FLA4_ARATH
ID FLA4_ARATH Reviewed; 420 AA.
AC Q9SNC3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Fasciclin-like arabinogalactan protein 4;
DE AltName: Full=Protein SALT OVERLY SENSITIVE 5;
DE Flags: Precursor;
GN Name=FLA4; Synonyms=SOS5; OrderedLocusNames=At3g46550; ORFNames=F12A12.70;
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], MUTAGENESIS OF SER-348, INDUCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12509519; DOI=10.1105/tpc.007872;
RA Shi H., Kim Y., Guo Y., Stevenson B., Zhu J.-K.;
RT "The Arabidopsis SOS5 locus encodes a putative cell surface adhesion
RT protein and is required for normal cell expansion.";
RL Plant Cell 15:19-32(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 that is required for
CC normal cell expansion.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12509519};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12509519}.
CC -!- TISSUE SPECIFICITY: Expressed in all plant organs and tissues,
CC including guard cells in the leaf. {ECO:0000269|PubMed:12509519}.
CC -!- INDUCTION: Up-regulated by abscisic acid, cold and drought treatments,
CC but not by high salt. {ECO:0000269|PubMed:12509519}.
CC -!- SIMILARITY: Belongs to the fasciclin-like AGP family. {ECO:0000305}.
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DR EMBL; AL133314; CAB62325.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78171.1; -; Genomic_DNA.
DR PIR; T45592; T45592.
DR RefSeq; NP_190239.1; NM_114522.4.
DR AlphaFoldDB; Q9SNC3; -.
DR SMR; Q9SNC3; -.
DR BioGRID; 9128; 1.
DR STRING; 3702.AT3G46550.1; -.
DR PaxDb; Q9SNC3; -.
DR PRIDE; Q9SNC3; -.
DR ProteomicsDB; 230520; -.
DR EnsemblPlants; AT3G46550.1; AT3G46550.1; AT3G46550.
DR GeneID; 823808; -.
DR Gramene; AT3G46550.1; AT3G46550.1; AT3G46550.
DR KEGG; ath:AT3G46550; -.
DR Araport; AT3G46550; -.
DR TAIR; locus:2075185; AT3G46550.
DR eggNOG; ENOG502QVC9; Eukaryota.
DR HOGENOM; CLU_036139_3_0_1; -.
DR InParanoid; Q9SNC3; -.
DR OMA; GIFLWCI; -.
DR OrthoDB; 984651at2759; -.
DR PhylomeDB; Q9SNC3; -.
DR PRO; PR:Q9SNC3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SNC3; baseline and differential.
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:0009897; C:external side of plasma membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0030247; F:polysaccharide binding; TAS:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IGI:TAIR.
DR GO; GO:0007155; P:cell adhesion; ISS:TAIR.
DR GO; GO:0010192; P:mucilage biosynthetic process; IMP:TAIR.
DR GO; GO:0048354; P:mucilage biosynthetic process involved in seed coat development; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; 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 Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Proteoglycan; Reference proteome; Repeat; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..396
FT /note="Fasciclin-like arabinogalactan protein 4"
FT /id="PRO_0000251263"
FT PROPEP 397..420
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251264"
FT DOMAIN 29..177
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 205..351
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 360..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 396
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 348
FT /note="S->F: Alters the cell wall structure."
FT /evidence="ECO:0000269|PubMed:12509519"
SQ SEQUENCE 420 AA; 44239 MW; 449C626DA86A3A57 CRC64;
MANVISISHF TLLALPYLLL LLSSTAAAIN VTAVLSSFPN LSSFSNLLVS SGIAAELSGR
NSLTLLAVPN SQFSSASLDL TRRLPPSALA DLLRFHVLLQ FLSDSDLRRI PPSGSAVTTL
YEASGRTFFG SGSVNVTRDP ASGSVTIGSP ATKNVTVLKL LETKPPNITV LTVDSLIVPT
GIDITASETL TPPPTSTSLS PPPAGINLTQ ILINGHNFNV ALSLLVASGV ITEFENDERG
AGITVFVPTD SAFSDLPSNV NLQSLPAEQK AFVLKFHVLH SYYTLGSLES ITNPVQPTLA
TEEMGAGSYT LNISRVNGSI VTINSGVVLA VVTQTAFDQN PVSVFGVSKV LLPKELFPKS
GQPVATAPPQ EISLSPESSS EQPSRLVSPP REIVSSGAVK RPLGFLVLWC WCIAFCYVLV
