KMS2_ARATH
ID KMS2_ARATH Reviewed; 416 AA.
AC F4I8Q7; O23033; Q0WTG8; Q8LG86;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Vacuole membrane protein KMS2 {ECO:0000303|PubMed:21294794};
DE AltName: Full=Protein KILLING ME SLOWLY 2 {ECO:0000303|PubMed:21294794};
GN Name=KMS2 {ECO:0000303|PubMed:21294794};
GN OrderedLocusNames=At1g05360 {ECO:0000312|Araport:AT1G05360};
GN ORFNames=YUP8H12.2 {ECO:0000312|EMBL:AAB71442.1};
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-416.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
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 -!- SIMILARITY: Belongs to the VMP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000098; AAB71442.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27829.1; -; Genomic_DNA.
DR EMBL; AY084410; AAM60984.1; -; mRNA.
DR EMBL; AK227587; BAE99580.1; -; mRNA.
DR PIR; E86188; E86188.
DR RefSeq; NP_563735.1; NM_100415.5.
DR AlphaFoldDB; F4I8Q7; -.
DR STRING; 3702.AT1G05360.1; -.
DR PaxDb; F4I8Q7; -.
DR PRIDE; F4I8Q7; -.
DR ProteomicsDB; 230317; -.
DR EnsemblPlants; AT1G05360.1; AT1G05360.1; AT1G05360.
DR GeneID; 837035; -.
DR Gramene; AT1G05360.1; AT1G05360.1; AT1G05360.
DR KEGG; ath:AT1G05360; -.
DR Araport; AT1G05360; -.
DR TAIR; locus:2207180; AT1G05360.
DR eggNOG; KOG1109; Eukaryota.
DR HOGENOM; CLU_033298_0_1_1; -.
DR InParanoid; F4I8Q7; -.
DR OMA; WWLYWIG; -.
DR OrthoDB; 822110at2759; -.
DR PRO; PR:F4I8Q7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I8Q7; baseline and differential.
DR Genevisible; F4I8Q7; 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.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5XF36"
FT CHAIN 2..416
FT /note="Vacuole membrane protein KMS2"
FT /id="PRO_0000430959"
FT TOPO_DOM 2..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5XF36"
FT TRANSMEM 60..80
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..100
FT /note="Lumenal"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 101..123
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 250..270
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..281
FT /note="Lumenal"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 282..304
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 316..336
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..364
FT /note="Lumenal"
FT /evidence="ECO:0000303|PubMed:21294794"
FT TRANSMEM 365..385
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5XF36"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q5XF36"
FT CONFLICT 134
FT /note="V -> A (in Ref. 3; AAM60984)"
FT CONFLICT 146
FT /note="I -> V (in Ref. 3; AAM60984)"
FT CONFLICT 217
FT /note="K -> R (in Ref. 4; BAE99580)"
FT CONFLICT 232
FT /note="K -> I (in Ref. 3; AAM60984)"
FT CONFLICT 411
FT /note="T -> S (in Ref. 3; AAM60984)"
SQ SEQUENCE 416 AA; 46619 MW; 5E9A041B844F123A CRC64;
MGYGNRASSK TPAISGLREK HQQDLEKLTL TSQPFKTLRL FVVAVFLYVR RWSSYLLANV
GWLILFCSIF VAFAALLVTL DGPHVKHVEE LSEYTRFGLW WIFLGVASSI GLGSGLHTFV
LYLGPHIALF TIKVMQCGRV DLKSAIYDTI QLKRSPSWLD KPCHEFGSPV FSSGVPLSSI
LPQVQIEAIL WGLGTALGEL PPYFISRAAS LSGGKMKELE TCSGDDNGFI AKRVNQIKSW
LLSHSQYLNF FTILILASVP NPLFDLAGIM CGQFEKPFWE FFLATLIGKA IIKTHIQTVF
IICVCNNQLL DWVENELIYI LSFVPGFASA LPELTAKLRL MKEKYLIASP PVSSDINVKK
WDLSFASVWN GVVWLMLLNF FGQIVTSTAQ RYLKKQQEEE LDALTNKSSL TSKKSK
