TDIF_ZINVI
ID TDIF_ZINVI Reviewed; 132 AA.
AC A1EC31;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein TDIF {ECO:0000303|PubMed:16902140};
DE AltName: Full=Tracheary element differentiation inhibitory factor {ECO:0000303|PubMed:16902140};
DE Contains:
DE RecName: Full=TDIFp {ECO:0000303|PubMed:16902140};
DE Flags: Precursor;
GN Name=TDIF {ECO:0000303|PubMed:16902140};
OS Zinnia violacea (Garden zinnia) (Zinnia elegans).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Zinnia.
OX NCBI_TaxID=34245;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 120-131, FUNCTION,
RP HYDROXYLATION AT PRO-123 AND PRO-126, MUTAGENESIS OF HIS-120; GLU-121;
RP VAL-122; SER-124; GLY-125; PRO-126; ASN-127; PRO-128; ILE-129; SER-130 AND
RP ASN-131, AND SUBCELLULAR LOCATION.
RX PubMed=16902140; DOI=10.1126/science.1128436;
RA Ito Y., Nakanomyo I., Motose H., Iwamoto K., Sawa S., Dohmae N., Fukuda H.;
RT "Dodeca-CLE peptides as suppressors of plant stem cell differentiation.";
RL Science 313:842-845(2006).
RN [2]
RP REVIEW.
RX PubMed=18034320; DOI=10.1007/s00018-007-7411-5;
RA Jun J.H., Fiume E., Fletcher J.C.;
RT "The CLE family of plant polypeptide signaling molecules.";
RL Cell. Mol. Life Sci. 65:743-755(2008).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF PRO-128.
RX PubMed=18812507; DOI=10.1073/pnas.0808444105;
RA Hirakawa Y., Shinohara H., Kondo Y., Inoue A., Nakanomyo I., Ogawa M.,
RA Sawa S., Ohashi-Ito K., Matsubayashi Y., Fukuda H.;
RT "Non-cell-autonomous control of vascular stem cell fate by a CLE
RT peptide/receptor system.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15208-15213(2008).
RN [4]
RP REVIEW.
RX PubMed=20016993; DOI=10.1007/s00709-009-0095-y;
RA Wang G., Fiers M.;
RT "CLE peptide signaling during plant development.";
RL Protoplasma 240:33-43(2010).
CC -!- FUNCTION: [TDIFp]: Extracellular signal peptide that regulates cell
CC fate. Represses tracheary element differentiation but promotes the
CC formation of procambial cells adjacent to phloem cells in the veins.
CC {ECO:0000269|PubMed:16902140, ECO:0000269|PubMed:18812507}.
CC -!- SUBUNIT: [TDIFp]: Interacts specifically with the leucine-rich repeat
CC receptor-like protein kinase TDR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [TDIFp]: Secreted, extracellular space
CC {ECO:0000269|PubMed:16902140}.
CC -!- SUBCELLULAR LOCATION: [CLAVATA3/ESR (CLE)-related protein TDIF]: Cell
CC membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- PTM: [TDIFp]: The TDIFp peptide contains two hydroxprolines, but
CC hydroxylation had no direct effect on TDIFp activity.
CC {ECO:0000269|PubMed:16902140}.
CC -!- PTM: [TDIFp]: The O-glycosylation (arabinosylation) of the
CC hydroxyproline Pro-126 enhances binding affinity of the TDIFp peptide
CC for its receptor. {ECO:0000250|UniProtKB:O49519}.
CC -!- SIMILARITY: Belongs to the CLV3/ESR signal peptide family.
CC {ECO:0000305}.
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DR EMBL; EF121243; ABL67522.1; -; mRNA.
DR AlphaFoldDB; A1EC31; -.
DR GO; GO:0048046; C:apoplast; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; ISS:UniProtKB.
DR GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; ISS:UniProtKB.
DR GO; GO:0010087; P:phloem or xylem histogenesis; ISS:UniProtKB.
DR GO; GO:0010067; P:procambium histogenesis; ISS:UniProtKB.
DR GO; GO:0010089; P:xylem development; ISS:UniProtKB.
DR InterPro; IPR037495; CLE41/42/44.
DR PANTHER; PTHR35301; PTHR35301; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Differentiation;
KW Direct protein sequencing; Glycoprotein; Hydroxylation; Membrane; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..132
FT /note="CLAVATA3/ESR (CLE)-related protein TDIF"
FT /id="PRO_0000401231"
FT PEPTIDE 120..131
FT /note="TDIFp"
FT /evidence="ECO:0000269|PubMed:16902140"
FT /id="PRO_0000401232"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 68..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:16902140"
FT MOD_RES 126
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:16902140"
FT CARBOHYD 126
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT MUTAGEN 120
FT /note="H->A: Impaired repression of tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 121
FT /note="E->A: No visible effect on tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 122
FT /note="V->A: Impaired repression of tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 124
FT /note="S->A: No visible effect on tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 125
FT /note="G->A: Impaired repression of tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 126
FT /note="P->A: No visible effect on tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 127
FT /note="N->A: Impaired repression of tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 128
FT /note="P->A: Impaired repression of tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140,
FT ECO:0000269|PubMed:18812507"
FT MUTAGEN 129
FT /note="I->A: No visible effect on tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 130
FT /note="S->A: No visible effect on tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
FT MUTAGEN 131
FT /note="N->A: Impaired repression of tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:16902140"
SQ SEQUENCE 132 AA; 14664 MW; 032D05FF8B0AEFDA CRC64;
MDIDLLWSFG GWFFILFPET INYCMAKLRS TSQISHFTNP RSCSSLFFVA LLIITILITM
LQSSTSMEVT SLPTHQPTSS NSHDESSTSS TATTTTDLHP KRTHHQSHPK PTRSFEAGAH
EVPSGPNPIS NR
