GILP_ARATH
ID GILP_ARATH Reviewed; 134 AA.
AC Q94CD4; A0A1P8BBV2; Q9LYV7;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=GSH-induced LITAF domain protein {ECO:0000303|PubMed:21526181};
DE Short=AtGILP {ECO:0000303|PubMed:21526181};
GN Name=GILP {ECO:0000303|PubMed:21526181};
GN OrderedLocusNames=At5g13190 {ECO:0000312|Araport:AT5G13190};
GN ORFNames=T19L5.5 {ECO:0000312|EMBL:AED91862.1},
GN T31B5_10 {ECO:0000312|EMBL:CAB86626.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH LSD1 AND MIEL1, SUBCELLULAR LOCATION, DOMAIN,
RP AND INDUCTION BY FUMONISIN B1 AND AVIRULENT PATHOGEN.
RX PubMed=21526181; DOI=10.1371/journal.pone.0018750;
RA He S., Tan G., Liu Q., Huang K., Ren J., Zhang X., Yu X., Huang P., An C.;
RT "The LSD1-interacting protein GILP is a LITAF domain protein that
RT negatively regulates hypersensitive cell death in Arabidopsis.";
RL PLoS ONE 6:E18750-E18750(2011).
CC -!- FUNCTION: Acts as a membrane anchor, bringing other regulators of
CC programmed cell death (PCD) to the plasma membrane. Negatively
CC regulates hypersensitive cell death. {ECO:0000269|PubMed:21526181}.
CC -!- SUBUNIT: Interacts (via N- and C-terminal) with MIEL1 and LSD1 (via N-
CC terminus). {ECO:0000269|PubMed:21526181}.
CC -!- INTERACTION:
CC Q94CD4; P94077: LSD1; NbExp=3; IntAct=EBI-6274018, EBI-5849461;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21526181};
CC Peripheral membrane protein {ECO:0000269|PubMed:21526181}; Cytoplasmic
CC side {ECO:0000269|PubMed:21526181}.
CC -!- INDUCTION: Up-regulated by Pseudomonas syringae avrRpt2 and fumonisin
CC B1 (FB1). {ECO:0000269|PubMed:21526181}.
CC -!- DOMAIN: The LITAF domain is stabilized by a bound zinc ion (By
CC similarity). The LITAF amphipathic helix region (68-90) is necessary
CC for plasma membrane localization. {ECO:0000250|UniProtKB:Q99732,
CC ECO:0000269|PubMed:21526181}.
CC -!- DOMAIN: Both N-terminal (1-47) and C-terminal (114-134) domains are
CC sufficient for the interaction with MIEL1 or with the N-terminal domain
CC of LSD1. {ECO:0000269|PubMed:21526181}.
CC -!- DOMAIN: The LITAF domain (48-113) is not involved in the interaction
CC with LSD1. {ECO:0000269|PubMed:21526181}.
CC -!- SIMILARITY: Belongs to the CDIP1/LITAF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ANM69073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB86626.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163491; CAB86626.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91862.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69073.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY034946; AAK59452.1; -; mRNA.
DR EMBL; AY062988; AAL34162.1; -; mRNA.
DR EMBL; AY088302; AAM65841.1; -; mRNA.
DR PIR; T48566; T48566.
DR RefSeq; NP_001330776.1; NM_001343258.1.
DR RefSeq; NP_568286.1; NM_121322.2.
DR AlphaFoldDB; Q94CD4; -.
DR IntAct; Q94CD4; 2.
DR STRING; 3702.AT5G13190.1; -.
DR TCDB; 9.B.230.1.1; the gsh-induced litaf domain protein (gilp) family.
DR PaxDb; Q94CD4; -.
DR PRIDE; Q94CD4; -.
DR ProteomicsDB; 221893; -.
DR EnsemblPlants; AT5G13190.1; AT5G13190.1; AT5G13190.
DR GeneID; 831158; -.
DR Gramene; AT5G13190.1; AT5G13190.1; AT5G13190.
DR KEGG; ath:AT5G13190; -.
DR Araport; AT5G13190; -.
DR TAIR; locus:2183891; AT5G13190.
DR eggNOG; ENOG502S0H7; Eukaryota.
DR HOGENOM; CLU_131782_0_0_1; -.
DR InParanoid; Q94CD4; -.
DR OMA; WIQESFA; -.
DR OrthoDB; 1564782at2759; -.
DR PhylomeDB; Q94CD4; -.
DR PRO; PR:Q94CD4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94CD4; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0034051; P:negative regulation of plant-type hypersensitive response; IMP:TAIR.
DR InterPro; IPR006629; LITAF.
DR InterPro; IPR037519; LITAF_fam.
DR PANTHER; PTHR23292; PTHR23292; 1.
DR Pfam; PF10601; zf-LITAF-like; 1.
DR SMART; SM00714; LITAF; 1.
DR PROSITE; PS51837; LITAF; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..134
FT /note="GSH-induced LITAF domain protein"
FT /id="PRO_0000440615"
FT DOMAIN 33..113
FT /note="LITAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT REGION 68..88
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000305|PubMed:21526181"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
SQ SEQUENCE 134 AA; 14560 MW; A9FC0A0C62D7D78A CRC64;
MAKEGTTVIG VPYYAGQNPY QAGIVPPNAI YGDPLGAPIQ QTIYRDTPAP FNCLYCGNTG
LTNLRSKPGV AAVVACMMPF MLGFCFLCPS MDCLWNKQHH CPQCGNKVAD FEKSDPCLVM
DPPQWKQPSF ALPA
