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FLA2_ARATH
ID   FLA2_ARATH              Reviewed;         403 AA.
AC   Q9SU13; Q8L9T2; Q9C5Q6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Fasciclin-like arabinogalactan protein 2;
DE   Flags: Precursor;
GN   Name=FLA2; OrderedLocusNames=At4g12730; ORFNames=T20K18.80;
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].
RX   PubMed=11554470; DOI=10.1023/a:1010683432529;
RA   Gaspar Y., Johnson K.L., McKenna J.A., Bacic A., Schultz C.J.;
RT   "The complex structures of arabinogalactan-proteins and the journey towards
RT   understanding function.";
RL   Plant Mol. Biol. 47:161-176(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   GENE FAMILY ORGANIZATION, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14645732; DOI=10.1104/pp.103.031237;
RA   Johnson K.L., Jones B.J., Bacic A., Schultz C.J.;
RT   "The fasciclin-like arabinogalactan proteins of Arabidopsis. A multigene
RT   family of putative cell adhesion molecules.";
RL   Plant Physiol. 133:1911-1925(2003).
CC   -!- FUNCTION: May be a cell surface adhesion protein.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in flowers and to a lesser extent
CC       in leaves and roots. {ECO:0000269|PubMed:14645732}.
CC   -!- INDUCTION: Down-regulated by abscisic acid (ABA).
CC       {ECO:0000269|PubMed:14645732}.
CC   -!- SIMILARITY: Belongs to the fasciclin-like AGP family. {ECO:0000305}.
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DR   EMBL; AF333971; AAK20858.1; -; mRNA.
DR   EMBL; AL049640; CAB40990.1; -; Genomic_DNA.
DR   EMBL; AL161534; CAB78315.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83171.1; -; Genomic_DNA.
DR   EMBL; AY142065; AAM98329.1; -; mRNA.
DR   EMBL; AY060582; AAL31207.1; -; mRNA.
DR   EMBL; AK230362; BAF02161.1; -; mRNA.
DR   EMBL; AY088236; AAM65777.1; -; mRNA.
DR   PIR; T06631; T06631.
DR   RefSeq; NP_193009.1; NM_117342.3.
DR   AlphaFoldDB; Q9SU13; -.
DR   SMR; Q9SU13; -.
DR   BioGRID; 12182; 7.
DR   IntAct; Q9SU13; 4.
DR   STRING; 3702.AT4G12730.1; -.
DR   PaxDb; Q9SU13; -.
DR   PRIDE; Q9SU13; -.
DR   ProteomicsDB; 230838; -.
DR   EnsemblPlants; AT4G12730.1; AT4G12730.1; AT4G12730.
DR   GeneID; 826885; -.
DR   Gramene; AT4G12730.1; AT4G12730.1; AT4G12730.
DR   KEGG; ath:AT4G12730; -.
DR   Araport; AT4G12730; -.
DR   TAIR; locus:2135818; AT4G12730.
DR   eggNOG; ENOG502QR33; Eukaryota.
DR   HOGENOM; CLU_036139_0_1_1; -.
DR   InParanoid; Q9SU13; -.
DR   OMA; VYNSMGM; -.
DR   OrthoDB; 984651at2759; -.
DR   PhylomeDB; Q9SU13; -.
DR   PRO; PR:Q9SU13; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SU13; baseline and differential.
DR   Genevisible; Q9SU13; AT.
DR   GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR   GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   Gene3D; 2.30.180.10; -; 2.
DR   InterPro; IPR036378; FAS1_dom_sf.
DR   InterPro; IPR000782; FAS1_domain.
DR   InterPro; IPR033254; Plant_FLA.
DR   PANTHER; PTHR32382; PTHR32382; 1.
DR   Pfam; PF02469; Fasciclin; 2.
DR   SMART; SM00554; FAS1; 2.
DR   SUPFAM; SSF82153; SSF82153; 2.
DR   PROSITE; PS50213; FAS1; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Proteoglycan; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..378
FT                   /note="Fasciclin-like arabinogalactan protein 2"
FT                   /id="PRO_0000251257"
FT   PROPEP          379..403
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000251258"
FT   DOMAIN          27..174
FT                   /note="FAS1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          187..326
FT                   /note="FAS1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   REGION          338..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           378
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        4
FT                   /note="L -> F (in Ref. 1; AAK20858 and 6; AAM65777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        369
FT                   /note="V -> G (in Ref. 6; AAM65777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388
FT                   /note="N -> S (in Ref. 1; AAK20858 and 6; AAM65777)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   403 AA;  43448 MW;  1F130E64DD5A7CAD CRC64;
     MAYLRRAATA LVLIFQLHLF LSLSNAHNIT RILAKDPDFS TFNHYLSATH LADEINRRQT
     ITVLAVDNSA MSSILSNGYS LYQIRNILSL HVLVDYFGTK KLHQITDGST STASMFQSTG
     SATGTSGYIN ITDIKGGKVA FGVQDDDSKL TAHYVKSVFE KPYNISVLHI SQVLTSPEAE
     APTASPSDLI LTTILEKQGC KAFSDILKST GADKTFQDTV DGGLTVFCPS DSAVGKFMPK
     FKSLSPANKT ALVLYHGMPV YQSLQMLRSG NGAVNTLATE GNNKFDFTVQ NDGEDVTLET
     DVVTAKVMGT LKDQEPLIVY KIDKVLLPRE IYKAVKTSAP APKSSKKKPK NAEADADGPS
     ADAPSDDDVE VADDKNGAVS AMITRTSNVV TAIVGLCFGV WLM
 
 
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