FLA13_ARATH
ID FLA13_ARATH Reviewed; 247 AA.
AC Q9FFH6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Fasciclin-like arabinogalactan protein 13;
DE Flags: Precursor;
GN Name=FLA13; OrderedLocusNames=At5g44130; ORFNames=MLN1_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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
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; AB005239; BAB10980.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95065.1; -; Genomic_DNA.
DR EMBL; AF083710; AAN60268.1; -; mRNA.
DR EMBL; AY058201; AAL25613.1; -; mRNA.
DR EMBL; AY098971; AAM19981.1; -; mRNA.
DR RefSeq; NP_199226.1; NM_123780.3.
DR AlphaFoldDB; Q9FFH6; -.
DR SMR; Q9FFH6; -.
DR STRING; 3702.AT5G44130.1; -.
DR PaxDb; Q9FFH6; -.
DR PRIDE; Q9FFH6; -.
DR ProteomicsDB; 228934; -.
DR EnsemblPlants; AT5G44130.1; AT5G44130.1; AT5G44130.
DR GeneID; 834436; -.
DR Gramene; AT5G44130.1; AT5G44130.1; AT5G44130.
DR KEGG; ath:AT5G44130; -.
DR Araport; AT5G44130; -.
DR TAIR; locus:2167664; AT5G44130.
DR eggNOG; ENOG502R770; Eukaryota.
DR HOGENOM; CLU_067693_1_0_1; -.
DR InParanoid; Q9FFH6; -.
DR OMA; GSGEMNT; -.
DR OrthoDB; 1402209at2759; -.
DR PhylomeDB; Q9FFH6; -.
DR PRO; PR:Q9FFH6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFH6; baseline and differential.
DR Genevisible; Q9FFH6; 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:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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 1: Evidence at protein 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 13"
FT /id="PRO_0000251261"
FT PROPEP 225..247
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251262"
FT DOMAIN 34..179
FT /note="FAS1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 189..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 224
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 247 AA; 26205 MW; 4D4BA68156BC3858 CRC64;
MATTPLLLLL LTAVFLSTEI TAQRAAPAPG PAGPINITAI LEKGGQFVTL IRLLNTTQIG
NQINIQINSS SEGMTVLAPT DNAFQNLKPG TLNKLSPDDQ VKLILYHVSP KFYTLEDLLS
VSNPVRTQAS GRDVGGVYGL NFTGQGNQVN VSTGVVETRL STSLRQERPL AVYVVDMVLL
PEEMFGERKI SPMAPPPKSK SPDVSDDSES SKKAAAPSES EKSGSGEMNT GLGLGLGLVV
LCLKFLL
