ID PHF1_ARATH Reviewed; 398 AA.
AC Q8GYE0; Q9SUY6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=SEC12-like protein 1;
DE AltName: Full=Protein PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR 1;
DE Short=PHF-1;
GN Name=PHF1; OrderedLocusNames=At3g52190; ORFNames=F4F15.300;
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] OF 14-398.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16284308; DOI=10.1105/tpc.105.036640;
RA Gonzalez E., Solano R., Rubio V., Leyva A., Paz-Ares J.;
RT "PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 is a plant-specific SEC12-
RT related protein that enables the endoplasmic reticulum exit of a high-
RT affinity phosphate transporter in Arabidopsis.";
RL Plant Cell 17:3500-3512(2005).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in Pi uptake by facilitating the trafficking of
CC PHT1-1/PHT1;1 from the endoplasmic reticulum to the plasma membrane.
CC {ECO:0000269|PubMed:16284308}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16284308}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16284308}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher levels in flowers, roots and
CC senescing leaves. {ECO:0000269|PubMed:16284308}.
CC -!- INDUCTION: By Pi starvation. {ECO:0000269|PubMed:16284308}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42349.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL049711; CAB41339.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78911.1; -; Genomic_DNA.
DR EMBL; AK117697; BAC42349.1; ALT_INIT; mRNA.
DR PIR; T49098; T49098.
DR RefSeq; NP_566961.1; NM_115079.4.
DR AlphaFoldDB; Q8GYE0; -.
DR SMR; Q8GYE0; -.
DR BioGRID; 9702; 10.
DR IntAct; Q8GYE0; 10.
DR STRING; 3702.Q8GYE0; -.
DR iPTMnet; Q8GYE0; -.
DR PaxDb; 3702-AT3G52190-1; -.
DR ProteomicsDB; 236728; -.
DR EnsemblPlants; AT3G52190.1; AT3G52190.1; AT3G52190.
DR GeneID; 824384; -.
DR Gramene; AT3G52190.1; AT3G52190.1; AT3G52190.
DR KEGG; ath:AT3G52190; -.
DR Araport; AT3G52190; -.
DR TAIR; AT3G52190; PHF1.
DR eggNOG; KOG0771; Eukaryota.
DR HOGENOM; CLU_058136_1_1_1; -.
DR InParanoid; Q8GYE0; -.
DR OMA; PMGRHQP; -.
DR OrthoDB; 315463at2759; -.
DR PhylomeDB; Q8GYE0; -.
DR PRO; PR:Q8GYE0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GYE0; baseline and differential.
DR Genevisible; Q8GYE0; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:TAIR.
DR GO; GO:0006817; P:phosphate ion transport; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR045260; Sec12-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR23284; PROLACTIN REGULATORY ELEMENT BINDING PROTEIN; 1.
DR PANTHER; PTHR23284:SF2; SEC12-LIKE PROTEIN 1; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Membrane; Protein transport;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport; WD repeat.
FT CHAIN 1..398
FT /note="SEC12-like protein 1"
FT /id="PRO_0000051123"
FT TOPO_DOM 1..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 71..110
FT /note="WD 1"
FT REPEAT 120..159
FT /note="WD 2"
FT REPEAT 162..201
FT /note="WD 3"
FT REPEAT 252..291
FT /note="WD 4"
FT REPEAT 296..334
FT /note="WD 5"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 398 AA; 43767 MW; 687F04E70EA90728 CRC64;
MEIEEASRES GHVVCGSWIR RPKKVNWVLI AKASKRRGSS VSSPALLNIF SFDPITASLS
SSPLATHTLK DSDGDPVAVS VHPGGDYFVC STSKGGCKLF ELVGGATGIT ILAKELLPLQ
NAGLQKCMAF SFDGSKLAVG GVDGCLRIME WPNLSVILDE PKAHKSIRDM DFSLDSEFLA
TTSTDGSARI WKAEDGFPLS TLERSGDENI ELCRFSKDGT KPFLFCAAQR GDTPMVNVYD
ISTWKKLGFK KLSRKTASTM AVSLDGKYIA LGGKDGDVSV AEVKTMEIYH YSKRLHLGQS
IASLEFCPSE RVMLTTSSEW GEMVTKLTVP KEWKEWQIYA LLFCLFMASV IAAYVFFENS
DSFWKLPMGK DQKRPKISLF GGSSSTPSED HSRWNLDL
//
