FTIP4_ARATH
ID FTIP4_ARATH Reviewed; 776 AA.
AC Q9C8H3; Q93VL4;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=FT-interacting protein 4 {ECO:0000303|PubMed:29742441};
DE AltName: Full=Multiple C2 domain and transmembrane region protein 4 {ECO:0000303|PubMed:29259105};
GN Name=FTIP4 {ECO:0000303|PubMed:29742441};
GN Synonyms=MCTP4 {ECO:0000303|PubMed:29259105};
GN OrderedLocusNames=At1g51570 {ECO:0000312|Araport:AT1G51570};
GN ORFNames=F19C24.20 {ECO:0000312|EMBL:AAG50882.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 466-776.
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH STM.
RC STRAIN=cv. Columbia;
RX PubMed=29742441; DOI=10.1016/j.celrep.2018.04.033;
RA Liu L., Li C., Song S., Teo Z.W.N., Shen L., Wang Y., Jackson D., Yu H.;
RT "FTIP-dependent STM trafficking regulates shoot meristem development in
RT Arabidopsis.";
RL Cell Rep. 23:1879-1890(2018).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=29259105; DOI=10.1104/pp.17.01144;
RA Liu L., Li C., Liang Z., Yu H.;
RT "Characterization of multiple C2 domain and transmembrane region proteins
RT in Arabidopsis.";
RL Plant Physiol. 176:2119-2132(2018).
CC -!- FUNCTION: Required for proliferation and differentiation of shoot stem
CC cells in the shoot apical meristem (SAM), thus determining the
CC appropriate balance between the maintenance of shoot stem cells and
CC their differentiation into other aboveground plant parts via the
CC control of subcellular localization and intercellular trafficking of
CC STM in the shoot apex. Prevents intracellular trafficking of STM to the
CC plasma membrane in cells in the peripheral shoot meristem region thus
CC facilitating STM recycling to the nucleus to maintain stem cells.
CC {ECO:0000269|PubMed:29742441}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with and regulates subcellular localization and
CC trafficking of STM. {ECO:0000269|PubMed:29742441}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9FL59}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29259105,
CC ECO:0000269|PubMed:29742441}. Vesicle {ECO:0000269|PubMed:29742441}.
CC Cell membrane {ECO:0000269|PubMed:29259105,
CC ECO:0000269|PubMed:29742441}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:29259105,
CC ECO:0000269|PubMed:29742441}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:29742441};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in both vegetative and
CC inflorescence shoot apical meristems (SAMs) (PubMed:29742441,
CC PubMed:29259105). Accumulates in root meristems (PubMed:29259105).
CC {ECO:0000269|PubMed:29259105, ECO:0000269|PubMed:29742441}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotypes. Plants lacking both FTIP3
CC and FTIP4 have a dwarf and bushy phenotype due to an accelerated stem
CC cell differentiation causing early termination of shoot apices
CC associated with an increased STM localization to the plasma membrane,
CC but compromises nuclear localization. {ECO:0000269|PubMed:29742441}.
CC -!- SIMILARITY: Belongs to the MCTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK74053.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC025294; AAG50882.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32684.1; -; Genomic_DNA.
DR EMBL; AY045695; AAK74053.1; ALT_INIT; mRNA.
DR EMBL; AY054155; AAL06816.1; -; mRNA.
DR PIR; C96554; C96554.
DR RefSeq; NP_175568.1; NM_104035.4.
DR AlphaFoldDB; Q9C8H3; -.
DR SMR; Q9C8H3; -.
DR STRING; 3702.AT1G51570.1; -.
DR MetOSite; Q9C8H3; -.
DR PaxDb; Q9C8H3; -.
DR PRIDE; Q9C8H3; -.
DR ProteomicsDB; 183067; -.
DR EnsemblPlants; AT1G51570.1; AT1G51570.1; AT1G51570.
DR GeneID; 841582; -.
DR Gramene; AT1G51570.1; AT1G51570.1; AT1G51570.
DR KEGG; ath:AT1G51570; -.
DR Araport; AT1G51570; -.
DR TAIR; locus:2017627; AT1G51570.
DR eggNOG; ENOG502R77N; Eukaryota.
DR HOGENOM; CLU_003762_1_0_1; -.
DR InParanoid; Q9C8H3; -.
DR OMA; CAVPLQY; -.
DR OrthoDB; 234298at2759; -.
DR PhylomeDB; Q9C8H3; -.
DR PRO; PR:Q9C8H3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8H3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IGI:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0031982; C:vesicle; IGI:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902182; P:shoot apical meristem development; IGI:TAIR.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR013583; PRibTrfase_C.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF08372; PRT_C; 1.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; SSF49562; 3.
DR PROSITE; PS50004; C2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Endoplasmic reticulum; Endosome;
KW Glycosyltransferase; Golgi apparatus; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..776
FT /note="FT-interacting protein 4"
FT /id="PRO_0000445998"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 22..142
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 181..305
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 346..474
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 776 AA; 89154 MW; CD03971D3FDE903D CRC64;
MQRPPPEDFS LKETKPHLGG GKVTGDKLTT TYDLVEQMQY LYVRVVKAKE LPGKDLTGSC
DPYVEVKLGN YRGTTRHFEK KSNPEWNQVF AFSKDRVQAS YLEATVKDKD LVKDDLIGRV
VFDLNEIPKR VPPDSPLAPQ WYRLEDGKGQ KVKGELMLAV WFGTQADEAF PEAWHSDAAT
VSGTDALANI RSKVYLSPKL WYLRVNVIEA QDLIPSDKGR YPEVFVKVIM GNQALRTRVS
QSRSINPMWN EDLMFVVAEP FEEPLILSVE DRVAPNKDEV LGRCAVPLQY LDKRFDYRPV
NSRWFNLEKH VIMEGGEKKE IKFASKIHMR ICLEGGYHVL DESTHYSSDL RPTAKQLWKP
NIGVLELGVL NATGLMPMKA KEGGRGTTDA YCVAKYGQKW IRTRTIIDSF TPRWNEQYTW
EVFDPCTVVT VGVFDNCHLH GGDKNNGGGK DSRIGKVRIR LSTLEADRVY THSYPLLVLH
PSGVKKMGEI HLAVRFTCSS LLNMMYMYSM PLLPKMHYLH PLTVSQLDNL RHQATQIVST
RLTRAEPPLR KEVVEYMLDV GSHMWSMRRS KANFFRIMGV LSGIIAVGKW FEQICVWKNP
ITTVLIHILF IILVIYPELI LPTIFLYLFL IGVWYYRWRP RHPPHMDTRL SHADSAHPDE
LDEEFDTFPT SRPSDIVRMR YDRLRSIAGR IQTVVGDLAT QGERFQSLLS WRDPRATALF
VLFCLIAAVI LYITPFQVVA FAIGLYVLRH PRLRYKLPSV PLNFFRRLPA RTDCML
