ID A0A1S4CSS1_TOBAC Unreviewed; 258 AA.
AC A0A1S4CSS1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Classical arabinogalactan protein 9-like {ECO:0000313|RefSeq:XP_016504069.1};
GN Name=LOC107822086 {ECO:0000313|RefSeq:XP_016504069.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016504069.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016504069.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
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DR RefSeq; XP_016504069.1; XM_016648583.1.
DR AlphaFoldDB; A0A1S4CSS1; -.
DR STRING; 4097.A0A1S4CSS1; -.
DR PaxDb; 4097-A0A1S4CSS1; -.
DR GeneID; 107822086; -.
DR KEGG; nta:107822086; -.
DR OrthoDB; 471472at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR CDD; cd00010; AAI_LTSS; 1.
DR Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR043325; LTSS.
DR PANTHER; PTHR33044; BIFUNCTIONAL INHIBITOR/LIPID-TRANSFER PROTEIN/SEED STORAGE 2S ALBUMIN SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR33044:SF142; NON-SPECIFIC LIPID TRANSFER PROTEIN GPI-ANCHORED 16; 1.
DR Pfam; PF14368; LTP_2; 1.
DR SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..258
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010373785"
FT TRANSMEM 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..110
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|Pfam:PF14368"
FT REGION 123..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 258 AA; 26760 MW; 4656536F21E184EB CRC64;
MEILKVSASA HVLFLTLLTF SAFKMLNGQI NTACTSSIFS TFTPCFNYLT GSSGNGSSPT
EDCCNSLKSS MSDSIDCVCL MVTGNVPVSI PFIRTLALSL PQACNTGVPV QCSASGVPLP
PPGPALFAPP PAPAPHHHHA PAYPPRHHRA AAFPPALAPR SQRVAKASAA PTAEVDPPVA
APTIEGPEAT ADTEKPTTSP PKSSLVPNTT PAGTRPVLQN PNTSTSAAIP SYSISSSLQS
LTLIFIAVII LFIDKSMY
//
