TMM11_HUMAN
ID TMM11_HUMAN Reviewed; 192 AA.
AC P17152; Q53YB2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Transmembrane protein 11, mitochondrial;
DE AltName: Full=Protein PM1;
DE AltName: Full=Protein PMI;
GN Name=TMEM11; Synonyms=C17orf35, PM1;
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].
RX PubMed=2110658; DOI=10.1093/nar/18.7.1896;
RA Murphy P.M., Malech H.L.;
RT "Nucleotide sequence of a cDNA encoding a protein with primary structural
RT similarity to G-protein coupled receptors.";
RL Nucleic Acids Res. 18:1896-1896(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Placenta, and Prostate;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21274005; DOI=10.1038/embor.2010.214;
RA Rival T., Macchi M., Arnaune-Pelloquin L., Poidevin M., Maillet F.,
RA Richard F., Fatmi A., Belenguer P., Royet J.;
RT "Inner-membrane proteins PMI/TMEM11 regulate mitochondrial morphogenesis
RT independently of the DRP1/MFN fission/fusion pathways.";
RL EMBO Rep. 12:223-230(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [10]
RP IDENTIFICATION BY 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).
RN [11]
RP INTERACTION WITH THE MICOS COMPLEX, AND INTERACTION WITH IMMT.
RX PubMed=25997101; DOI=10.7554/elife.06265;
RA Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA Gygi S.P., Van Vactor D., Harper J.W.;
RT "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT and cristae morphology.";
RL Elife 4:0-0(2015).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Plays a role in mitochondrial morphogenesis.
CC {ECO:0000269|PubMed:21274005}.
CC -!- SUBUNIT: Associates with the mitochondrial contact site and cristae
CC organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC and QIL1/MIC13. This complex was also known under the names MINOS or
CC MitOS complex. The MICOS complex associates with mitochondrial outer
CC membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner
CC membrane protein TMEM11 and with HSPA9. Interacts with IMMT/MIC60.
CC {ECO:0000269|PubMed:25997101}.
CC -!- INTERACTION:
CC P17152; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-723946, EBI-11343438;
CC P17152; Q13323: BIK; NbExp=3; IntAct=EBI-723946, EBI-700794;
CC P17152; Q12983: BNIP3; NbExp=11; IntAct=EBI-723946, EBI-749464;
CC P17152; O60238: BNIP3L; NbExp=9; IntAct=EBI-723946, EBI-849893;
CC P17152; Q6NSX1: CCDC70; NbExp=3; IntAct=EBI-723946, EBI-6873045;
CC P17152; P11912: CD79A; NbExp=3; IntAct=EBI-723946, EBI-7797864;
CC P17152; O95471: CLDN7; NbExp=3; IntAct=EBI-723946, EBI-740744;
CC P17152; Q96BA8: CREB3L1; NbExp=6; IntAct=EBI-723946, EBI-6942903;
CC P17152; P49447: CYB561; NbExp=3; IntAct=EBI-723946, EBI-8646596;
CC P17152; Q8WUJ1: CYB5D2; NbExp=3; IntAct=EBI-723946, EBI-19113794;
CC P17152; Q15125: EBP; NbExp=3; IntAct=EBI-723946, EBI-3915253;
CC P17152; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-723946, EBI-18535450;
CC P17152; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-723946, EBI-18636064;
CC P17152; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-723946, EBI-18304435;
CC P17152; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-723946, EBI-18938272;
CC P17152; Q969F0: FATE1; NbExp=4; IntAct=EBI-723946, EBI-743099;
CC P17152; O15552: FFAR2; NbExp=3; IntAct=EBI-723946, EBI-2833872;
CC P17152; Q9NTQ9: GJB4; NbExp=3; IntAct=EBI-723946, EBI-12831526;
CC P17152; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-723946, EBI-3917143;
CC P17152; Q8N6L0: KASH5; NbExp=5; IntAct=EBI-723946, EBI-749265;
CC P17152; O95214: LEPROTL1; NbExp=3; IntAct=EBI-723946, EBI-750776;
CC P17152; Q6IN84: MRM1; NbExp=3; IntAct=EBI-723946, EBI-5454865;
CC P17152; Q15800: MSMO1; NbExp=3; IntAct=EBI-723946, EBI-949102;
CC P17152; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-723946, EBI-3923617;
CC P17152; P15941-11: MUC1; NbExp=3; IntAct=EBI-723946, EBI-17263240;
CC P17152; O75489: NDUFS3; NbExp=3; IntAct=EBI-723946, EBI-1224896;
CC P17152; P32243-2: OTX2; NbExp=3; IntAct=EBI-723946, EBI-9087860;
CC P17152; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-723946, EBI-716063;
CC P17152; O00623: PEX12; NbExp=3; IntAct=EBI-723946, EBI-594836;
CC P17152; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-723946, EBI-10192441;
CC P17152; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-723946, EBI-12375429;
CC P17152; O60930: RNASEH1; NbExp=3; IntAct=EBI-723946, EBI-2372399;
CC P17152; Q16585: SGCB; NbExp=3; IntAct=EBI-723946, EBI-5663627;
CC P17152; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-723946, EBI-18159983;
CC P17152; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-723946, EBI-10262251;
CC P17152; Q96L08: SUSD3; NbExp=3; IntAct=EBI-723946, EBI-18194029;
CC P17152; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-723946, EBI-19027521;
CC P17152; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-723946, EBI-2821497;
CC P17152; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-723946, EBI-8638294;
CC P17152; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-723946, EBI-6269551;
CC P17152; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-723946, EBI-10982110;
CC P17152; Q6PEY1: TMEM88; NbExp=3; IntAct=EBI-723946, EBI-17198826;
CC P17152; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-723946, EBI-12345267;
CC P17152; O43557: TNFSF14; NbExp=3; IntAct=EBI-723946, EBI-524131;
CC P17152; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-723946, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21274005}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21274005}.
