TMN7_ARATH
ID TMN7_ARATH Reviewed; 641 AA.
AC Q9LIC2; Q0WPY4;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Transmembrane 9 superfamily member 7 {ECO:0000305};
DE AltName: Full=Endomembrane protein 5 {ECO:0000303|PubMed:22570441};
DE AltName: Full=Transmembrane nine protein 7 {ECO:0000303|PubMed:20681974};
DE Short=AtTMN7 {ECO:0000303|PubMed:20681974};
DE Flags: Precursor;
GN Name=TMN7 {ECO:0000303|PubMed:20681974};
GN Synonyms=EMP5 {ECO:0000303|PubMed:22570441};
GN OrderedLocusNames=At3g13772 {ECO:0000312|Araport:AT3G13772};
GN ORFNames=MMM17.20 {ECO:0000312|EMBL:BAB01926.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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] OF 280-641.
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 [4]
RP GENE FAMILY, NOMENCLATURE, FUNCTION, AND TISSUE SPECIFICITY.
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 -!- FUNCTION: May play a role as effector of cellular copper homeostasis.
CC {ECO:0000269|PubMed:20681974}.
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 -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the root elongation
CC zone. {ECO:0000269|PubMed:20681974}.
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.
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DR EMBL; AP001307; BAB01926.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75410.1; -; Genomic_DNA.
DR EMBL; AK228926; BAF00815.1; -; mRNA.
DR RefSeq; NP_187991.1; NM_112228.3.
DR AlphaFoldDB; Q9LIC2; -.
DR BioGRID; 5921; 2.
DR STRING; 3702.AT3G13772.1; -.
DR TCDB; 8.A.68.1.2; the endomembrane protein-70 (emp70) family.
DR PaxDb; Q9LIC2; -.
DR PRIDE; Q9LIC2; -.
DR ProteomicsDB; 234434; -.
DR EnsemblPlants; AT3G13772.1; AT3G13772.1; AT3G13772.
DR GeneID; 820587; -.
DR Gramene; AT3G13772.1; AT3G13772.1; AT3G13772.
DR KEGG; ath:AT3G13772; -.
DR Araport; AT3G13772; -.
DR TAIR; locus:2091561; AT3G13772.
DR eggNOG; KOG1278; Eukaryota.
DR HOGENOM; CLU_010714_4_1_1; -.
DR InParanoid; Q9LIC2; -.
DR OMA; CKIVCRI; -.
DR OrthoDB; 641127at2759; -.
DR PhylomeDB; Q9LIC2; -.
DR PRO; PR:Q9LIC2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIC2; baseline and differential.
DR Genevisible; Q9LIC2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IDA:TAIR.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:TAIR.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
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; Ion transport; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..641
FT /note="Transmembrane 9 superfamily member 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431264"
FT TOPO_DOM 28..278
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..299
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 349..369
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..374
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..395
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 416..436
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..444
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 445..465
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 500..520
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..531
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 532..552
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 570..590
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..597
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 598..618
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 630..635
FT /note="Endoplasmic reticulum export signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
FT MOTIF 639..641
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
SQ SEQUENCE 641 AA; 74234 MW; 796A508F7B11B8BB CRC64;
MKKTKGSSFR FYATLLLSFL SFSLSRAFYL PGVAPRDFQK GDPLYVKVNK LSSTKTQLPY
DYYYLNYCKP PKILNNAENL GEVLRGDRIE NSVYTFQMLE DQPCKVGCRV KLNADSTKNF
KEKIDDEYRA NMILDNLPVA VLRQRRDGSQ STTYEHGFRV GFKGSYEGSK EEKYFIHNHL
SFRVMYHRDQ ESDSARIVGF EVTPNSILHE YKEWDEKNPQ LTTCNKDTKN LIQGNTVPQE
VEQGKEIVFT YDVSFKESEI KWASRWDTYL LMNDDQIHWF SIINSLMIVL FLSGMVAMIM
MRTLYKDISN YNQLETQDEA QEETGWKLVH GDVFRPPVNS GLLCVYVGTG VQIFGMSLVT
MMFALLGFLS PSNRGGLMTA MVLLWVFMGI FAGYSSSRLH KMFKGNKWKR MTLKTAFMFP
GILFAIFFVL NALIWGEQSS GAIPFGTMFA LFCLWFGISV PLVFVGSYLG YKKPAIEDPV
KTNKIPRQVP EQPWYMKPVF SILIGGILPF GAVFIELFFI LTSIWLNQFY YIFGFLFIVF
LILIVTCAEI TVVLCYFQLC SEDYNWWWRA YLTAGSSAFY LFLYSIFYFF TKLEITKLVS
GMLYFGYMII ISYAFFVLTG TIGFYACFWF VRKIYSSVKI D
