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   27-MAR-2024, entry version 137.
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; 53.
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; 9606-ENSP00000305892; -.
DR   PeptideAtlas; Q9BTX3; -.
DR   ProteomicsDB; 79025; -. [Q9BTX3-1]
DR   ProteomicsDB; 79026; -. [Q9BTX3-2]
DR   Pumba; Q9BTX3; -.
DR   TopDownProteomics; Q9BTX3-1; -. [Q9BTX3-1]
DR   Antibodypedia; 48545; 40 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   AGR; HGNC:25015; -.
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; PIRAGWM; -.
DR   OrthoDB; 2908595at2759; -.
DR   PhylomeDB; Q9BTX3; -.
DR   TreeFam; TF318118; -.
DR   PathwayCommons; Q9BTX3; -.
DR   SignaLink; Q9BTX3; -.
DR   BioGRID-ORCS; 29100; 56 hits in 1158 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 191 other cell types or tissues.
DR   ExpressionAtlas; Q9BTX3; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; TRANSMEMBRANE PROTEIN 208; 1.
DR   PANTHER; PTHR13505:SF7; TRANSMEMBRANE PROTEIN 208; 1.
DR   Pfam; PF05620; TMEM208_SND2; 1.
DR   Genevisible; Q9BTX3; HS.
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
//