FLA9_ARATH
ID FLA9_ARATH Reviewed; 247 AA.
AC Q9ZWA8; Q8H794;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Fasciclin-like arabinogalactan protein 9;
DE Flags: Precursor;
GN Name=FLA9; OrderedLocusNames=At1g03870; ORFNames=F21M11.20;
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=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].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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 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 [7]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
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; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the fasciclin-like AGP family. {ECO:0000305}.
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DR EMBL; AF333974; AAK20861.1; -; mRNA.
DR EMBL; AC003027; AAD10681.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27627.1; -; Genomic_DNA.
DR EMBL; AF083781; AAN60339.1; -; mRNA.
DR EMBL; AY087938; AAM65486.1; -; mRNA.
DR EMBL; AK227010; BAE99074.1; -; mRNA.
DR PIR; D86169; D86169.
DR RefSeq; NP_563692.1; NM_100267.4.
DR AlphaFoldDB; Q9ZWA8; -.
DR SMR; Q9ZWA8; -.
DR BioGRID; 24619; 2.
DR STRING; 3702.AT1G03870.1; -.
DR PaxDb; Q9ZWA8; -.
DR PRIDE; Q9ZWA8; -.
DR ProteomicsDB; 230601; -.
DR EnsemblPlants; AT1G03870.1; AT1G03870.1; AT1G03870.
DR GeneID; 839384; -.
DR Gramene; AT1G03870.1; AT1G03870.1; AT1G03870.
DR KEGG; ath:AT1G03870; -.
DR Araport; AT1G03870; -.
DR TAIR; locus:2024122; AT1G03870.
DR eggNOG; ENOG502R770; Eukaryota.
DR HOGENOM; CLU_067693_1_0_1; -.
DR InParanoid; Q9ZWA8; -.
DR OMA; TMFMRLM; -.
DR OrthoDB; 1402209at2759; -.
DR PhylomeDB; Q9ZWA8; -.
DR PRO; PR:Q9ZWA8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZWA8; baseline and differential.
DR Genevisible; Q9ZWA8; 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:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IBA:GO_Central.
DR Gene3D; 2.30.180.10; -; 1.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR045003; FLA_A.
DR PANTHER; PTHR32077; PTHR32077; 1.
DR Pfam; PF02469; Fasciclin; 1.
DR SMART; SM00554; FAS1; 1.
DR SUPFAM; SSF82153; SSF82153; 1.
DR PROSITE; PS50213; FAS1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Proteoglycan; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..224
FT /note="Fasciclin-like arabinogalactan protein 9"
FT /id="PRO_0000251259"
FT PROPEP 225..247
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251260"
FT DOMAIN 37..181
FT /note="FAS1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 193..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 224
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 31
FT /note="A -> T (in Ref. 4; AAN60339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 26115 MW; 23C97E6F4E1BE874 CRC64;
MATTRLTLAP LLLIAAVLLA TKATAQPAAP APEPAGPINL TAILEKGGQF TTFIHLLNIT
QVGSQVNIQV NSSSEGMTVF APTDNAFQNL KPGTLNQLSP DDQVKLILYH VSPKYYSMDD
LLSVSNPVRT QASGRDNGVY GLNFTGQTNQ INVSTGYVET RISNSLRQQR PLAVYVVDMV
LLPGEMFGEH KLSPIAPAPK SKSGGVTDDS GSTKKAASPS DKSGSGEKKV GLGFGLGLIV
LCLKFLF
