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GIP1L_ARATH
ID   GIP1L_ARATH             Reviewed;         575 AA.
AC   A4FVR1; Q9LFZ2; Q9LG31;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=GBF-interacting protein 1-like {ECO:0000303|PubMed:24484953};
DE            Short=Protein GIP1-like {ECO:0000303|PubMed:24484953};
GN   Name=GIP1L {ECO:0000303|PubMed:24484953};
GN   OrderedLocusNames=At1g55820 {ECO:0000312|Araport:AT1G55820};
GN   ORFNames=F14J16.6 {ECO:0000312|EMBL:AAF79311.1},
GN   F20N2.19 {ECO:0000312|EMBL:AAF79498.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=24484953; DOI=10.1016/j.jplph.2013.11.003;
RA   Lee H.W., Park J.H., Park M.Y., Kim J.;
RT   "GIP1 may act as a coactivator that enhances transcriptional activity of
RT   LBD18 in Arabidopsis.";
RL   J. Plant Physiol. 171:14-18(2014).
CC   -!- FUNCTION: May act as a transcriptional coactivator of LOB domain-
CC       containing proteins. {ECO:0000250|UniProtKB:Q8VZS6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24484953}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC       {ECO:0000269|PubMed:24484953}.
CC   -!- SIMILARITY: Belongs to the GIP1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79311.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF79498.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC002304; AAF79311.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC002328; AAF79498.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33303.1; -; Genomic_DNA.
DR   EMBL; BT030359; ABO38772.1; -; mRNA.
DR   PIR; F96599; F96599.
DR   RefSeq; NP_175978.2; NM_104459.4.
DR   AlphaFoldDB; A4FVR1; -.
DR   IntAct; A4FVR1; 1.
DR   iPTMnet; A4FVR1; -.
DR   PaxDb; A4FVR1; -.
DR   PRIDE; A4FVR1; -.
DR   ProteomicsDB; 220765; -.
DR   EnsemblPlants; AT1G55820.1; AT1G55820.1; AT1G55820.
DR   GeneID; 842032; -.
DR   Gramene; AT1G55820.1; AT1G55820.1; AT1G55820.
DR   KEGG; ath:AT1G55820; -.
DR   Araport; AT1G55820; -.
DR   TAIR; locus:2012015; AT1G55820.
DR   eggNOG; ENOG502RQC4; Eukaryota.
DR   HOGENOM; CLU_482657_0_0_1; -.
DR   InParanoid; A4FVR1; -.
DR   OMA; FVKETCC; -.
DR   OrthoDB; 345523at2759; -.
DR   PhylomeDB; A4FVR1; -.
DR   PRO; PR:A4FVR1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; A4FVR1; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   InterPro; IPR044277; GIP1.
DR   InterPro; IPR009719; GIP1_N.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR46775; PTHR46775; 2.
DR   Pfam; PF06972; GIP1_N; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..575
FT                   /note="GBF-interacting protein 1-like"
FT                   /id="PRO_0000435636"
FT   REGION          66..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  61877 MW;  EA9530C15839548A CRC64;
     MSSSDGGSSR VSIPYHLRKT LQKIREYTGK QHSDEDIFAV YKDSFNDPHE TAQKLLFLDT
     FHEVRSKREK KKEPIVPVTQ PSGRGGRRNF ASSNSYQGSG RNASFKRENG ANHVTRGSRT
     AQPATNKASN ITVPNETKVS GPASIPSEVS NHKAQDDPSL ISASRCSSKS DQAIEIETAS
     KQGKNQSLPK PDVSEQSHVT FPFHLQVAKG LQNGLTFGSF DSNFVKEVSS SNGASGGYDS
     NFESSHGTGD DERESSPTTN GITGVASARE ETSTVSEDKD YGISNSATGA EPVVHSDHIV
     PPVEEVPKEE ALSNTETHQI AYGQEAPLSV FGLVPSLSAI GQPVNTEAAE TQPGNSNSPP
     ISLVSYPPDQ SSIAAATQQT NFLRQQYPPN FFPYGYYSPY YMPPPYIHQF LSPNGIPQQS
     YFPQGAALTA PSHAKPVDNT ENPPTTNPYL HTSPMVASSI PSTTTLNSIH SEEKASHLTE
     SAAAWIGQGF GNLQVNPMYN LAYQGQPLGF PVVQAGHGGL MGMHQPTQPM AAASTTYQTL
     PPPPHTTTAM GEPIGHPHIA YQQPQAALTN WVNNY
 
 
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