FLA7_ARATH
ID FLA7_ARATH Reviewed; 254 AA.
AC Q9SJ81; Q8LG01;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Fasciclin-like arabinogalactan protein 7;
DE Flags: Precursor;
GN Name=FLA7; OrderedLocusNames=At2g04780; ORFNames=F28I8.18;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 TISSUE=Leaf;
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].
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 [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, 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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF333973; AAK20860.1; -; mRNA.
DR EMBL; AC006955; AAD22328.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05861.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05862.1; -; Genomic_DNA.
DR EMBL; AF083754; AAN60312.1; -; mRNA.
DR EMBL; AY094449; AAM19820.1; -; mRNA.
DR EMBL; BT001123; AAN64514.1; -; mRNA.
DR EMBL; AY084541; AAM61109.1; ALT_INIT; mRNA.
DR PIR; D84461; D84461.
DR RefSeq; NP_565313.1; NM_126508.5.
DR RefSeq; NP_849935.1; NM_179604.2.
DR AlphaFoldDB; Q9SJ81; -.
DR SMR; Q9SJ81; -.
DR BioGRID; 422; 2.
DR STRING; 3702.AT2G04780.2; -.
DR PaxDb; Q9SJ81; -.
DR PRIDE; Q9SJ81; -.
DR ProteomicsDB; 230950; -.
DR EnsemblPlants; AT2G04780.1; AT2G04780.1; AT2G04780.
DR EnsemblPlants; AT2G04780.2; AT2G04780.2; AT2G04780.
DR GeneID; 815021; -.
DR Gramene; AT2G04780.1; AT2G04780.1; AT2G04780.
DR Gramene; AT2G04780.2; AT2G04780.2; AT2G04780.
DR KEGG; ath:AT2G04780; -.
DR Araport; AT2G04780; -.
DR TAIR; locus:2049218; AT2G04780.
DR eggNOG; ENOG502QV96; Eukaryota.
DR HOGENOM; CLU_067693_2_0_1; -.
DR InParanoid; Q9SJ81; -.
DR OMA; MEFSRIF; -.
DR OrthoDB; 1348986at2759; -.
DR PhylomeDB; Q9SJ81; -.
DR PRO; PR:Q9SJ81; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ81; baseline and differential.
DR Genevisible; Q9SJ81; 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:0005739; C:mitochondrion; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..232
FT /note="Fasciclin-like arabinogalactan protein 7"
FT /id="PRO_0000008778"
FT PROPEP 233..254
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008779"
FT DOMAIN 44..186
FT /note="FAS1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 203..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 232
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 182
FT /note="V -> L (in Ref. 6; AAM61109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 26846 MW; C671DF59CDE5AF8F CRC64;
MAKMQLSIFI AVVALIVCSA SAKTASPPAP VLPPTPAPAP APENVNLTEL LSVAGPFHTF
LDYLLSTGVI ETFQNQANNT EEGITIFVPK DDAFKAQKNP PLSNLTKDQL KQLVLFHALP
HYYSLSEFKN LSQSGPVSTF AGGQYSLKFT DVSGTVRIDS LWTRTKVSSS VFSTDPVAVY
QVNRVLLPEA IFGTDVPPMP APAPAPIVSA PSDSPSVADS EGASSPKSSH KNSGQKLLLA
PISMVISGLV ALFL
