TM208_HUMAN
ID TM208_HUMAN Reviewed; 173 AA.
AC Q9BTX3; Q05CT0; Q96D25; Q9NZZ7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transmembrane protein 208;
GN Name=TMEM208; ORFNames=HSPC171;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TYR-82.
RC TISSUE=Ovary, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23691174; DOI=10.1371/journal.pone.0064228;
RA Zhao Y., Hu J., Miao G., Qu L., Wang Z., Li G., Lv P., Ma D., Chen Y.;
RT "Transmembrane protein 208: a novel ER-localized protein that regulates
RT autophagy and ER stress.";
RL PLoS ONE 8:E64228-E64228(2013).
RN [6]
RP ACETYLATION AT MET-1.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
CC -!- FUNCTION: May function as a negative regulator of endoplasmic
CC reticulum-stress induced autophagy. {ECO:0000269|PubMed:23691174}.
CC -!- INTERACTION:
CC Q9BTX3; Q8IYJ2-2: C10orf67; NbExp=3; IntAct=EBI-12876824, EBI-13381098;
CC Q9BTX3; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12876824, EBI-6942903;
CC Q9BTX3; Q15125: EBP; NbExp=3; IntAct=EBI-12876824, EBI-3915253;
CC Q9BTX3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12876824, EBI-18304435;
CC Q9BTX3; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12876824, EBI-13345167;
CC Q9BTX3; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-12876824, EBI-13067820;
CC Q9BTX3; P48051: KCNJ6; NbExp=3; IntAct=EBI-12876824, EBI-12017638;
CC Q9BTX3; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-12876824, EBI-373355;
CC Q9BTX3; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-12876824, EBI-11978907;
CC Q9BTX3; O15173: PGRMC2; NbExp=3; IntAct=EBI-12876824, EBI-1050125;
CC Q9BTX3; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-12876824, EBI-11337973;
CC Q9BTX3; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-12876824, EBI-7545592;
CC Q9BTX3; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-12876824, EBI-2466594;
CC Q9BTX3; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-12876824, EBI-12823227;
CC Q9BTX3; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12876824, EBI-17247926;
CC Q9BTX3; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12876824, EBI-18159983;
CC Q9BTX3; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-12876824, EBI-10262251;
CC Q9BTX3; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-12876824, EBI-13292283;
CC Q9BTX3; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-12876824, EBI-742688;
CC Q9BTX3; P27105: STOM; NbExp=3; IntAct=EBI-12876824, EBI-1211440;
CC Q9BTX3; Q9Y320: TMX2; NbExp=3; IntAct=EBI-12876824, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23691174}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23691174}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BTX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTX3-2; Sequence=VSP_032505;
CC -!- SIMILARITY: Belongs to the TMEM208 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29134.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF161519; AAF29134.1; ALT_FRAME; mRNA.
DR EMBL; CH471092; EAW83106.1; -; Genomic_DNA.
DR EMBL; CH471092; EAW83107.1; -; Genomic_DNA.
DR EMBL; BC003080; AAH03080.1; -; mRNA.
DR EMBL; BC021109; AAH21109.1; -; mRNA.
DR EMBL; BC013412; AAH13412.1; -; mRNA.
DR CCDS; CCDS45511.1; -. [Q9BTX3-1]
DR RefSeq; NP_001305146.1; NM_001318217.1.
DR RefSeq; NP_054906.2; NM_014187.3. [Q9BTX3-1]
DR AlphaFoldDB; Q9BTX3; -.
DR BioGRID; 118868; 51.
DR IntAct; Q9BTX3; 25.
DR STRING; 9606.ENSP00000305892; -.
DR TCDB; 9.B.26.1.1; the regulator of er stress and autophagy tmem208 (tmem208) family.
DR iPTMnet; Q9BTX3; -.
DR BioMuta; TMEM208; -.
DR DMDM; 74733157; -.
DR EPD; Q9BTX3; -.
DR jPOST; Q9BTX3; -.
DR MassIVE; Q9BTX3; -.
DR MaxQB; Q9BTX3; -.
DR PaxDb; Q9BTX3; -.
DR PeptideAtlas; Q9BTX3; -.
DR PRIDE; Q9BTX3; -.
DR ProteomicsDB; 79025; -. [Q9BTX3-1]
DR ProteomicsDB; 79026; -. [Q9BTX3-2]
DR TopDownProteomics; Q9BTX3-1; -. [Q9BTX3-1]
DR Antibodypedia; 48545; 29 antibodies from 11 providers.
DR DNASU; 29100; -.
DR Ensembl; ENST00000304800.14; ENSP00000305892.9; ENSG00000168701.19. [Q9BTX3-1]
DR Ensembl; ENST00000562235.5; ENSP00000457502.1; ENSG00000168701.19. [Q9BTX3-2]
DR GeneID; 29100; -.
DR KEGG; hsa:29100; -.
DR MANE-Select; ENST00000304800.14; ENSP00000305892.9; NM_014187.4; NP_054906.2.
DR UCSC; uc002esi.3; human. [Q9BTX3-1]
DR CTD; 29100; -.
DR DisGeNET; 29100; -.
DR GeneCards; TMEM208; -.
DR HGNC; HGNC:25015; TMEM208.
DR HPA; ENSG00000168701; Low tissue specificity.
DR neXtProt; NX_Q9BTX3; -.
DR OpenTargets; ENSG00000168701; -.
DR PharmGKB; PA162406408; -.
DR VEuPathDB; HostDB:ENSG00000168701; -.
DR eggNOG; KOG3269; Eukaryota.
DR GeneTree; ENSGT00390000008139; -.
DR HOGENOM; CLU_094308_3_0_1; -.
DR InParanoid; Q9BTX3; -.
DR OMA; VFMHILA; -.
DR OrthoDB; 1407446at2759; -.
DR PhylomeDB; Q9BTX3; -.
DR TreeFam; TF318118; -.
DR PathwayCommons; Q9BTX3; -.
DR SignaLink; Q9BTX3; -.
DR BioGRID-ORCS; 29100; 55 hits in 1082 CRISPR screens.
DR ChiTaRS; TMEM208; human.
DR GenomeRNAi; 29100; -.
DR Pharos; Q9BTX3; Tdark.
DR PRO; PR:Q9BTX3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BTX3; protein.
DR Bgee; ENSG00000168701; Expressed in islet of Langerhans and 189 other tissues.
DR ExpressionAtlas; Q9BTX3; baseline and differential.
DR Genevisible; Q9BTX3; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
DR InterPro; IPR008506; SND2/TMEM208.
DR PANTHER; PTHR13505; PTHR13505; 1.
DR Pfam; PF05620; TMEM208_SND2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Autophagy; Endoplasmic reticulum;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..173
FT /note="Transmembrane protein 208"
FT /id="PRO_0000325967"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 152..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:25732826,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 101..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11042152,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032505"
FT VARIANT 82
FT /note="D -> Y (in dbSNP:rs17851038)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039958"
FT VARIANT 102
FT /note="L -> P (in dbSNP:rs11553801)"
FT /id="VAR_053933"
FT CONFLICT 90
FT /note="M -> T (in Ref. 1; AAF29134)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 173 AA; 19642 MW; F6AE0798B79967A6 CRC64;
MAPKGKVGTR GKKQIFEENR ETLKFYLRII LGANAIYCLV TLVFFYSSAS FWAWLALGFS
LAVYGASYHS MSSMARAAFS EDGALMDGGM DLNMEQGMAE HLKDVILLTA IVQVLSCFSL
YVWSFWLLAP GRALYLLWVN VLGPWFTADS GTPAPEHNEK RQRRQERRQM KRL
