TMN2_ARATH
ID TMN2_ARATH Reviewed; 592 AA.
AC Q940S0; Q9LQW5; Q9LQW6; Q9MA18;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Transmembrane 9 superfamily member 2 {ECO:0000305};
DE AltName: Full=Endomembrane protein 8 {ECO:0000303|PubMed:22570441};
DE AltName: Full=Transmembrane nine protein 2 {ECO:0000303|PubMed:20681974};
DE Short=AtTMN2 {ECO:0000303|PubMed:20681974};
DE Flags: Precursor;
GN Name=TMN2 {ECO:0000303|PubMed:20681974};
GN Synonyms=EMP8 {ECO:0000303|PubMed:22570441};
GN OrderedLocusNames=At1g14670 {ECO:0000312|Araport:AT1G14670};
GN ORFNames=F10B6.2/F10B6.3 {ECO:0000312|EMBL:AAF79216.1,
GN ECO:0000312|EMBL:AAF79217.1}, T5E21.15 {ECO:0000312|EMBL:AAF63170.1};
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].
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20681974; DOI=10.1111/j.1399-3054.2010.01404.x;
RA Hegelund J.N., Jahn T.P., Baekgaard L., Palmgren M.G., Schjoerring J.K.;
RT "Transmembrane nine proteins in yeast and Arabidopsis affect cellular metal
RT contents without changing vacuolar morphology.";
RL Physiol. Plantarum 140:355-367(2010).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22570441; DOI=10.1105/tpc.112.096057;
RA Gao C., Yu C.K., Qu S., San M.W., Li K.Y., Lo S.W., Jiang L.;
RT "The Golgi-localized Arabidopsis endomembrane protein12 contains both
RT endoplasmic reticulum export and Golgi retention signals at its C
RT terminus.";
RL Plant Cell 24:2086-2104(2012).
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:P32802};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q940G0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The C-terminal KXD/E motif functions as a Golgi retention
CC signal, certainly through the binding to the COP1 coatomer.
CC {ECO:0000250|UniProtKB:Q940G0}.
CC -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63170.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79216.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=AAF79217.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
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DR EMBL; AC006917; AAF79216.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006917; AAF79217.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010657; AAF63170.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29200.1; -; Genomic_DNA.
DR EMBL; AY053419; AAK96649.1; -; mRNA.
DR EMBL; AY093961; AAM16222.1; -; mRNA.
DR PIR; H86280; H86280.
DR RefSeq; NP_172919.1; NM_101334.3.
DR AlphaFoldDB; Q940S0; -.
DR BioGRID; 23269; 23.
DR IntAct; Q940S0; 23.
DR STRING; 3702.AT1G14670.1; -.
DR PaxDb; Q940S0; -.
DR PRIDE; Q940S0; -.
DR ProMEX; Q940S0; -.
DR ProteomicsDB; 234450; -.
DR EnsemblPlants; AT1G14670.1; AT1G14670.1; AT1G14670.
DR GeneID; 838029; -.
DR Gramene; AT1G14670.1; AT1G14670.1; AT1G14670.
DR KEGG; ath:AT1G14670; -.
DR Araport; AT1G14670; -.
DR TAIR; locus:2006872; AT1G14670.
DR eggNOG; KOG1277; Eukaryota.
DR HOGENOM; CLU_010714_0_2_1; -.
DR InParanoid; Q940S0; -.
DR OMA; NAPCRTT; -.
DR OrthoDB; 641127at2759; -.
DR PhylomeDB; Q940S0; -.
DR PRO; PR:Q940S0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q940S0; baseline and differential.
DR Genevisible; Q940S0; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0072657; P:protein localization to membrane; IBA:GO_Central.
DR InterPro; IPR004240; EMP70.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10766; PTHR10766; 1.
DR Pfam; PF02990; EMP70; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 2: Evidence at transcript level;
KW Endosome; Golgi apparatus; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..592
FT /note="Transmembrane 9 superfamily member 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431259"
FT TOPO_DOM 25..229
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 230..250
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..323
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..345
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 363..383
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..397
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 398..418
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 453..473
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..485
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 486..506
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 522..542
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..553
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 554..574
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 581..586
FT /note="Endoplasmic reticulum export signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
FT MOTIF 590..592
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
SQ SEQUENCE 592 AA; 68084 MW; FE31F94669A2E963 CRC64;
MRTPTTILLL VGAILFSGAG YVRSDASDHR YKEGDTVPLY ANKVGPFHNP SETYRYFDLP
FCIPEGVKEK KEALGEVLNG DRLVSAPYKL NFRDEKESEV YCNKKLSKEE VKQFRKAVEK
DYYFQMYYDD LPIWGFIGKV DKDIKSDPSE FKYFLYKHIQ FEILYNKDRV IEISARMDPH
SLVDLTEDKE VDAEFMYTVK WKETETPFEK RMEKYSMSSS LPHHLEIHWF SIINSCVTVL
LLTGFLATIL MRVLKNDFMK YAQDEEAADD QEETGWKYIH GDVFRFPTHN SLFAASLGSG
TQLFTLTIFI FMLALVGVFY PYNRGALFTA LVVIYALTSG IAGYTSASFY CQLEGKSWVR
NLLLTGCLFC GPLFLTFCFL NTVAITYTAT AALPFGTIVV IVLIWTLVTS PLLVLGGIAG
KNSKAEFQAP CRTTKYPREI PPLPWYRSAI PQMAMAGFLP FSAIYIELYY IFASVWGHRI
YTIYSILFIV FIILIIVTAF ITVALTYFQL AAEDHQWWWR SFLCGGSTGL FIYAYCLYYY
YARSDMSGFM QTSFFFGYMA CICYGFFLML GTVGFRAALL FVRHIYRSIK CE
