmasterol binding
RT   protein.";
RL   J. Plant Physiol. 196:28-40(2016).
CC   -!- FUNCTION: Involved in the regulation of gravitropic response and
CC       basipetal auxin transport in roots. Involved in salt stress tolerance.
CC       May facilitate membrane trafficking and asymmetric cell elongation via
CC       SYT1. Binds stigmasterol and dipalmitoyl phosphoethanolamine (DPPE) in
CC       vitro. {ECO:0000269|PubMed:27044028}.
CC   -!- SUBUNIT: Interacts with SYT1. {ECO:0000269|PubMed:27044028}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27044028}.
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in roots, in epidermis and
CC       cortex cells of the root elongation zone, and lateral root cap cells at
CC       the root tip. {ECO:0000269|PubMed:27044028}.
CC   -!- INDUCTION: Induced by gravity stimulation.
CC       {ECO:0000269|PubMed:27044028}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants exhibit decreased root basipetal auxin
CC       transport, faster root gravitropic response and increase in salt stress
CC       tolerance. {ECO:0000269|PubMed:27044028}.
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DR   EMBL; AC007134; AAM15402.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06454.1; -; Genomic_DNA.
DR   EMBL; AF361840; AAK32852.1; -; mRNA.
DR   EMBL; AY066048; AAL47415.1; -; mRNA.
DR   EMBL; AY088910; AAM67216.1; -; mRNA.
DR   RefSeq; NP_565385.1; NM_127159.3.
DR   AlphaFoldDB; Q9AST8; -.
DR   SMR; Q9AST8; -.
DR   STRING; 3702.AT2G16005.1; -.
DR   PaxDb; Q9AST8; -.
DR   PRIDE; Q9AST8; -.
DR   ProteomicsDB; 228218; -.
DR   EnsemblPlants; AT2G16005.1; AT2G16005.1; AT2G16005.
DR   GeneID; 816096; -.
DR   Gramene; AT2G16005.1; AT2G16005.1; AT2G16005.
DR   KEGG; ath:AT2G16005; -.
DR   Araport; AT2G16005; -.
DR   TAIR; locus:505006248; AT2G16005.
DR   eggNOG; KOG4680; Eukaryota.
DR   HOGENOM; CLU_140610_0_0_1; -.
DR   InParanoid; Q9AST8; -.
DR   OMA; HASMINQ; -.
DR   OrthoDB; 1548356at2759; -.
DR   PhylomeDB; Q9AST8; -.
DR   PRO; PR:Q9AST8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9AST8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:TAIR.
DR   GO; GO:0032934; F:sterol binding; IDA:TAIR.
DR   GO; GO:0032366; P:intracellular sterol transport; IEA:InterPro.
DR   GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0015918; P:sterol transport; IBA:GO_Central.
DR   CDD; cd00917; PG-PI_TP; 1.
DR   Gene3D; 2.70.220.10; -; 1.
DR   InterPro; IPR036846; GM2-AP_sf.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR003172; ML_dom.
DR   InterPro; IPR033917; ML_PG-PI_TP.
DR   InterPro; IPR039670; NPC2-like.
DR   PANTHER; PTHR11306; PTHR11306; 1.
DR   Pfam; PF02221; E1_DerP2_DerF2; 1.
DR   SMART; SM00737; ML; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..160
FT                   /note="MD-2-related lipid-recognition protein ROSY1"
FT                   /id="PRO_5010510524"
FT   CONFLICT        137
FT                   /note="E -> K (in Ref. 4; AAM67216)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   160 AA;  17228 MW;  C249FFC4345768AE CRC64;
     MAISHTQLLL LLLVSLFFSP ALCGPKFQTC DTGKEYPLKV SSVEISPDPV KRSGNGEITI
     TGVTNKEISD GVTVNLKLAV GMFPVSTKSY SLCDITACPV APGPIVLTLP NIFTPREKRT
     AIGYTIIISI TDKPLKESMM CILFVVKLTG HASMINQVTE