ID   FTIP1_ARATH             Reviewed;         794 AA.
AC   Q9FL59; Q93ZA2;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=FT-interacting protein 1 {ECO:0000303|PubMed:22529749};
GN   Name=FTIP1 {ECO:0000303|PubMed:22529749};
GN   OrderedLocusNames=At5g06850 {ECO:0000312|Araport:AT5G06850};
GN   ORFNames=MOJ9.2 {ECO:0000312|EMBL:BAB11143.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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 88-794.
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, LACK OF INDUCTION,
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH FT.
RX   PubMed=22529749; DOI=10.1371/journal.pbio.1001313;
RA   Liu L., Liu C., Hou X., Xi W., Shen L., Tao Z., Wang Y., Yu H.;
RT   "FTIP1 is an essential regulator required for florigen transport.";
RL   PLoS Biol. 10:E1001313-E1001313(2012).
RN   [5]
RP   INDUCTION BY APL/FE.
RX   PubMed=26239308; DOI=10.1111/tpj.12951;
RA   Abe M., Kaya H., Watanabe-Taneda A., Shibuta M., Yamaguchi A., Sakamoto T.,
RA   Kurata T., Ausin I., Araki T., Alonso-Blanco C.;
RT   "FE, a phloem-specific Myb-related protein, promotes flowering through
RT   transcriptional activation of FLOWERING LOCUS T and FLOWERING LOCUS T
RT   INTERACTING PROTEIN 1.";
RL   Plant J. 83:1059-1068(2015).
CC   -!- FUNCTION: Involved in the export of FT from the phloem companion cells
CC       to the sieve elements through the plasmodesmata. Regulates flowering
CC       time under long days. {ECO:0000269|PubMed:22529749}.
CC   -!- SUBUNIT: Interacts with FT in phloem companion cells.
CC       {ECO:0000269|PubMed:22529749}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22529749}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell junction, plasmodesma
CC       {ECO:0000269|PubMed:22529749}. Note=Localized in plasmodesmata between
CC       companion cells and sieve elements. {ECO:0000269|PubMed:22529749}.
CC   -!- TISSUE SPECIFICITY: Expressed in the vascular tissues of cotyledons and
CC       rosette leaves. Specifically located in the phloem including companion
CC       cells. Not detected in the shoot apical meristem.
CC       {ECO:0000269|PubMed:22529749}.
CC   -!- INDUCTION: Up-regulated by APL/FE (PubMed:26239308). Not regulated by
CC       photoperiod, circadian rhythm under long days, vernalization or
CC       gibberellin treatment (PubMed:22529749). {ECO:0000269|PubMed:22529749,
CC       ECO:0000269|PubMed:26239308}.
CC   -!- DISRUPTION PHENOTYPE: Late flowering under long days.
CC       {ECO:0000269|PubMed:22529749}.
CC   -!- MISCELLANEOUS: Unlike other flowering promoters, overexpression of
CC       FTIP1 causes late flowering due to the deregulation of FT transport out
CC       of the phloem system. {ECO:0000269|PubMed:22529749}.
CC   -!- SIMILARITY: Belongs to the MCTP family. {ECO:0000305}.
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DR   EMBL; AB010697; BAB11143.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91075.1; -; Genomic_DNA.
DR   EMBL; AY057690; AAL15320.1; -; mRNA.
DR   EMBL; AY133622; AAM91452.1; -; mRNA.
DR   RefSeq; NP_568175.2; NM_120768.3.
DR   AlphaFoldDB; Q9FL59; -.
DR   SMR; Q9FL59; -.
DR   STRING; 3702.AT5G06850.1; -.
DR   TCDB; 9.A.57.1.5; the extended-synaptotagmin (e-syt) family.
DR   PaxDb; Q9FL59; -.
DR   PRIDE; Q9FL59; -.
DR   ProteomicsDB; 230041; -.
DR   EnsemblPlants; AT5G06850.1; AT5G06850.1; AT5G06850.
DR   GeneID; 830576; -.
DR   Gramene; AT5G06850.1; AT5G06850.1; AT5G06850.
DR   KEGG; ath:AT5G06850; -.
DR   Araport; AT5G06850; -.
DR   TAIR; locus:2169379; AT5G06850.
DR   eggNOG; ENOG502QR9H; Eukaryota.
DR   HOGENOM; CLU_003762_1_0_1; -.
DR   InParanoid; Q9FL59; -.
DR   OMA; KNDSRIG; -.
DR   OrthoDB; 234298at2759; -.
DR   PhylomeDB; Q9FL59; -.
DR   PRO; PR:Q9FL59; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FL59; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0009511; C:plasmodesmatal endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0048574; P:long-day photoperiodism, flowering; IMP:TAIR.
DR   GO; GO:0009911; P:positive regulation of flower development; IMP:UniProtKB.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:UniProtKB.
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   Cell junction; Endoplasmic reticulum; Flowering; Membrane;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..794
FT                   /note="FT-interacting protein 1"
FT                   /id="PRO_0000436871"
FT   TRANSMEM        510..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        595..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        619..639
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        737..757
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..158
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          198..321
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          364..492
FT                   /note="C2 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  91003 MW;  3E0F79E6F2C4F2D9 CRC64;
     MAAKDGAKSQ EDYKLKDMKP ELGERWPHGG QRGGTGWIGS ERAASTYDLV EQMFYLYVRV
     VKAKDLPPNP VTSNCDPYVE VKIGNYKGKT KHFEKRTNPE WNQVFAFSKD KVQSSTVEVF
     VRDKEMVTRD EYIGKVVFDM REVPTRVPPD SPLAPQWYRL EDRRGESKKR GEVMVAVWLG
     TQADEAFPDA WHSDASSVQG EGVQSVRSKV YVSPKLWYLR VNVIEAQDVE PSDRSQPPQA
     FVKVQVGNQI LKTKLCPNKT TNPMWNEDLV FVAAEPFEEQ FFLTVENKVT PAKDEVMGRL
     ISPLSVFEKR LDHRAVHSKW YNLEKFGFGA LEGDKRHELK FSSRIHLRVC LEGGYHVMDE
     STLYISDVKP TARQLWKSPI GILEVGILSA QGLSPMKTKD GKATTDPYCV AKYGQKWVRT
     RTIIDSSSPK WNEQYTWEVY DPCTVITLGV FDNCHLGGSE KSNSGAKVDS RIGKVRIRLS
     TLEADRIYTH SYPLLVLQTK GLKKMGEVQL AVRFTCLSLA HMIYLYGHPL LPKMHYLHPF
     TVNQLDSLRY QAMSIVAARL SRAEPPLRKE NVEYMLDVDS HMWSMRRSKA NFFRIVSVFA
     GLIAMSKWLG DVCYWKNPLT TILFHVLFFI LICYPELILP TTFLYMFLIG LWNFRFRPRH
     PAHMDTKVSW AEAASPDELD EEFDTFPTSK GQDVVKMRYD RLRSVAGRIQ MVVGDIATQG
     ERFQALLSWR DPRATCLFVI FCLVAAMILY VTPFKIIALA GGMFWMRHPK FRSKMPSAPS
     NFFRKLPSKA DCML