GRIP_ARATH
ID GRIP_ARATH Reviewed; 788 AA.
AC Q8S2T0; Q3E854; Q944S6; Q9FKX9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein GRIP;
DE Short=AtGRIP;
GN Name=GRIP; OrderedLocusNames=At5g66030; ORFNames=K2A18.10;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=15605178; DOI=10.1007/s00425-004-1311-9;
RA Gilson P.R., Vergara C.E., Kjer-Nielsen L., Teasdale R.D., Bacic A.,
RA Gleeson P.A.;
RT "Identification of a Golgi-localised GRIP domain protein from Arabidopsis
RT thaliana.";
RL Planta 219:1050-1056(2004).
RN [2]
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 [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] OF 119-788 (ISOFORM 1).
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 [5]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-717, AND INTERACTION WITH
RP ARF3/ARL1.
RX PubMed=16236155; DOI=10.1111/j.1365-313x.2005.02542.x;
RA Latijnhouwers M., Hawes C., Carvalho C., Oparka K., Gillingham A.K.,
RA Boevink P.;
RT "An Arabidopsis GRIP domain protein locates to the trans-Golgi and binds
RT the small GTPase ARL1.";
RL Plant J. 44:459-470(2005).
RN [6]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-717 AND LYS-719, AND INTERACTION
RP WITH ARF3/ARL1.
RX PubMed=16830178; DOI=10.1007/s11103-006-0022-y;
RA Stefano G., Renna L., Hanton S.L., Chatre L., Haas T.A., Brandizzi F.;
RT "ARL1 plays a role in the binding of the GRIP domain of a peripheral matrix
RT protein to the Golgi apparatus in plant cells.";
RL Plant Mol. Biol. 61:431-449(2006).
CC -!- FUNCTION: Golgi matrix protein playing a role in tethering of vesicles
CC to Golgi membranes and in maintaining the overall structure of the
CC Golgi apparatus. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the GTP-bound ARF3/ARL1, but not with the GDP-
CC bound ARF3/ARL1. {ECO:0000269|PubMed:16236155,
CC ECO:0000269|PubMed:16830178}.
CC -!- INTERACTION:
CC Q8S2T0; P40940: ARF3; NbExp=5; IntAct=EBI-1537908, EBI-1537890;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15605178,
CC ECO:0000269|PubMed:16236155, ECO:0000269|PubMed:16830178}. Note=Locates
CC to the trans-Golgi or to the trans-Golgi network (TGN).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S2T0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S2T0-2; Sequence=VSP_035178;
CC -!- DOMAIN: The C-terminal GRIP domain (711-788) is necessary and
CC sufficient for Golgi targeting.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL11549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB10408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF499634; AAM18966.1; -; mRNA.
DR EMBL; AB011474; BAB10408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98143.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98144.1; -; Genomic_DNA.
DR EMBL; AF424555; AAL11549.1; ALT_INIT; mRNA.
DR EMBL; BT002691; AAO11607.1; -; mRNA.
DR RefSeq; NP_569025.2; NM_126000.2. [Q8S2T0-2]
DR RefSeq; NP_851277.1; NM_180946.3. [Q8S2T0-1]
DR AlphaFoldDB; Q8S2T0; -.
DR SMR; Q8S2T0; -.
DR BioGRID; 21975; 9.
DR IntAct; Q8S2T0; 1.
DR STRING; 3702.AT5G66030.1; -.
DR iPTMnet; Q8S2T0; -.
DR MetOSite; Q8S2T0; -.
DR PaxDb; Q8S2T0; -.
DR PRIDE; Q8S2T0; -.
DR ProteomicsDB; 247292; -. [Q8S2T0-1]
DR EnsemblPlants; AT5G66030.1; AT5G66030.1; AT5G66030. [Q8S2T0-1]
DR EnsemblPlants; AT5G66030.2; AT5G66030.2; AT5G66030. [Q8S2T0-2]
DR GeneID; 836733; -.
