KMS1_ARATH
ID KMS1_ARATH Reviewed; 416 AA.
AC Q5XF36; O23350; Q93YX1;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Vacuole membrane protein KMS1 {ECO:0000303|PubMed:21294794};
DE AltName: Full=Protein KILLING ME SLOWLY 1 {ECO:0000303|PubMed:21294794};
GN Name=KMS1 {ECO:0000303|PubMed:21294794};
GN OrderedLocusNames=At4g14950 {ECO:0000312|Araport:AT4G14950};
GN ORFNames=dl3515w {ECO:0000312|EMBL:CAB46053.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [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;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21294794; DOI=10.1111/j.1365-313x.2011.04522.x;
RA Wang P., Hummel E., Osterrieder A., Meyer A.J., Frigerio L., Sparkes I.,
RA Hawes C.;
RT "KMS1 and KMS2, two plant endoplasmic reticulum proteins involved in the
RT early secretory pathway.";
RL Plant J. 66:613-628(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in the early secretory pathway. Required for the
CC correct export of secretory products from the endoplasmic reticulum
CC (ER) and involved in the maintenance of ER integrity.
CC {ECO:0000269|PubMed:21294794}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21294794}; Multi-pass membrane protein
CC {ECO:0000303|PubMed:21294794}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Name=1;
CC IsoId=Q5XF36-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the VMP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB46053.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g14950 has been split into 2 genes: At4g14950 and At4g14965.; Evidence={ECO:0000305};
CC Sequence=CAB78537.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g14950 has been split into 2 genes: At4g14950 and At4g14965.; Evidence={ECO:0000305};
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DR EMBL; Z97337; CAB46053.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78537.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83528.1; -; Genomic_DNA.
DR EMBL; AY059730; AAL24087.1; -; mRNA.
DR EMBL; BT015780; AAU90070.1; -; mRNA.
DR PIR; C85164; C85164.
DR PIR; H71412; H71412.
DR RefSeq; NP_567450.1; NM_117581.5. [Q5XF36-1]
DR AlphaFoldDB; Q5XF36; -.
DR BioGRID; 12450; 6.
DR IntAct; Q5XF36; 6.
DR STRING; 3702.AT4G14950.1; -.
DR iPTMnet; Q5XF36; -.
DR PaxDb; Q5XF36; -.
DR PRIDE; Q5XF36; -.
DR ProteomicsDB; 230383; -. [Q5XF36-1]
DR EnsemblPlants; AT4G14950.1; AT4G14950.1; AT4G14950. [Q5XF36-1]
DR GeneID; 827153; -.
DR Gramene; AT4G14950.1; AT4G14950.1; AT4G14950. [Q5XF36-1]
DR KEGG; ath:AT4G14950; -.
DR Araport; AT4G14950; -.
DR TAIR; locus:2129530; AT4G14950.
DR eggNOG; KOG1109; Eukaryota.
DR InParanoid; Q5XF36; -.
DR OMA; EEPYDKR; -.
DR OrthoDB; 822110at2759; -.
DR PhylomeDB; Q5XF36; -.
DR PRO; PR:Q5XF36; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5XF36; baseline and differential.
DR Genevisible; Q5XF36; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0010256; P:endomembrane system organization; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR InterPro; IPR032816; SNARE_assoc.
DR Pfam; PF09335; SNARE_assoc; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..416
FT /note="Vacuole membrane protein KMS1"
FT /id="PRO_0000430958"
FT TOPO_DOM 2..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21294794"
FT TRANSMEM 61..81
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..101
FT /note="Lumenal"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 102..124
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 258..278
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..289
FT /note="Lumenal"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 290..312
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 324..344
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..372
FT /note="Lumenal"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 373..393
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21294794"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 94
FT /note="E -> G (in Ref. 4; AAL24087)"
FT CONFLICT 380
FT /note="I -> M (in Ref. 4; AAL24087)"
SQ SEQUENCE 416 AA; 45848 MW; 593ED01EBCD49E75 CRC64;
MGSAGVASSS SDVAISALRE KHEKEVENLT LTTQPLNTLK LFVEATIQYI KRSISYLLAH
GGWFILITTL LVVSGGLLVT VDGPHGKHVE EVLEYVRYGL WWIALGVASS IGLGSGLHTF
VLYLGPHIAL FTLKATLCGR VDLKSAPYDT IQLKRVPSWL DKSCSEFGPP LMISAAGSRV
PLTSILPQVQ LEAILWGIGT ALGELPPYFI SRAASISGST VDGMEELDGS STEDSGFMAT
HLNRVKRWLL THSQHLNFFT VLVLASVPNP LFDLAGIMCG QFGIPFWEFF LATLIGKAII
KTHIQTIFII CVCNNQLLDW MENELIWILS HVPGLASMLP GLTAKLHAMK EKYIDAPSPV
PSHIKVKKWD FSFASIWNGI VWLMLLNFFV KIVTATAQRH LKKKQEKEMA TLTHSD
