TM115_HUMAN
ID TM115_HUMAN Reviewed; 351 AA.
AC Q12893; A2IDB7; O14568; Q6IAY4; Q9UIX3;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Transmembrane protein 115 {ECO:0000305};
DE AltName: Full=Placental protein 6 {ECO:0000305};
DE AltName: Full=Protein PL6 {ECO:0000305};
GN Name=TMEM115 {ECO:0000312|HGNC:HGNC:30055};
GN Synonyms=PL6 {ECO:0000312|EMBL:AAA92281.1}; ORFNames=LUCA11.2;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11085536;
RG The international lung cancer chromosome 3p21.3 tumor suppressor gene consortium;
RA Lerman M.I., Minna J.D.;
RT "The 630-kb lung cancer homozygous deletion region on human chromosome
RT 3p21.3: identification and evaluation of the resident candidate tumor
RT suppressor genes.";
RL Cancer Res. 60:6116-6133(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17973242; DOI=10.1002/path.2252;
RA Ivanova A.V., Vortmeyer A., Ivanov S.V., Nickerson M.L., Maher E.R.,
RA Lerman M.I.;
RT "Loss of PL6 protein expression in renal clear cell carcinomas and other
RT VHL-deficient tumours.";
RL J. Pathol. 214:46-57(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-329, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COPB1; LMAN1; COG3,
RP HOMOOLIGOMERIZATION, REGION, AND TOPOLOGY.
RX PubMed=24806965; DOI=10.1242/jcs.136754;
RA Ong Y.S., Tran T.H., Gounko N.V., Hong W.;
RT "TMEM115 is an integral membrane protein of the Golgi complex involved in
RT retrograde transport.";
RL J. Cell Sci. 127:2825-2839(2014).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-329, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play a role in retrograde transport of proteins from the
CC Golgi to the endoplasmic reticulum. May indirectly play a role in
CC protein glycosylation in the Golgi. {ECO:0000269|PubMed:24806965}.
CC -!- SUBUNIT: Homooligomer (PubMed:24806965). Interacts with COPB1
CC (PubMed:24806965). May interact with LMAN1 (PubMed:24806965). Interacts
CC with the COG complex; probably through COG3 (PubMed:24806965).
CC {ECO:0000269|PubMed:24806965}.
CC -!- INTERACTION:
CC Q12893; Q13520: AQP6; NbExp=3; IntAct=EBI-8633987, EBI-13059134;
CC Q12893; Q86U10: ASPG; NbExp=3; IntAct=EBI-8633987, EBI-19946665;
CC Q12893; P00387: CYB5R3; NbExp=3; IntAct=EBI-8633987, EBI-1046040;
CC Q12893; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-8633987, EBI-12937691;
CC Q12893; P42858: HTT; NbExp=3; IntAct=EBI-8633987, EBI-466029;
CC Q12893; P13473-2: LAMP2; NbExp=3; IntAct=EBI-8633987, EBI-21591415;
CC Q12893; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-8633987, EBI-3867271;
CC Q12893; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-8633987, EBI-712367;
CC Q12893; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-8633987, EBI-2623095;
CC Q12893; Q8N205: SYNE4; NbExp=3; IntAct=EBI-8633987, EBI-7131783;
CC Q12893; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-8633987, EBI-12947623;
CC Q12893; Q6PL24: TMED8; NbExp=3; IntAct=EBI-8633987, EBI-11603430;
CC Q12893; Q9Y320: TMX2; NbExp=3; IntAct=EBI-8633987, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:17973242, ECO:0000269|PubMed:24806965}; Multi-pass
CC membrane protein {ECO:0000303|PubMed:24806965}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in kidney and skeletal muscle,
CC followed by liver, placenta, pancreas, and lung, with low amounts in
CC heart and only traces in brain (PubMed:11085536). Widely expressed with
CC ubiquitous expression in epithelial tissues (at protein level)
CC (PubMed:17973242). {ECO:0000269|PubMed:11085536,
CC ECO:0000269|PubMed:17973242}.
CC -!- SIMILARITY: Belongs to the TMEM115 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67308.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U09584; AAA92281.1; -; mRNA.
DR EMBL; CR457020; CAG33301.1; -; mRNA.
DR EMBL; AC002481; AAB67308.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z84492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65115.1; -; Genomic_DNA.
DR EMBL; BC011948; AAH11948.1; -; mRNA.
