MLP28_ARATH
ID MLP28_ARATH Reviewed; 335 AA.
AC Q9SSK9;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=MLP-like protein 28;
GN Name=MLP28; OrderedLocusNames=At1g70830; ORFNames=F15H11.8;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Muller S., Klimt S., Hauser M.T.;
RT "Molecular and phylogenetic analysis of a gene family in Arabidopsis
RT thaliana with similarities to major latex, pathogenesis-related and
RT ripening-induced proteins.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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 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 [5]
RP STRUCTURE BY NMR OF 17-173, AND FUNCTION.
RX PubMed=19326460; DOI=10.1002/prot.22396;
RA Lytle B.L., Song J., de la Cruz N.B., Peterson F.C., Johnson K.A.,
RA Bingman C.A., Phillips G.N. Jr., Volkman B.F.;
RT "Structures of two Arabidopsis thaliana major latex proteins represent
RT novel helix-grip folds.";
RL Proteins 76:237-243(2009).
CC -!- FUNCTION: Can bind steroids (in vitro), and may also bind other types
CC of hydrophobic ligands. {ECO:0000269|PubMed:19326460}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SSK9-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the MLP family. {ECO:0000305}.
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DR EMBL; AJ306143; CAC83581.1; -; Genomic_DNA.
DR EMBL; AC008148; AAD55498.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35122.1; -; Genomic_DNA.
DR EMBL; AY070107; AAL49844.1; -; mRNA.
DR EMBL; AY102107; AAM26677.1; -; mRNA.
DR EMBL; AY123016; AAM67549.1; -; mRNA.
DR EMBL; BT000581; AAN18150.1; -; mRNA.
DR PIR; A96733; A96733.
DR RefSeq; NP_849875.1; NM_179544.2. [Q9SSK9-1]
DR PDB; 2I9Y; NMR; -; A=17-173.
DR PDBsum; 2I9Y; -.
DR AlphaFoldDB; Q9SSK9; -.
DR SMR; Q9SSK9; -.
DR BioGRID; 28640; 4.
DR IntAct; Q9SSK9; 1.
DR STRING; 3702.AT1G70830.1; -.
DR iPTMnet; Q9SSK9; -.
DR PaxDb; Q9SSK9; -.
DR PRIDE; Q9SSK9; -.
DR ProteomicsDB; 251414; -. [Q9SSK9-1]
DR DNASU; 843420; -.
DR EnsemblPlants; AT1G70830.1; AT1G70830.1; AT1G70830. [Q9SSK9-1]
DR GeneID; 843420; -.
DR Gramene; AT1G70830.1; AT1G70830.1; AT1G70830. [Q9SSK9-1]
DR KEGG; ath:AT1G70830; -.
DR Araport; AT1G70830; -.
DR TAIR; locus:2014000; AT1G70830.
DR eggNOG; ENOG502RN75; Eukaryota.
DR InParanoid; Q9SSK9; -.
DR OrthoDB; 1315011at2759; -.
DR PhylomeDB; Q9SSK9; -.
DR EvolutionaryTrace; Q9SSK9; -.
DR PRO; PR:Q9SSK9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSK9; baseline and differential.
DR Genevisible; Q9SSK9; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR Gene3D; 3.30.530.20; -; 2.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 2.
DR SMART; SM01037; Bet_v_1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Reference proteome.
FT CHAIN 1..335
FT /note="MLP-like protein 28"
FT /id="PRO_0000210068"
FT STRAND 20..34
FT /evidence="ECO:0007829|PDB:2I9Y"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:2I9Y"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2I9Y"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2I9Y"
FT STRAND 84..96
FT /evidence="ECO:0007829|PDB:2I9Y"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:2I9Y"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:2I9Y"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2I9Y"
FT STRAND 115..129
FT /evidence="ECO:0007829|PDB:2I9Y"
FT STRAND 132..145
FT /evidence="ECO:0007829|PDB:2I9Y"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2I9Y"
FT HELIX 152..170
FT /evidence="ECO:0007829|PDB:2I9Y"
SQ SEQUENCE 335 AA; 37615 MW; 0FC210430B2ABC0B CRC64;
MADVATKHPM EDEVKKTEAS SLVGKLETDV EIKASADKFH HMFAGKPHHV SKASPGNIQG
CDLHEGDWGT VGSIVFWNYV HDGEAKVAKE RIEAVEPDKN LITFRVIEGD LMKEYKSFLL
TIQVTPKPGG PGSIVHWHLE YEKISEEVAH PETLLQFCVE VSKEIDEHLL AEEEEVKTPE
TPSLVGKLET DVEIKASAEK FHHMFAGKPH HVSKASPGNI QGCDLHEGDW GQVGSIVFWN
YVHDREAKVA KERIEAVEPN KNLITFRVID GDLMKEYKSF LLTIQVTPKL GGPGSIVHWH
LEYEKISEEV AHPETLLQFC VEVSKEIDEH LLAEE
