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AGP4_ARATH
ID   AGP4_ARATH              Reviewed;         135 AA.
AC   Q9ZT16;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Classical arabinogalactan protein 4;
DE   Flags: Precursor;
GN   Name=AGP4; OrderedLocusNames=At5g10430; ORFNames=F12B17_220;
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].
RC   STRAIN=cv. Columbia;
RA   Schultz C.J., Gilson P.R., Oxley D., Youl J.J., Bacic A.;
RT   "GPI-anchors on arabinogalactan-proteins: implications for signalling in
RT   plants.";
RL   Trends Plant Sci. 3:426-431(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10451111;
RX   DOI=10.1002/(sici)1522-2683(19990701)20:10<2027::aid-elps2027>3.0.co;2-a;
RA   Sherrier D.J., Prime T.A., Dupree P.;
RT   "Glycosylphosphatidylinositol-anchored cell-surface proteins from
RT   Arabidopsis.";
RL   Electrophoresis 20:2027-2035(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
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   [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 22-40, HYDROXYLATION AT PRO-24; PRO-26; PRO-28; PRO-32;
RP   PRO-33; PRO-34; PRO-37; PRO-38 AND PRO-39, PYROGLUTAMATE FORMATION AT
RP   GLN-22, AND TISSUE 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   [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.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots, flowers and leaves.
CC       {ECO:0000269|PubMed:11006345}.
CC   -!- PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline
CC       residues are glycosylated with arabinogalactan.
CC   -!- SIMILARITY: Belongs to the classical AGP family. {ECO:0000305}.
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DR   EMBL; AF082301; AAC77826.1; -; mRNA.
DR   EMBL; AF060874; AAD38870.1; -; mRNA.
DR   EMBL; AL353995; CAB89400.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91539.1; -; Genomic_DNA.
DR   EMBL; AF372885; AAK49601.1; -; mRNA.
DR   EMBL; AY042794; AAK68734.1; -; mRNA.
DR   EMBL; BT002666; AAO11582.1; -; mRNA.
DR   PIR; T49996; T49996.
DR   RefSeq; NP_196605.1; NM_121081.3.
DR   AlphaFoldDB; Q9ZT16; -.
DR   STRING; 3702.AT5G10430.1; -.
DR   PaxDb; Q9ZT16; -.
DR   EnsemblPlants; AT5G10430.1; AT5G10430.1; AT5G10430.
DR   GeneID; 830907; -.
DR   Gramene; AT5G10430.1; AT5G10430.1; AT5G10430.
DR   KEGG; ath:AT5G10430; -.
DR   Araport; AT5G10430; -.
DR   TAIR; locus:2142524; AT5G10430.
DR   eggNOG; ENOG502SY2B; Eukaryota.
DR   HOGENOM; CLU_149596_0_0_1; -.
DR   InParanoid; Q9ZT16; -.
DR   OMA; APHADRT; -.
DR   PRO; PR:Q9ZT16; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9ZT16; baseline and differential.
DR   Genevisible; Q9ZT16; 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:0010198; P:synergid death; IMP:TAIR.
DR   InterPro; IPR044959; AGP.
DR   PANTHER; PTHR36321; PTHR36321; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW   Hydroxylation; Lipoprotein; Membrane; Proteoglycan;
KW   Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   CHAIN           22..111
FT                   /note="Classical arabinogalactan protein 4"
FT                   /id="PRO_0000268991"
FT   PROPEP          112..135
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000268992"
FT   REGION          22..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..97
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         22
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         24
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         26
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         28
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         32
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         33
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         34
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         37
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         38
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   MOD_RES         39
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11006345"
FT   LIPID           111
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        26
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        32
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        33
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        34
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        37
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        38
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="O-linked (Ara...) hydroxyproline"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   135 AA;  12803 MW;  E2F4095EFB5BDBC3 CRC64;
     MGSKIVQVFL MLALFATSAL AQAPAPTPTA TPPPATPPPV ATPPPVATPP PAATPAPATP
     PPAATPAPAT TPPSVAPSPA DVPTASPPAP EGPTVSPSSA PGPSDASPAP SAAFSNKAFF
     AGTAFAAIMY AAVLA
 
 
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