FLA1_ARATH
ID FLA1_ARATH Reviewed; 424 AA.
AC Q9FM65; Q8L8T1;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Fasciclin-like arabinogalactan protein 1;
DE Flags: Precursor;
GN Name=FLA1; OrderedLocusNames=At5g55730; ORFNames=MDF20.17;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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] OF 232-424.
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 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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=15593128; DOI=10.1002/pmic.200400882;
RA Boudart G., Jamet E., Rossignol M., Lafitte C., Borderies G., Jauneau A.,
RA Esquerre-Tugaye M.-T., Pont-Lezica R.;
RT "Cell wall proteins in apoplastic fluids of Arabidopsis thaliana rosettes:
RT identification by mass spectrometry and bioinformatics.";
RL Proteomics 5:212-221(2005).
CC -!- FUNCTION: May be a cell surface adhesion protein.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:15593128}. Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in flowers.
CC {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; AF333970; AAK20857.1; -; mRNA.
DR EMBL; AB009050; BAB09240.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96673.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96674.1; -; Genomic_DNA.
DR EMBL; BT002537; AAO00897.1; -; mRNA.
DR EMBL; BT008510; AAP37869.1; -; mRNA.
DR EMBL; AY088827; AAM67371.1; -; mRNA.
DR RefSeq; NP_001190550.1; NM_001203621.1.
DR RefSeq; NP_200384.1; NM_124955.4.
DR AlphaFoldDB; Q9FM65; -.
DR SMR; Q9FM65; -.
DR STRING; 3702.AT5G55730.1; -.
DR iPTMnet; Q9FM65; -.
DR SwissPalm; Q9FM65; -.
DR PaxDb; Q9FM65; -.
DR PRIDE; Q9FM65; -.
DR ProteomicsDB; 230602; -.
DR EnsemblPlants; AT5G55730.1; AT5G55730.1; AT5G55730.
DR EnsemblPlants; AT5G55730.2; AT5G55730.2; AT5G55730.
DR GeneID; 835667; -.
DR Gramene; AT5G55730.1; AT5G55730.1; AT5G55730.
DR Gramene; AT5G55730.2; AT5G55730.2; AT5G55730.
DR KEGG; ath:AT5G55730; -.
DR Araport; AT5G55730; -.
DR TAIR; locus:2162197; AT5G55730.
DR eggNOG; ENOG502QR33; Eukaryota.
DR HOGENOM; CLU_036139_0_1_1; -.
DR InParanoid; Q9FM65; -.
DR OMA; VQNDGQE; -.
DR OrthoDB; 984651at2759; -.
DR PhylomeDB; Q9FM65; -.
DR PRO; PR:Q9FM65; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM65; baseline and differential.
DR Genevisible; Q9FM65; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP: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 1: Evidence at protein level;
KW Apoplast; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..396
FT /note="Fasciclin-like arabinogalactan protein 1"
FT /id="PRO_0000008776"
FT PROPEP 397..424
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008777"
FT DOMAIN 25..170
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 184..323
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 338..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 396
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 424 AA; 44849 MW; 6B256D3CE592881B CRC64;
MAKKMSSLII IFNILLLLTT QTHAHNVTRL LANHPSFSSF SHFLTQTHLA DEINRRRTIT
VCAVDNAAMS ALTSKGYTLS TLKNILSLHV LLDYFGTKKL HQIRDGSALA ATLFQATGAA
PGTSGFVNIT DLRGGKVGFG PDGGDLSSFF VKSIEEVPYN ISIIQISRVL PSETAAAPTP
APAEMNLTGI MSAHGCKVFA ETLLTNPGAS KTYQESLEGG MTVFCPGDDA MKGFLPKYKN
LTAPKKEAFL DFLAVPTYYS MAMLKSNNGP MNTLATDGAN KFELTVQNDG EKVTLKTRIN
TVKIVDTLID EQPLAIYATD KVLLPKELFK ASAVEAPAPA PAPEDGDVAD SPKAAKGKAK
GKKKKAAPSP DNDPFGDSDS PAEGPDGEAD DATADDAGAV RIIGGAKAGL VVSLLCLFAS
SWLL
