TMN8_ARATH
ID TMN8_ARATH Reviewed; 648 AA.
AC F4KIB2; Q9LEV5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Transmembrane 9 superfamily member 8 {ECO:0000305};
DE AltName: Full=Endomembrane protein 1 {ECO:0000303|PubMed:22570441};
DE AltName: Full=Transmembrane nine protein 8 {ECO:0000303|PubMed:20681974};
DE Short=AtTMN8 {ECO:0000303|PubMed:20681974};
DE Flags: Precursor;
GN Name=TMN8 {ECO:0000303|PubMed:20681974};
GN Synonyms=EMP1 {ECO:0000303|PubMed:22570441};
GN OrderedLocusNames=At5g10840 {ECO:0000312|Araport:AT5G10840};
GN ORFNames=T30N20_110 {ECO:0000312|EMBL:CAB96839.1};
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=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] OF 545-648.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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=BX833631; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB96839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL365234; CAB96839.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91602.1; -; Genomic_DNA.
DR EMBL; BX833631; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T50793; T50793.
DR RefSeq; NP_196645.2; NM_121122.4.
DR AlphaFoldDB; F4KIB2; -.
DR BioGRID; 16229; 34.
DR IntAct; F4KIB2; 32.
DR STRING; 3702.AT5G10840.1; -.
DR SwissPalm; F4KIB2; -.
DR PaxDb; F4KIB2; -.
DR PRIDE; F4KIB2; -.
DR ProteomicsDB; 234435; -.
DR EnsemblPlants; AT5G10840.1; AT5G10840.1; AT5G10840.
DR GeneID; 830951; -.
DR Gramene; AT5G10840.1; AT5G10840.1; AT5G10840.
DR KEGG; ath:AT5G10840; -.
DR Araport; AT5G10840; -.
DR TAIR; locus:2183710; AT5G10840.
DR eggNOG; KOG1278; Eukaryota.
DR HOGENOM; CLU_010714_4_1_1; -.
DR InParanoid; F4KIB2; -.
DR OMA; FCPPEKI; -.
DR OrthoDB; 641127at2759; -.
DR PRO; PR:F4KIB2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KIB2; baseline and differential.
DR Genevisible; F4KIB2; 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:0005797; C:Golgi medial cisterna; 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:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..648
FT /note="Transmembrane 9 superfamily member 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431265"
FT TOPO_DOM 34..285
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 286..306
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 356..376
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..381
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 382..402
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 423..443
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..455
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 456..476
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 507..527
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..538
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 539..559
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 578..598
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..604
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 605..625
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 637..642
FT /note="Endoplasmic reticulum export signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
FT MOTIF 646..648
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:Q940G0"
FT CONFLICT 570
FT /note="D -> E (in Ref. 3; BX833631)"
FT CONFLICT 592
FT /note="A -> T (in Ref. 3; BX833631)"
FT CONFLICT 612
FT /note="F -> L (in Ref. 3; BX833631)"
FT CONFLICT 623
FT /note="F -> I (in Ref. 3; BX833631)"
FT CONFLICT 634
FT /note="C -> Y (in Ref. 3; BX833631)"
SQ SEQUENCE 648 AA; 74467 MW; A2E22FC979A8360E CRC64;
MAMEFLRSSR RILESSGCAI ALIFLLFIHG AHSFYLPGVA PQDFEKGDEL KVKVNKLTSI
KTQLPYSYYS LPFCRPSKIV DSTENLGEVL RGDRIENAPY SFKMREAQMC NILGRVTLDA
KTAKAFKEKI DDEYRVNMIL DNLPLVVPIE RVDQGSPSVV YQLGYHVGLK GQYEGSKEQK
FFMHNHLAFT VRYHRDIQTD AARIVGFEVK PYSVKHEYEG EWSEKTRLTT CDPHTKRLVV
SSATPQEVEQ KKEIIFTYDV DFQESEVKWA SRWDTYLLMS DNQIHWFSIV NSLMIVLFLS
GMVAMIMLRT LYRDISRYNE LETQEEAQEE TGWKLVHGDV FRLPTNSDLL CVYVGTGVQC
LGMVFVTMIF AMLGFLSPSN RGGLMTAMLL LWVFMGLFAG YASSRLYKMF KGTEWKRIAF
RTAFLFPAVV SAIFFVLNAL IWGQKSSGAV PFGTMFALIF LWFGISVPLV FVGGYIGFKK
PAADDPVKTN KIPRQIPEQA WYMNPVFSIL IGGILPFGAV FIELFFILTS IWLNQFYYIF
GFLFLVFVIL IVTCAEITVV LCYFQLCSED YLWWWRSYLT SGSSALYLFL YATFYFFTKL
QITKLVSAML YFGYMLIASY AFFVLTGTIG FYACLWFTRL IYSSVKID
