GILT_ARATH
ID GILT_ARATH Reviewed; 233 AA.
AC Q9SV73; Q8L9R1;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Gamma-interferon-responsive lysosomal thiol protein {ECO:0000303|PubMed:21052676};
DE Short=AtGILT {ECO:0000303|PubMed:21052676};
DE Flags: Precursor;
GN Name=GILT {ECO:0000303|PubMed:21052676};
GN OrderedLocusNames=At4g12960 {ECO:0000312|Araport:AT4G12960};
GN ORFNames=F25G13.50 {ECO:0000312|EMBL:CAB45495.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 TISSUE SPECIFICITY.
RX PubMed=17177805; DOI=10.1111/j.1467-7652.2006.00189.x;
RA Tiwari S., Spielman M., Day R.C., Scott R.J.;
RT "Proliferative phase endosperm promoters from Arabidopsis thaliana.";
RL Plant Biotechnol. J. 4:393-407(2006).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=21052676; DOI=10.1007/s00299-010-0945-2;
RA Wu L., El-Mezawy A., Shah S.;
RT "A seed coat outer integument-specific promoter for Brassica napus.";
RL Plant Cell Rep. 30:75-80(2011).
CC -!- FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide
CC bonds. May facilitate the complete unfolding of proteins destined for
CC lysosomal degradation. {ECO:0000250|UniProtKB:Q5XJN2}.
CC -!- SUBUNIT: Dimer; disulfide-linked. {ECO:0000250|UniProtKB:P13284}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P13284}. Lysosome
CC {ECO:0000250|UniProtKB:P13284}.
CC -!- TISSUE SPECIFICITY: Expressed in the outer integument of seed coat.
CC {ECO:0000269|PubMed:17177805, ECO:0000269|PubMed:21052676}.
CC -!- SIMILARITY: Belongs to the GILT family. {ECO:0000305}.
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DR EMBL; AL079349; CAB45495.1; -; Genomic_DNA.
DR EMBL; AL161535; CAB78338.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83207.1; -; Genomic_DNA.
DR EMBL; AY058119; AAL25536.1; -; mRNA.
DR EMBL; BT000483; AAN18052.1; -; mRNA.
DR EMBL; AY088280; AAM65819.1; -; mRNA.
DR PIR; T10198; T10198.
DR RefSeq; NP_193032.1; NM_117365.3.
DR AlphaFoldDB; Q9SV73; -.
DR SMR; Q9SV73; -.
DR STRING; 3702.AT4G12960.2; -.
DR PRIDE; Q9SV73; -.
DR ProteomicsDB; 221894; -.
DR EnsemblPlants; AT4G12960.1; AT4G12960.1; AT4G12960.
DR GeneID; 826908; -.
DR Gramene; AT4G12960.1; AT4G12960.1; AT4G12960.
DR KEGG; ath:AT4G12960; -.
DR Araport; AT4G12960; -.
DR HOGENOM; CLU_066886_1_1_1; -.
DR PhylomeDB; Q9SV73; -.
DR PRO; PR:Q9SV73; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SV73; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR InterPro; IPR004911; Interferon-induced_GILT.
DR PANTHER; PTHR13234; PTHR13234; 1.
DR Pfam; PF03227; GILT; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Lysosome; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..233
FT /note="Gamma-interferon-responsive lysosomal thiol protein"
FT /id="PRO_5011951341"
FT PROPEP 200..233
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P13284"
FT /id="PRO_0000444149"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 42..45
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P13284"
FT CONFLICT 194
FT /note="N -> K (in Ref. 4; AAM65819)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..201
FT /note="TT -> VA (in Ref. 4; AAM65819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 26082 MW; 6126FB09DCEB0E25 CRC64;
MVSSSLTKLV FFGCLLLLTF TDNLVAGKSG KVKLNLYYES LCPGCQEFIV DDLGKIFDYD
LYTITDLKLF PFGNAELSDN LTVTCQHGEE ECKLNALEAC ALRTWPDQKS QYSFIRCVES
DTKGWESCVK NSGREKAIND CYNGDLSRKL ILGYATKTKN LKPPHEYVPW VTLNGKPLDD
SVQSTDDLVA QICNAYKGKT TLPKVCNSSA SMSKSPERKW KLQVSYANKA TNY
