ID   TM135_HUMAN             Reviewed;         458 AA.
AC   Q86UB9; Q6AW91; Q8ND01; Q9H6M3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   13-SEP-2023, entry version 130.
DE   RecName: Full=Transmembrane protein 135;
DE   AltName: Full=Peroxisomal membrane protein 52 {ECO:0000250|UniProtKB:Q9CYV5};
DE            Short=PMP52 {ECO:0000250|UniProtKB:Q9CYV5};
GN   Name=TMEM135 {ECO:0000312|HGNC:HGNC:26167};
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), AND VARIANT ARG-218.
RC   TISSUE=Endometrial adenocarcinoma, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-193
RP   AND ARG-218.
RC   TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-458 (ISOFORM 2), AND VARIANT
RP   ARG-218.
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   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=18637193; DOI=10.1186/1471-2164-9-340;
RA   Scheideler M., Elabd C., Zaragosi L.E., Chiellini C., Hackl H.,
RA   Sanchez-Cabo F., Yadav S., Duszka K., Friedl G., Papak C., Prokesch A.,
RA   Windhager R., Ailhaud G., Dani C., Amri E.Z., Trajanoski Z.;
RT   "Comparative transcriptomics of human multipotent stem cells during
RT   adipogenesis and osteoblastogenesis.";
RL   BMC Genomics 9:340-340(2008).
CC   -!- FUNCTION: Involved in mitochondrial metabolism by regulating the
CC       balance between mitochondrial fusion and fission. May act as a
CC       regulator of mitochondrial fission that promotes DNM1L-dependent
CC       fission through activation of DNM1L. May be involved in peroxisome
CC       organization. {ECO:0000250|UniProtKB:Q5U4F4,
CC       ECO:0000250|UniProtKB:Q9CYV5}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000250|UniProtKB:Q9CYV5}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9CYV5}. Peroxisome membrane
CC       {ECO:0000250|UniProtKB:Q9CYV5}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86UB9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86UB9-2; Sequence=VSP_024579;
CC   -!- DEVELOPMENTAL STAGE: Up-regulated in bone marrow-derived mesenchymal
CC       stem cells during differentiation into adipocytes compared to
CC       osteoblasts. {ECO:0000269|PubMed:18637193}.
CC   -!- SIMILARITY: Belongs to the TMEM135 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15233.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL834493; CAD39151.1; -; mRNA.
DR   EMBL; BX648678; CAH10546.1; -; mRNA.
DR   EMBL; AP000811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051462; AAH51462.2; -; mRNA.
DR   EMBL; AK025757; BAB15233.1; ALT_INIT; mRNA.
DR   CCDS; CCDS53692.1; -. [Q86UB9-2]
DR   CCDS; CCDS8280.1; -. [Q86UB9-1]
DR   RefSeq; NP_001162195.1; NM_001168724.1. [Q86UB9-2]
DR   RefSeq; NP_075069.3; NM_022918.3. [Q86UB9-1]
DR   AlphaFoldDB; Q86UB9; -.
DR   BioGRID; 122392; 9.
DR   IntAct; Q86UB9; 4.
DR   STRING; 9606.ENSP00000306344; -.
DR   GlyGen; Q86UB9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q86UB9; -.
DR   PhosphoSitePlus; Q86UB9; -.
DR   BioMuta; TMEM135; -.
DR   DMDM; 215273901; -.
DR   EPD; Q86UB9; -.
DR   jPOST; Q86UB9; -.
DR   MassIVE; Q86UB9; -.
DR   MaxQB; Q86UB9; -.
DR   PaxDb; Q86UB9; -.
DR   PeptideAtlas; Q86UB9; -.
DR   ProteomicsDB; 69795; -. [Q86UB9-1]
DR   ProteomicsDB; 69796; -. [Q86UB9-2]
DR   Antibodypedia; 31460; 54 antibodies from 19 providers.
DR   DNASU; 65084; -.
DR   Ensembl; ENST00000305494.6; ENSP00000306344.5; ENSG00000166575.17. [Q86UB9-1]
DR   Ensembl; ENST00000340353.11; ENSP00000345513.6; ENSG00000166575.17. [Q86UB9-2]
DR   GeneID; 65084; -.
DR   KEGG; hsa:65084; -.
DR   MANE-Select; ENST00000305494.6; ENSP00000306344.5; NM_022918.4; NP_075069.3.