DR EMBL; BC017367; AAH17367.1; -; mRNA.
DR CCDS; CCDS2828.1; -.
DR PIR; G01430; G01430.
DR RefSeq; NP_008955.1; NM_007024.4.
DR AlphaFoldDB; Q12893; -.
DR BioGRID; 116254; 44.
DR IntAct; Q12893; 23.
DR MINT; Q12893; -.
DR STRING; 9606.ENSP00000266025; -.
DR iPTMnet; Q12893; -.
DR PhosphoSitePlus; Q12893; -.
DR SwissPalm; Q12893; -.
DR BioMuta; TMEM115; -.
DR DMDM; 24638130; -.
DR EPD; Q12893; -.
DR jPOST; Q12893; -.
DR MassIVE; Q12893; -.
DR MaxQB; Q12893; -.
DR PaxDb; Q12893; -.
DR PeptideAtlas; Q12893; -.
DR PRIDE; Q12893; -.
DR ProteomicsDB; 59007; -.
DR Antibodypedia; 3346; 117 antibodies from 20 providers.
DR DNASU; 11070; -.
DR Ensembl; ENST00000266025.4; ENSP00000266025.3; ENSG00000126062.4.
DR GeneID; 11070; -.
DR KEGG; hsa:11070; -.
DR MANE-Select; ENST00000266025.4; ENSP00000266025.3; NM_007024.5; NP_008955.1.
DR UCSC; uc003dan.2; human.
DR CTD; 11070; -.
DR DisGeNET; 11070; -.
DR GeneCards; TMEM115; -.
DR HGNC; HGNC:30055; TMEM115.
DR HPA; ENSG00000126062; Low tissue specificity.
DR MIM; 607069; gene.
DR neXtProt; NX_Q12893; -.
DR OpenTargets; ENSG00000126062; -.
DR PharmGKB; PA143485636; -.
DR VEuPathDB; HostDB:ENSG00000126062; -.
DR eggNOG; KOG2890; Eukaryota.
DR GeneTree; ENSGT00390000002470; -.
DR HOGENOM; CLU_043563_2_0_1; -.
DR InParanoid; Q12893; -.
DR OMA; FACLFPD; -.
DR OrthoDB; 1156492at2759; -.
DR PhylomeDB; Q12893; -.
DR TreeFam; TF315100; -.
DR PathwayCommons; Q12893; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; Q12893; -.
DR BioGRID-ORCS; 11070; 16 hits in 1084 CRISPR screens.
DR GenomeRNAi; 11070; -.
DR Pharos; Q12893; Tbio.
DR PRO; PR:Q12893; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q12893; protein.
DR Bgee; ENSG00000126062; Expressed in stromal cell of endometrium and 194 other tissues.
DR ExpressionAtlas; Q12893; baseline and differential.
DR Genevisible; Q12893; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR013861; TMEM115/Pdh1/Rbl19.
DR PANTHER; PTHR13377; PTHR13377; 1.
DR Pfam; PF08551; DUF1751; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..351
FT /note="Transmembrane protein 115"
FT /id="PRO_0000058451"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..97
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 98..118
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..165
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24806965"
FT REGION 1..205
FT /note="Mediates homooligomerization"
FT /evidence="ECO:0000269|PubMed:24806965"
FT REGION 206..229
FT /note="Mediates localization to the Golgi"
FT /evidence="ECO:0000269|PubMed:24806965"
FT REGION 301..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
SQ SEQUENCE 351 AA; 38197 MW; 8CFBF66322FDEEFC CRC64;
MQRALPGARQ HLGAILASAS VVVKALCAAV LFLYLLSFAV DTGCLAVTPG YLFPPNFWIW
TLATHGLMEQ HVWDVAISLT TVVVAGRLLE PLWGALELLI FFSVVNVSVG LLGAFAYLLT
YMASFNLVYL FTVRIHGALG FLGGVLVALK QTMGDCVVLR VPQVRVSVMP MLLLALLLLL
RLATLLQSPA LASYGFGLLS SWVYLRFYQR HSRGRGDMAD HFAFATFFPE ILQPVVGLLA
NLVHSLLVKV KICQKTVKRY DVGAPSSITI SLPGTDPQDA ERRRQLALKA LNERLKRVED
QSIWPSMDDD EEESGAKVDS PLPSDKAPTP PGKGAAPESS LITFEAAPPT L
