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AGP16_ARATH
ID   AGP16_ARATH             Reviewed;          73 AA.
AC   O82337;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Arabinogalactan protein 16 {ECO:0000303|PubMed:11006345};
DE            Short=AtAGP16 {ECO:0000303|PubMed:11006345};
DE   AltName: Full=Arabinogalactan peptide 16 {ECO:0000303|PubMed:11006345};
DE            Short=AG-peptide 16 {ECO:0000303|PubMed:11006345};
DE   Flags: Precursor;
GN   Name=AGP16 {ECO:0000303|PubMed:11006345}; OrderedLocusNames=At2g46330;
GN   ORFNames=F11C10.2;
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], PROTEIN SEQUENCE OF 27-37, PYROGLUTAMATE
RP   FORMATION AT GLN-27, HYDROXYLATION AT PRO-31; PRO-33 AND PRO-35, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11006345; DOI=10.2307/3871187;
RA   Schultz C.J., Johnson K.L., Currie G., Bacic A.;
RT   "The classical arabinogalactan protein gene family of Arabidopsis.";
RL   Plant Cell 12:1751-1767(2000).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   PROTEIN SEQUENCE OF 27-37, HYDROXYLATION AT PRO-31; PRO-33 AND PRO-35,
RP   PYROGLUTAMATE FORMATION AT GLN-27, GLYCOSYLATION AT PRO-31; PRO-33 AND
RP   PRO-35, AND GPI-ANCHOR AT SER-37.
RX   PubMed=15322080; DOI=10.1074/jbc.m407594200;
RA   Schultz C.J., Ferguson K.L., Lahnstein J., Bacic A.;
RT   "Post-translational modifications of arabinogalactan-peptides of
RT   Arabidopsis thaliana. Endoplasmic reticulum and
RT   glycosylphosphatidylinositol-anchor signal cleavage sites and hydroxylation
RT   of proline.";
RL   J. Biol. Chem. 279:45503-45511(2004).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12177459; DOI=10.1104/pp.003459;
RA   Schultz C.J., Rumsewicz M.P., Johnson K.L., Jones B.J., Gaspar Y.M.,
RA   Bacic A.;
RT   "Using genomic resources to guide research directions. The arabinogalactan
RT   protein gene family as a test case.";
RL   Plant Physiol. 129:1448-1463(2002).
CC   -!- FUNCTION: Proteoglycan that seems to be implicated in diverse
CC       developmental roles such as differentiation, cell-cell recognition,
CC       embryogenesis and programmed cell death. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000269|PubMed:15322080}.
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=O82337-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in flowers.
CC       {ECO:0000269|PubMed:11006345}.
CC   -!- PTM: Contains 4-hydroxyproline; hydroxylated on Pro-31, Pro-33 and Pro-
CC       35. {ECO:0000269|PubMed:11006345, ECO:0000269|PubMed:15322080}.
CC   -!- PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline
CC       residues are glycosylated with arabinogalactan.
CC       {ECO:0000305|PubMed:15322080}.
CC   -!- SIMILARITY: Belongs to the AG-peptide AGP family. {ECO:0000305}.
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DR   EMBL; AF195897; AAG24284.1; -; mRNA.
DR   EMBL; AC005397; AAM15047.1; -; Genomic_DNA.
DR   EMBL; AC006526; AAD23036.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10680.1; -; Genomic_DNA.
DR   EMBL; AF410276; AAK95262.1; -; mRNA.
DR   EMBL; AY097370; AAM19886.1; -; mRNA.
DR   EMBL; AY085631; AAM62852.1; -; mRNA.
DR   PIR; E84901; E84901.
DR   RefSeq; NP_566070.3; NM_130196.5. [O82337-1]
DR   AlphaFoldDB; O82337; -.
DR   BioGRID; 4576; 17.
DR   IntAct; O82337; 16.
DR   STRING; 3702.AT2G46330.1; -.
DR   PaxDb; O82337; -.
DR   EnsemblPlants; AT2G46330.1; AT2G46330.1; AT2G46330. [O82337-1]
DR   GeneID; 819241; -.
DR   Gramene; AT2G46330.1; AT2G46330.1; AT2G46330. [O82337-1]
DR   KEGG; ath:AT2G46330; -.
DR   Araport; AT2G46330; -.
DR   TAIR; locus:2039079; AT2G46330.
DR   eggNOG; ENOG502S708; Eukaryota.
DR   HOGENOM; CLU_187330_0_0_1; -.
DR   InParanoid; O82337; -.
DR   OMA; TIFVFIM; -.
DR   PhylomeDB; O82337; -.
DR   PRO; PR:O82337; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82337; baseline and differential.
DR   Genevisible; O82337; AT.
DR   GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR009424; AGP16/20/22/41.
DR   PANTHER; PTHR33374; PTHR33374; 1.
DR   Pfam; PF06376; AGP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Direct protein sequencing;
KW   Glycoprotein; GPI-anchor; Hydroxylation; Lipoprotein; Membrane;
KW   Proteoglycan; Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   PEPTIDE         27..37
FT                   /note="Arabinogalactan protein 16"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT                   /id="PRO_0000269019"
FT   PROPEP          38..73
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:11006345,
FT                   ECO:0000305|PubMed:15322080"
FT                   /id="PRO_0000269020"
FT   MOD_RES         27
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   MOD_RES         31
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   MOD_RES         33
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   MOD_RES         35
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   LIPID           37
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000269|PubMed:15322080"
FT   CARBOHYD        31
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:15322080"
FT   CARBOHYD        33
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:15322080"
FT   CARBOHYD        35
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:15322080"
SQ   SEQUENCE   73 AA;  7602 MW;  F7BE0B27F92DD1C2 CRC64;
     MASRNSVTGF ALFSFVFAVI LSLAGAQSLA PAPAPTSDGT SIDQGIAYLL MVVALVLTYL
     IHPLDASSSY SFF
 
 
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