FTIP7_ORYSJ
ID FTIP7_ORYSJ Reviewed; 774 AA.
AC Q60EW9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=FT-interacting protein 7 {ECO:0000303|PubMed:29915329};
DE Short=OsFTIP7 {ECO:0000303|PubMed:29915329};
GN Name=FTIP7 {ECO:0000303|PubMed:29915329};
GN OrderedLocusNames=Os05g0370600 {ECO:0000312|EMBL:BAF17265.1},
GN LOC_Os05g30750 {ECO:0000305};
GN ORFNames=OJ1118_F06.6 {ECO:0000312|EMBL:AAV31232.1},
GN OsJ_18293 {ECO:0000312|EMBL:EEE63479.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH OSH1, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=29915329; DOI=10.1038/s41477-018-0175-0;
RA Song S., Chen Y., Liu L., See Y.H.B., Mao C., Gan Y., Yu H.;
RT "OsFTIP7 determines auxin-mediated anther dehiscence in rice.";
RL Nat. Plants 4:495-504(2018).
CC -!- FUNCTION: Promotes nuclear translocation of the transcription factor
CC OSH1, which directly suppresses the auxin biosynthetic gene YUCCA4
CC during the late development of anthers (PubMed:29915329). Reduction of
CC auxin levels at late stage of anther development, after meiosis of
CC microspore mother cells, is necessary for normal anther dehiscence and
CC seed setting (PubMed:29915329). Required for jasmonate (JA)
CC biosynthetic genes expression and JA production in anthers
CC (PubMed:29915329). {ECO:0000269|PubMed:29915329}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with OSH1. {ECO:0000269|PubMed:29915329}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29915329};
CC Multi-pass membrane protein {ECO:0000255}. Note=May be associated with
CC the endoplasmic reticulum membrane in the close vicinity of the plasma
CC membrane. {ECO:0000305|PubMed:29915329}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, lemma, palea, pistils
CC and ovules (PubMed:29915329). Expressed at low levels in leaves
CC (PubMed:29915329). {ECO:0000269|PubMed:29915329}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in developing anthers before
CC pollen mitotic divisions from stage 8 to stage 12, with a peak of
CC expression at stage 9 (at protein level) (PubMed:29915329). Expressed
CC in developing seeds from 3 to 10 days after flowering (at protein
CC level) (PubMed:29915329). {ECO:0000269|PubMed:29915329}.
CC -!- DISRUPTION PHENOTYPE: Male sterility due to defect in anther dehiscence
CC and mature pollen grain release at anthesis.
CC {ECO:0000269|PubMed:29915329}.
CC -!- SIMILARITY: Belongs to the MCTP family. {ECO:0000305}.
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DR EMBL; AC104707; AAV31232.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17265.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS93680.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE63479.1; -; Genomic_DNA.
DR RefSeq; XP_015640336.1; XM_015784850.1.
DR RefSeq; XP_015640337.1; XM_015784851.1.
DR RefSeq; XP_015640338.1; XM_015784852.1.
DR RefSeq; XP_015640339.1; XM_015784853.1.
DR RefSeq; XP_015640340.1; XM_015784854.1.
DR AlphaFoldDB; Q60EW9; -.
DR SMR; Q60EW9; -.
DR STRING; 4530.OS05T0370600-01; -.
DR PaxDb; Q60EW9; -.
DR PRIDE; Q60EW9; -.
DR EnsemblPlants; Os05t0370600-01; Os05t0370600-01; Os05g0370600.
DR EnsemblPlants; Os05t0370600-02; Os05t0370600-02; Os05g0370600.
DR GeneID; 4338582; -.
DR Gramene; Os05t0370600-01; Os05t0370600-01; Os05g0370600.
DR Gramene; Os05t0370600-02; Os05t0370600-02; Os05g0370600.
DR KEGG; osa:4338582; -.
DR eggNOG; ENOG502R77N; Eukaryota.
DR HOGENOM; CLU_003762_1_0_1; -.
DR InParanoid; Q60EW9; -.
DR OMA; DCGPTLE; -.
DR OrthoDB; 234298at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009901; P:anther dehiscence; IMP:UniProtKB.
DR GO; GO:0010930; P:negative regulation of auxin mediated signaling pathway; IDA: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 Calcium; Cell membrane; Membrane; Metal-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..774
FT /note="FT-interacting protein 7"
FT /id="PRO_0000445340"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 23..143
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 182..305
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 346..472
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 774 AA; 89345 MW; E28E278C95760E95 CRC64;
MMQRPFRPEE YSLKETSPHL GGGAAGDKLT TTYDLVEQMQ YLYVRVVKAK DLPSKDITGS
CDPYVEVKLG NYKGTTRHFE KKTNPEWNQV FAFSKERIQS SVVEIIVKDK DFVKDDFIGR
VLFDLNEVPK RVPPDSPLAP QWYRLEERNG HKVKGELMLA VWMGTQADEA FPEAWHSDAA
SIPGDGLASI RSKVYLTPKL WYLRVNVIEA QDLIPNDRTR FPDVYVKAML GNQALRTRVS
PSRTLNPMWN EDLMFVAAEP FEEHLILSVE DRIAPGKDDV LGRTIISLQH VPRRLDHKLL
NSQWYNLEKH VIVDGEQKKE TKFSSRIHLR ICLEGGYHVL DESTHYSSDL RPTAKQLWKH
SIGILELGIL TAQGLLPMKT KDGRGTTDAY CVAKYGQKWV RTRTIIDSFT PKWNEQYTWE
VYDPCTVITI GVFDNCHLNG GEKANGARDT RIGKVRIRLS TLETDRVYTH AYPLIVLTPA
GVKKMGEVQL AVRFTCSSLL NMMHLYSQPL LPKMHYVHPL SVMQVDNLRR QATNIVSTRL
SRAEPPLRKE IVEYMLDVDS HMWSMRKSKA NFFRIMGVLS PLIAVAKWFD QICHWRNPLT
TILIHILFVI LVLYPELILP TIFLYLFLIG VWYYRWRPRQ PPHMDTRLSH AESAHPDELD
EEFDTFPTSR PPDIVRMRYD RLRSVAGRIQ TVVGDLATQG ERLQSLLSWR DPRATALFVT
FCFVAAIVLY VTPFRVVVFL AGLYTLRHPR FRHKMPSVPL NFFRRLPART DSML