DR Gramene; AT5G66030.1; AT5G66030.1; AT5G66030. [Q8S2T0-1]
DR Gramene; AT5G66030.2; AT5G66030.2; AT5G66030. [Q8S2T0-2]
DR KEGG; ath:AT5G66030; -.
DR Araport; AT5G66030; -.
DR TAIR; locus:2156922; AT5G66030.
DR eggNOG; ENOG502QTVU; Eukaryota.
DR InParanoid; Q8S2T0; -.
DR OrthoDB; 461847at2759; -.
DR PhylomeDB; Q8S2T0; -.
DR PRO; PR:Q8S2T0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8S2T0; baseline and differential.
DR Genevisible; Q8S2T0; AT.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0048193; P:Golgi vesicle transport; TAS:TAIR.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR InterPro; IPR000237; GRIP_dom.
DR Pfam; PF01465; GRIP; 1.
DR SMART; SM00755; Grip; 1.
DR PROSITE; PS50913; GRIP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Golgi apparatus; Reference proteome.
FT CHAIN 1..788
FT /note="Protein GRIP"
FT /id="PRO_0000348541"
FT DOMAIN 708..755
FT /note="GRIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 30..615
FT /evidence="ECO:0000255"
FT COMPBIAS 11..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 751..774
FT /note="KCQQAYHSSTTAATTTEATPSPAS -> N (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035178"
FT MUTAGEN 717
FT /note="Y->A: Reduced interaction with ARF3/ARL1 and loss of
FT Golgi targeting."
FT /evidence="ECO:0000269|PubMed:16236155,
FT ECO:0000269|PubMed:16830178"
FT MUTAGEN 719
FT /note="K->A: Reduced interaction with ARF3/ARL1 and loss of
FT Golgi targeting."
FT /evidence="ECO:0000269|PubMed:16830178"
FT CONFLICT 179
FT /note="L -> F (in Ref. 1; AAM18966)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="S -> A (in Ref. 1; AAM18966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 788 AA; 89859 MW; C2B98C5E8A20B10F CRC64;
MSEDKESDVV GEEEESHVIK EDKELNDASN ETLTENGDQL LQMIAELRLE NDFLRSQFEG
LKDEVAQGRS LQKAEQVEAD SAQLKQLQEQ VASLSREIDV EKQTRVAAEQ ALEHLREAYS
EADAKSQEYS SKFSQVEQKL DQEIKERDEK YADLDAKFTR LHKRAKQRIQ EIQKEKDDLD
ARFREVNETA ERASSQHSSM QQELERTRQQ ANEALKAMDA ERQQLRSANN KLRDTIEELR
GSLQPKENKI ETLQQSLLDK DQILEDLKKQ LQAVEERKQI AVTELSAKHQ KNLEGLEAQV
VDALSERDKA AETISSLQVL LAEKESKIAE MEAAATGEAA RLRAAAETLK GELAHLKSEN
EKEKETWEAS CDALKSKLEI AESNYLQAEI EVAKMRSQLG SEMSMQTQIL STKDAELKGA
REEINRLQSE FSSYKIRAHA LLQKKDMELA AAKDSEQIKS LEEALKEAEK EVYLVSAERD
RAQQDLQSAL ASLEKELEER AGALKDASEQ IKSLEVKLDS TVARNQAEKQ AWEEDLRVLE
ETWRRRCEAL TAQNEASPAE GIEKELENAK LRNKRMKEEH ESVRELADRL IEEKDREISR
LVDEMTNLRK SMESKPVWNK SPSQVHHYGN NNTESQQQDV SNLSTSAAEH QILILARQQA
QREEELAQTQ RHILALQEEI EELERENRLH SQQEAVLKTE LREMERKQKR EGVDMTYLKN
VILKLLETGE VEALLPVVGM LLQFSPEEIQ KCQQAYHSST TAATTTEATP SPASEGSGLS
VFSRFSFS