TMN12_ARATH
ID TMN12_ARATH Reviewed; 652 AA.
AC F4JRE0; Q67ZI3; Q67ZX5; Q9SU21;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Transmembrane 9 superfamily member 12 {ECO:0000305};
DE AltName: Full=Endomembrane protein 7 {ECO:0000303|PubMed:22570441};
DE AltName: Full=Transmembrane nine protein 12 {ECO:0000303|PubMed:20681974};
DE Short=AtTMN12 {ECO:0000303|PubMed:20681974};
DE Flags: Precursor;
GN Name=TMN12 {ECO:0000303|PubMed:20681974};
GN Synonyms=EMP7 {ECO:0000303|PubMed:22570441};
GN OrderedLocusNames=At4g12650 {ECO:0000312|Araport:AT4G12650};
GN ORFNames=T1P17.240 {ECO:0000312|EMBL:CAB53758.1};
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] OF 325-652.
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL049730; CAB53758.1; -; Genomic_DNA.
DR EMBL; AL161534; CAB78308.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83160.1; -; Genomic_DNA.
DR EMBL; AK175697; BAD43460.1; -; mRNA.
DR EMBL; AK175992; BAD43755.1; -; mRNA.
DR EMBL; AK176134; BAD43897.1; -; mRNA.
DR PIR; H85135; H85135.
DR RefSeq; NP_001319915.1; NM_001340796.1.
DR AlphaFoldDB; F4JRE0; -.
DR BioGRID; 12175; 1.
DR STRING; 3702.AT4G12650.1; -.
DR PaxDb; F4JRE0; -.
DR PRIDE; F4JRE0; -.
DR ProteomicsDB; 234439; -.
DR EnsemblPlants; AT4G12650.1; AT4G12650.1; AT4G12650.
DR GeneID; 826878; -.
DR Gramene; AT4G12650.1; AT4G12650.1; AT4G12650.
DR KEGG; ath:AT4G12650; -.
DR Araport; AT4G12650; -.
DR TAIR; locus:2135620; AT4G12650.
DR eggNOG; KOG1278; Eukaryota.
DR HOGENOM; CLU_010714_4_1_1; -.
DR InParanoid; F4JRE0; -.
DR OMA; RRANYMI; -.
DR OrthoDB; 641127at2759; -.
DR PRO; PR:F4JRE0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JRE0; baseline and differential.
DR Genevisible; F4JRE0; AT.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0072657; P:protein localization to membrane; IBA:GO_Central.
DR InterPro; IPR004240; EMP70.
DR PANTHER; PTHR10766; PTHR10766; 1.
DR Pfam; PF02990; EMP70; 1.
PE 2: Evidence at transcript level;
KW Endosome; Golgi apparatus; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..652
FT /note="Transmembrane 9 superfamily member 12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431269"
FT TOPO_DOM 21..286
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..307
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 363..383
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..386
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..407
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 427..447
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..460
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 461..481
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 511..531
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..541
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 542..562
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 581..601
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..613
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 614..634
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 641..646
FT /note="Endoplasmic reticulum export signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
FT MOTIF 650..652
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
FT CONFLICT 568
FT /note="H -> N (in Ref. 3; BAD43755)"
FT CONFLICT 597
FT /note="N -> Y (in Ref. 3; BAD43755)"
SQ SEQUENCE 652 AA; 74140 MW; 9C530433E6661FB7 CRC64;
MFGVYRVFVL LVFVSQLCNG FYLPGSYMHT YSDGDSIFAK VNSLTSIETE LPFSYYSLPY
CQPLEGIKKS AENLGELLMG DQIDNSAYRF RMRTNESLYL CTTSPLNEHE VKLLKQRTRE
LYQVNMILDN LPALRFAKQN GVTIQWTGYP VGYSPPNSND DYIINHLKFK VLVHEYEGNV
MEVIGTGEEG MGVISEADKK KALGYEIVGF EVVPCSVKYD AEKMTKLHMY DPVPSVNCPL
ELDKAQIIKE HERITFTYEV EFVKSETRWP SRWDAYLKME GARVHWFSIL NSLMVIFFLA
GIVFVIFLRT VRRDLTKYEE LDKEAQAQMN EELSGWKLVV GDVFREPEMS KLLCIMVGDG
VRITGMAVVT IVFAALGFMS PASRGMLLTG MIILYLFLGI VAGYAGVRLW RTVKGTSEGW
RSLSWSIACF FPGIAFVILT VLNFLLWSSN STGAIPISLY FELLALWFCI SVPLTLFGGF
LGTRAEAIQF PVRTNQIPRE IPERKYPSWL LVLGAGTLPF GTLFIELFFI FSSIWLGRFY
YVFGFLLIVL LLLVVVCAEV SVVLTYMHLC VEDWRWWWKA FYASGSVALY VFAYSINYLV
FDLQSLSGPV SAMLYIGYSL LMAIAIMLAT GTIGFLTSFY FVHYLFSSVK ID