TMN9_ARATH
ID TMN9_ARATH Reviewed; 644 AA.
AC Q9C5N2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Transmembrane 9 superfamily member 9 {ECO:0000305};
DE AltName: Full=Endomembrane protein 2 {ECO:0000303|PubMed:22570441};
DE AltName: Full=Transmembrane nine protein 9 {ECO:0000303|PubMed:20681974};
DE Short=AtTMN9 {ECO:0000303|PubMed:20681974};
DE Flags: Precursor;
GN Name=TMN9 {ECO:0000303|PubMed:20681974};
GN Synonyms=EMP2 {ECO:0000303|PubMed:22570441};
GN OrderedLocusNames=At5g25100 {ECO:0000312|Araport:AT5G25100};
GN ORFNames=T11H3_110 {ECO:0000312|EMBL:AC005964};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C5N2-1; Sequence=Displayed;
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; AC005964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93399.1; -; Genomic_DNA.
DR EMBL; AF360135; AAK25845.1; -; mRNA.
DR RefSeq; NP_568465.1; NM_122419.4. [Q9C5N2-1]
DR AlphaFoldDB; Q9C5N2; -.
DR SMR; Q9C5N2; -.
DR BioGRID; 17856; 3.
DR STRING; 3702.AT5G25100.2; -.
DR SwissPalm; Q9C5N2; -.
DR PaxDb; Q9C5N2; -.
DR PRIDE; Q9C5N2; -.
DR EnsemblPlants; AT5G25100.1; AT5G25100.1; AT5G25100. [Q9C5N2-1]
DR GeneID; 832581; -.
DR Gramene; AT5G25100.1; AT5G25100.1; AT5G25100. [Q9C5N2-1]
DR KEGG; ath:AT5G25100; -.
DR Araport; AT5G25100; -.
DR eggNOG; KOG1278; Eukaryota.
DR HOGENOM; CLU_010714_4_1_1; -.
DR OMA; TILITYH; -.
DR PhylomeDB; Q9C5N2; -.
DR PRO; PR:Q9C5N2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5N2; baseline and differential.
DR Genevisible; Q9C5N2; AT.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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: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 Alternative splicing; Endosome; Golgi apparatus; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..644
FT /note="Transmembrane 9 superfamily member 9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431266"
FT TOPO_DOM 28..281
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..302
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 352..372
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..377
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 378..398
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 419..439
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..451
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..472
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 502..522
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..534
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 535..555
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 574..594
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..600
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 601..621
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 633..638
FT /note="Endoplasmic reticulum export signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
FT MOTIF 642..644
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
SQ SEQUENCE 644 AA; 74120 MW; B694B9BC87469708 CRC64;
MEFYRSSRRL QILGSVILLL SIHVAHSFYL PGVAPQDFEK GDELKVKVNK LTSIKTQLPY
SYYSLPFCRP KKIVDSTENL GEVLRGDRIE NAPYSFKMRE AQMCNVLGRV MLDAKSAKAF
KEKIDDEYRV NMILDNLPLV VPIERIDPGQ GSPSVVYQLG YHVGLKGQYE GSKEQKYFMH
NHLAFTVRYH RDMQTDAARI VGFEVKPYSV KHEYEGQWSE KTRLTTCDPH TKRLVVSSAT
PQEVENKKEI IFTYDVDFQE SEVKWASRWD AYLLMSDNQI HWFSIVNSLM IVLFLSGMVA
MIMLRTLYRD ISRYNELETQ EEAQEETGWK LVHGDVFRPP ANSDLLCVYV GTGVQCLGMV
LVTMIFAMLG FLSPSNRGGL MTAMLLLWVF MGLFAGYASS RLYKMFKGTE WKRIAFRTAF
LFPAVVSAIF FVLNALIWGQ KSSGAVPFGT MFALIFLWFG ISVPLVFVGA YLGFKKPPLD
DPVKTNKIPR QIPEQAWYMN PIFSILIGGI LPFGAVFIEL FFILTSIWLN QFYYIFGFLF
LVFVILMVTC AEITIVLCYF QLCSEDYLWW WRSYLTSGSS AVYLFLYAAF YFFTKLQITK
LVSAMLYFGY MLIASYAFFV LTGTIGFYAC LWFTRLIYSS VKID