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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.
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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
 
 
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