PHIP1_ARATH
ID PHIP1_ARATH Reviewed; 597 AA.
AC Q9M3B8; A0A178VII4; Q681R8; Q8W2K5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Phragmoplastin interacting protein 1 {ECO:0000303|PubMed:18621982};
GN Name=PHIP1 {ECO:0000303|PubMed:18621982};
GN OrderedLocusNames=At3g55340 {ECO:0000312|Araport:AT3G55340};
GN ORFNames=T26I12.220 {ECO:0000312|EMBL:CAB75768.1};
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 [MRNA], FUNCTION, INTERACTION WITH PHRAGMOPLASTINS;
RP RAN2 AND ARAC11/ROP1, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18621982; DOI=10.1104/pp.108.120527;
RA Ma L., Xie B., Hong Z., Verma D.P.S., Zhang Z.;
RT "A novel RNA-binding protein associated with cell plate formation.";
RL Plant Physiol. 148:223-234(2008).
RN [2]
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 [3]
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 [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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein which mediates polarized mRNA (e.g. Ran2
CC transcripts mRNA) transport from the nucleus to the vicinity of the
CC cell plate during cytokinesis and phragmoplast formation.
CC {ECO:0000269|PubMed:18621982}.
CC -!- SUBUNIT: Interacts with phragmoplastins (e.g. DRP1A, DRP1B, DRP1C,
CC DRP1D and DRP1E) and with GTP-bound ARAC11/ROP1 as well as with Ran2
CC transcripts. {ECO:0000269|PubMed:18621982}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Cell membrane {ECO:0000269|PubMed:18621982}; Peripheral membrane
CC protein {ECO:0000269|PubMed:18621982}. Cytoplasm, cytoskeleton,
CC phragmoplast {ECO:0000269|PubMed:18621982}. Note=Associates with the
CC forming cell plate during cytokinesis; may shuttle between the nucleus
CC and the forming cell plate. {ECO:0000269|PubMed:18621982}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL55607.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF196776; AAL55607.1; ALT_FRAME; mRNA.
DR EMBL; AL132954; CAB75768.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79370.1; -; Genomic_DNA.
DR EMBL; AK175549; BAD43312.1; -; mRNA.
DR PIR; T47673; T47673.
DR RefSeq; NP_191094.1; NM_115392.4.
DR AlphaFoldDB; Q9M3B8; -.
DR SMR; Q9M3B8; -.
DR STRING; 3702.AT3G55340.1; -.
DR PaxDb; Q9M3B8; -.
DR PRIDE; Q9M3B8; -.
DR ProteomicsDB; 183203; -.
DR EnsemblPlants; AT3G55340.1; AT3G55340.1; AT3G55340.
DR GeneID; 824700; -.
DR Gramene; AT3G55340.1; AT3G55340.1; AT3G55340.
DR KEGG; ath:AT3G55340; -.
DR Araport; AT3G55340; -.
DR TAIR; locus:2100696; AT3G55340.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_424151_0_0_1; -.
DR InParanoid; Q9M3B8; -.
DR OMA; KNRRCYN; -.
DR OrthoDB; 1202220at2759; -.
DR PhylomeDB; Q9M3B8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M3B8; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IPI:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009920; P:cell plate formation involved in plant-type cell wall biogenesis; IDA:TAIR.
DR GO; GO:0000914; P:phragmoplast assembly; IDA:UniProtKB.
DR CDD; cd12271; RRM1_PHIP1; 1.
DR CDD; cd12272; RRM2_PHIP1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034361; PHIP1_RRM1.
DR InterPro; IPR034362; PHIP1_RRM2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF00098; zf-CCHC; 3.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF57756; SSF57756; 3.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..597
FT /note="Phragmoplastin interacting protein 1"
FT /id="PRO_0000452574"
FT DOMAIN 161..238
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 262..338
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 397..411
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 481..495
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 576..591
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 18..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 112..119
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 18..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 138
FT /note="E -> Q (in Ref. 1; AAL55607)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="A -> V (in Ref. 4; BAD43312)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="T -> A (in Ref. 1; AAL55607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 65997 MW; EA358A8D22E4673C CRC64;
MVLSNKKLKQ RIRQDLAESL SVSVSETNPQ SQSLKLLLDS SSHKPRLSKR EKRRNCETFA
REDDEIRENE VGNGGSSEKT DTKIKKKRKR DDAVEVDELE GDEGTKEEQK PQKKKNKKKK
KKRKVNKTPK KAEEGNVEEK VKVEEIEVNT DNKEEDGVVP NKLYVGGIPY QSTEDEIRSY
FRSCGVIIKV DCKMRPEDGA FSGIAFITFD TEDGAKRALA FDRAAMGDRY LTIQQYVKTT
TPSIPRRKTS SGFAPEMVDG YNRVYIGNLA WDTTERDIRK LFSDCVINSV RLGKNKETGE
FKGYAHVDFK DSVSVAIALK LDQQVICGRP VKICCALKDR PATDHTPGET NNAGSYNMED
TYAAADPVPA LAGRSEVDDG NYFATTVSSS KVKRRVCYEC GEKGHLSTAC PIKLQKADDQ
ANSKLGQETV DGRPAMQSYG LPKNSGDSYY MNETYASTNE TYNGGYSASA VGTGKVKRRN
CYECGEKGHL STACPIKLQN TSHTNSTLDH QTVEAGPTQV TSYSLQKKTR DTENNGGSFM
DESYATVPIS IDVTNGANDA SLTSAVSTGK IKKRNCYECG EKGHLSSACP NKLQKQG