CC -!- SIMILARITY: Belongs to the TMEM11 family. {ECO:0000305}.
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DR EMBL; X51804; CAA36102.1; -; mRNA.
DR EMBL; AK311965; BAG34905.1; -; mRNA.
DR EMBL; BT006768; AAP35414.1; -; mRNA.
DR EMBL; AC087294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471210; EAX02598.1; -; Genomic_DNA.
DR EMBL; BC002819; AAH02819.1; -; mRNA.
DR EMBL; BC005268; AAH05268.1; -; mRNA.
DR EMBL; BC020815; AAH20815.1; -; mRNA.
DR CCDS; CCDS11216.1; -.
DR PIR; S15930; S15930.
DR RefSeq; NP_003867.1; NM_003876.2.
DR AlphaFoldDB; P17152; -.
DR BioGRID; 114361; 99.
DR IntAct; P17152; 77.
DR MINT; P17152; -.
DR STRING; 9606.ENSP00000319992; -.
DR iPTMnet; P17152; -.
DR PhosphoSitePlus; P17152; -.
DR SwissPalm; P17152; -.
DR BioMuta; TMEM11; -.
DR EPD; P17152; -.
DR jPOST; P17152; -.
DR MassIVE; P17152; -.
DR MaxQB; P17152; -.
DR PaxDb; P17152; -.
DR PeptideAtlas; P17152; -.
DR PRIDE; P17152; -.
DR ProteomicsDB; 53458; -.
DR TopDownProteomics; P17152; -.
DR Antibodypedia; 26137; 67 antibodies from 16 providers.
DR DNASU; 8834; -.
DR Ensembl; ENST00000317635.6; ENSP00000319992.6; ENSG00000178307.10.
DR GeneID; 8834; -.
DR KEGG; hsa:8834; -.
DR MANE-Select; ENST00000317635.6; ENSP00000319992.6; NM_003876.3; NP_003867.1.
DR UCSC; uc002gyp.3; human.
DR CTD; 8834; -.
DR DisGeNET; 8834; -.
DR GeneCards; TMEM11; -.
DR HGNC; HGNC:16823; TMEM11.
DR HPA; ENSG00000178307; Tissue enhanced (skeletal).
DR MIM; 618817; gene.
DR neXtProt; NX_P17152; -.
DR OpenTargets; ENSG00000178307; -.
DR PharmGKB; PA134893886; -.
DR VEuPathDB; HostDB:ENSG00000178307; -.
DR eggNOG; ENOG502QUAI; Eukaryota.
DR GeneTree; ENSGT00390000006617; -.
DR HOGENOM; CLU_095460_0_0_1; -.
DR InParanoid; P17152; -.
DR OMA; LYTVSWQ; -.
DR OrthoDB; 1222072at2759; -.
DR PhylomeDB; P17152; -.
DR TreeFam; TF324685; -.
DR PathwayCommons; P17152; -.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; P17152; -.
DR BioGRID-ORCS; 8834; 30 hits in 1086 CRISPR screens.
DR ChiTaRS; TMEM11; human.
DR GenomeRNAi; 8834; -.
DR Pharos; P17152; Tbio.
DR PRO; PR:P17152; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P17152; protein.
DR Bgee; ENSG00000178307; Expressed in hindlimb stylopod muscle and 197 other tissues.
DR Genevisible; P17152; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR InterPro; IPR026120; TMEM11.
DR PANTHER; PTHR15099; PTHR15099; 1.
DR Pfam; PF14972; Mito_morph_reg; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..192
FT /note="Transmembrane protein 11, mitochondrial"
FT /id="PRO_0000072562"
FT TRANSMEM 84..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 192 AA; 21541 MW; FE46BACEBF5ACD1D CRC64;
MAAWGRRRLG PGSSGGSARE RVSLSATDCY IVHEIYNGEN AQDQFEYELE QALEAQYKYI
VIEPTRIGDE TARWITVGNC LHKTAVLAGT ACLFTPLALP LDYSHYISLP AGVLSLACCT
LYGISWQFDP CCKYQVEYDA YKLSRLPLHT LTSSTPVVLV RKDDLHRKRL HNTIALAALV
YCVKKIYELY AV
