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AGP14_ARATH
ID   AGP14_ARATH             Reviewed;          60 AA.
AC   Q9LVC0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Arabinogalactan protein 14 {ECO:0000303|PubMed:11006345};
DE            Short=AtAGP14 {ECO:0000303|PubMed:11006345};
DE   AltName: Full=Arabinogalactan peptide 14 {ECO:0000303|PubMed:11006345};
DE            Short=AG-peptide 14 {ECO:0000303|PubMed:11006345};
DE   Flags: Precursor;
GN   Name=AGP14 {ECO:0000303|PubMed:11006345}; OrderedLocusNames=At5g56540;
GN   ORFNames=MKN22.5;
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], HYDROXYLATION AT PRO-32; PRO-34 AND PRO-36, AND
RP   PROTEIN SEQUENCE OF 29-38.
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
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   [6]
RP   PROTEIN SEQUENCE OF 29-38, HYDROXYLATION AT PRO-32; PRO-34 AND PRO-36,
RP   GLYCOSYLATION AT PRO-32; PRO-34 AND PRO-36, AND GPI-ANCHOR AT SER-38.
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).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21248074; DOI=10.1104/pp.110.166520;
RA   Lin W.D., Liao Y.Y., Yang T.J., Pan C.Y., Buckhout T.J., Schmidt W.;
RT   "Coexpression-based clustering of Arabidopsis root genes predicts
RT   functional modules in early phosphate deficiency signaling.";
RL   Plant Physiol. 155:1383-1402(2011).
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 (Probable). Involved in the
CC       regulation of root hair elongation (PubMed:21248074).
CC       {ECO:0000269|PubMed:21248074, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9LVC0; Q94F58: NAC089; NbExp=2; IntAct=EBI-4429269, EBI-2319707;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000269|PubMed:15322080}.
CC   -!- PTM: Contains 4-hydroxyproline; hydroxylated on Pro-32, Pro-34 and Pro-
CC       36. {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   -!- DISRUPTION PHENOTYPE: Formation of abnormal long root hairs.
CC       {ECO:0000269|PubMed:21248074}.
CC   -!- SIMILARITY: Belongs to the AG-peptide AGP family. {ECO:0000305}.
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DR   EMBL; AF195895; AAG24282.1; -; mRNA.
DR   EMBL; AB019234; BAA97180.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96779.1; -; Genomic_DNA.
DR   EMBL; AK117330; BAC42000.1; -; mRNA.
DR   EMBL; BT004644; AAO42890.1; -; mRNA.
DR   RefSeq; NP_200465.1; NM_125037.3.
DR   AlphaFoldDB; Q9LVC0; -.
DR   BioGRID; 20999; 3.
DR   IntAct; Q9LVC0; 3.
DR   STRING; 3702.AT5G56540.1; -.
DR   PaxDb; Q9LVC0; -.
DR   EnsemblPlants; AT5G56540.1; AT5G56540.1; AT5G56540.
DR   GeneID; 835755; -.
DR   Gramene; AT5G56540.1; AT5G56540.1; AT5G56540.
DR   KEGG; ath:AT5G56540; -.
DR   Araport; AT5G56540; -.
DR   TAIR; locus:2167126; AT5G56540.
DR   eggNOG; ENOG502S9IR; Eukaryota.
DR   HOGENOM; CLU_183441_3_0_1; -.
DR   InParanoid; Q9LVC0; -.
DR   OMA; MMMTIMA; -.
DR   PhylomeDB; Q9LVC0; -.
DR   PRO; PR:Q9LVC0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LVC0; baseline and differential.
DR   Genevisible; Q9LVC0; AT.
DR   GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR   InterPro; IPR039281; AGP3/12/13/14/21.
DR   PANTHER; PTHR34114; PTHR34114; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW   Hydroxylation; Lipoprotein; Membrane; Proteoglycan; Reference proteome;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   PEPTIDE         29..38
FT                   /note="Arabinogalactan protein 14"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT                   /id="PRO_0000269015"
FT   PROPEP          39..60
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:11006345,
FT                   ECO:0000305|PubMed:15322080"
FT                   /id="PRO_0000269016"
FT   MOD_RES         32
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   MOD_RES         34
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   MOD_RES         36
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345,
FT                   ECO:0000269|PubMed:15322080"
FT   LIPID           38
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000269|PubMed:15322080"
FT   CARBOHYD        32
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:15322080"
FT   CARBOHYD        34
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:15322080"
FT   CARBOHYD        36
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:15322080"
SQ   SEQUENCE   60 AA;  6363 MW;  83F3A3185C53C0B4 CRC64;
     MEAMKMKLYV VVLVAVIAFS TVHQTVAAVD APAPSPTSDA SSFIPTFFAS VAVMAFGFFF
 
 
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