DR   UCSC; uc001pch.4; human. [Q86UB9-1]
DR   AGR; HGNC:26167; -.
DR   CTD; 65084; -.
DR   DisGeNET; 65084; -.
DR   GeneCards; TMEM135; -.
DR   HGNC; HGNC:26167; TMEM135.
DR   HPA; ENSG00000166575; Low tissue specificity.
DR   MIM; 616360; gene.
DR   neXtProt; NX_Q86UB9; -.
DR   OpenTargets; ENSG00000166575; -.
DR   PharmGKB; PA143485658; -.
DR   VEuPathDB; HostDB:ENSG00000166575; -.
DR   eggNOG; KOG1398; Eukaryota.
DR   GeneTree; ENSGT00390000000303; -.
DR   HOGENOM; CLU_046474_0_0_1; -.
DR   InParanoid; Q86UB9; -.
DR   OMA; TDKCVNA; -.
DR   OrthoDB; 4611717at2759; -.
DR   PhylomeDB; Q86UB9; -.
DR   TreeFam; TF314580; -.
DR   PathwayCommons; Q86UB9; -.
DR   SignaLink; Q86UB9; -.
DR   BioGRID-ORCS; 65084; 9 hits in 1157 CRISPR screens.
DR   ChiTaRS; TMEM135; human.
DR   GenomeRNAi; 65084; -.
DR   Pharos; Q86UB9; Tdark.
DR   PRO; PR:Q86UB9; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q86UB9; Protein.
DR   Bgee; ENSG00000166575; Expressed in jejunal mucosa and 197 other tissues.
DR   ExpressionAtlas; Q86UB9; baseline and differential.
DR   Genevisible; Q86UB9; HS.
DR   GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR   GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR   GO; GO:0090140; P:regulation of mitochondrial fission; IEA:Ensembl.
DR   GO; GO:0002082; P:regulation of oxidative phosphorylation; IEA:Ensembl.
DR   GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR   GO; GO:0032094; P:response to food; IEA:Ensembl.
DR   GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR   InterPro; IPR026749; Tmem135.
DR   InterPro; IPR031926; TMEM135_N.
DR   PANTHER; PTHR12459:SF6; TRANSMEMBRANE PROTEIN 135; 1.
DR   PANTHER; PTHR12459; UNCHARACTERIZED; 1.
DR   Pfam; PF02466; Tim17; 1.
DR   Pfam; PF15982; TMEM135_C_rich; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Mitochondrion; Peroxisome;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..458
FT                   /note="Transmembrane protein 135"
FT                   /id="PRO_0000284622"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         133..154
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_024579"
FT   VARIANT         193
FT                   /note="P -> H (in dbSNP:rs17854687)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_031787"
FT   VARIANT         218
FT                   /note="G -> R (in dbSNP:rs2276102)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT                   /id="VAR_031788"
FT   VARIANT         430
FT                   /note="G -> A (in dbSNP:rs11235097)"
FT                   /id="VAR_031789"
FT   CONFLICT        339
FT                   /note="I -> T (in Ref. 4; BAB15233)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   458 AA;  52291 MW;  B6BDEC84237D5FE2 CRC64;
     MAALSKSIPH NCYEIGHTWH PSCRVSFLQI TGGALEESLK IYAPLYLIAA ILRKRKLDYY
     LHKLLPEILQ SASFLTANGA LYMAFFCILR KILGKFYSWT PGFGAALPAS YVAILIERKS
     RRGLLTIYMA NLATETLFRM GVARGTITTL RNGEVLLFCI TAAMYMFFFR CKDGLKGFTF
     SALRFIVGKE EIPTHSFSPE AAYAKVEQKR EQHEEKPGRM NMIGLVRKFV DSICKHGPRH
     RCCKHYEDNC ISYCIKGFIR MFSVGYLIQC CLRIPSAFRH LFTQPSRLLS LFYNKENFQL
     GAFLGSFVSI YKGTSCFLRW IRNLDDELHA IIAGFLAGIS MMFYKSTTIS MYLASKLVET
     MYFKGIEAGK VPYFPHADTI IYSISTAICF QAAVMEVQTL RPSYWKFLLR LTKGKFAVMN
     RKVLDVFGTG ASKHFQDFIP RLDPRYTTVT PELPTEFS
//