FTIP3_ARATH
ID FTIP3_ARATH Reviewed; 773 AA.
AC Q9M2R0; A0A178VJU5; Q0TV71; Q94JQ8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=FT-interacting protein 3 {ECO:0000303|PubMed:29742441};
DE AltName: Full=Multiple C2 domain and transmembrane region protein 3 {ECO:0000303|PubMed:29259105};
GN Name=FTIP3 {ECO:0000303|PubMed:29742441};
GN Synonyms=MCTP3 {ECO:0000303|PubMed:29259105};
GN OrderedLocusNames=At3g57880 {ECO:0000312|Araport:AT3G57880};
GN ORFNames=T10K17.90 {ECO:0000312|EMBL:CAB67616.1};
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=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 [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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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:0000250|UniProtKB:Q9C8H3}.
CC Cell membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane
CC protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:29259105};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9C8H3}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Accumulates in vascular tissues, leaf primordia and
CC developing flowers (PubMed:29259105). Highly expressed in both
CC vegetative and inflorescence shoot apical meristems (SAMs)
CC (PubMed:29742441, PubMed:29259105). {ECO:0000269|PubMed:29259105,
CC 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}.
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DR EMBL; AL132977; CAB67616.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79712.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65757.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65758.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65759.1; -; Genomic_DNA.
DR EMBL; AF375436; AAK53020.1; -; mRNA.
DR EMBL; AY120689; AAM52232.1; -; mRNA.
DR EMBL; AK229856; BAF01685.1; -; mRNA.
DR PIR; T46010; T46010.
DR RefSeq; NP_001327704.1; NM_001339898.1.
DR RefSeq; NP_001327705.1; NM_001339896.1.
DR RefSeq; NP_001327706.1; NM_001339897.1.
DR RefSeq; NP_191347.1; NM_115650.5.
DR AlphaFoldDB; Q9M2R0; -.
DR SMR; Q9M2R0; -.
DR IntAct; Q9M2R0; 3.
DR STRING; 3702.AT3G57880.1; -.
DR PaxDb; Q9M2R0; -.
DR PRIDE; Q9M2R0; -.
DR ProteomicsDB; 189223; -.
DR EnsemblPlants; AT3G57880.1; AT3G57880.1; AT3G57880.
DR EnsemblPlants; AT3G57880.2; AT3G57880.2; AT3G57880.
DR EnsemblPlants; AT3G57880.3; AT3G57880.3; AT3G57880.
DR EnsemblPlants; AT3G57880.4; AT3G57880.4; AT3G57880.
DR GeneID; 824957; -.
DR Gramene; AT3G57880.1; AT3G57880.1; AT3G57880.
DR Gramene; AT3G57880.2; AT3G57880.2; AT3G57880.
DR Gramene; AT3G57880.3; AT3G57880.3; AT3G57880.
DR Gramene; AT3G57880.4; AT3G57880.4; AT3G57880.
DR KEGG; ath:AT3G57880; -.
DR Araport; AT3G57880; -.
DR TAIR; locus:2095853; AT3G57880.
DR eggNOG; ENOG502R77N; Eukaryota.
DR HOGENOM; CLU_003762_1_0_1; -.
DR InParanoid; Q9M2R0; -.
DR OMA; DCGPTLE; -.
DR OrthoDB; 234298at2759; -.
DR PhylomeDB; Q9M2R0; -.
DR PRO; PR:Q9M2R0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2R0; 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; HDA: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..773
FT /note="FT-interacting protein 3"
FT /id="PRO_0000445997"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
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 345..471
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..24
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"
FT CONFLICT 280
FT /note="V -> A (in Ref. 4; BAF01685)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="R -> Q (in Ref. 3; AAK53020/AAM52232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 89193 MW; B70E9DC1774A36F8 CRC64;
MQRPPPEDFS LKETRPHLGG GKLSGDKLTS TYDLVEQMQY LYVRVVKAKE LPGKDMTGSC
DPYVEVKLGN YKGTTRHFEK KSNPEWNQVF AFSKDRIQAS FLEATVKDKD FVKDDLIGRV
VFDLNEVPKR VPPDSPLAPQ WYRLEDRKGD KVKGELMLAV WFGTQADEAF PEAWHSDAAT
VSGTDALANI RSKVYLSPKL WYLRVNVIEA QDLIPTDKQR YPEVYVKAIV GNQALRTRVS
QSRTINPMWN EDLMFVAAEP FEEPLILSVE DRVAPNKDEV LGRCAIPLQY LDRRFDHKPV
NSRWYNLEKH IMVDGEKKET KFASRIHMRI CLEGGYHVLD ESTHYSSDLR PTAKQLWKPN
IGVLELGILN ATGLMPMKTK DGRGTTDAYC VAKYGQKWIR TRTIIDSFTP RWNEQYTWEV
FDPCTVVTVG VFDNCHLHGG EKIGGAKDSR IGKVRIRLST LETDRVYTHS YPLLVLHPNG
VKKMGEIHLA VRFTCSSLLN MMYMYSQPLL PKMHYIHPLT VSQLDNLRHQ ATQIVSMRLT
RAEPPLRKEV VEYMLDVGSH MWSMRRSKAN FFRIMGVLSG LIAVGKWFEQ ICNWKNPITT
VLIHLLFIIL VLYPELILPT IFLYLFLIGI WYYRWRPRHP PHMDTRLSHA DSAHPDELDE
EFDTFPTSRP SDIVRMRYDR LRSIAGRIQT VVGDLATQGE RLQSLLSWRD PRATALFVLF
CLIAAVILYV TPFQVVALCI GIYALRHPRF RYKLPSVPLN FFRRLPARTD CML
