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TM242_MOUSE
ID   TM242_MOUSE             Reviewed;         140 AA.
AC   Q8VCR3; Q8C2T2; Q8CEX9; Q9CYJ2; Q9D1H4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Transmembrane protein 242 {ECO:0000305};
GN   Name=Tmem242 {ECO:0000312|MGI:MGI:1917794};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Inner ear, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
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).
CC   -!- FUNCTION: Scaffold protein that participates in the c-ring assembly of
CC       mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by
CC       facilitating the membrane insertion and oligomer formation of the
CC       subunit c/ATP5MC3. Participates in the incorporation of the c-ring into
CC       vestigial complexes. Additionally influences the incorporation of
CC       subunits MT-ATP6, MT-ATP8, ATP5MJ, and ATP5MK in the ATP synthase.
CC       {ECO:0000250|UniProtKB:Q9NWH2}.
CC   -!- SUBUNIT: Interacts with the core subunits NDUFAF1, ECSIT and ACAD9 of
CC       the MCIA complex. Interacts with ATP5MC3, NDUFC2, TMEM70, MT-ND2 AND
CC       MT-ND3. {ECO:0000250|UniProtKB:Q9NWH2}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9NWH2}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9NWH2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VCR3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VCR3-2; Sequence=VSP_027110;
CC       Name=3;
CC         IsoId=Q8VCR3-3; Sequence=VSP_027111, VSP_027112;
CC   -!- SIMILARITY: Belongs to the TMEM242 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25272.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK003559; BAB22856.1; -; mRNA.
DR   EMBL; AK009851; BAC25272.1; ALT_FRAME; mRNA.
DR   EMBL; AK017626; BAB30845.1; -; mRNA.
DR   EMBL; AK088025; BAC40103.1; -; mRNA.
DR   EMBL; AK155326; BAE33193.1; -; mRNA.
DR   EMBL; AK158107; BAE34359.1; -; mRNA.
DR   EMBL; BC019420; AAH19420.1; -; mRNA.
DR   CCDS; CCDS49930.1; -. [Q8VCR3-1]
DR   RefSeq; NP_081733.3; NM_027457.4. [Q8VCR3-1]
DR   AlphaFoldDB; Q8VCR3; -.
DR   SMR; Q8VCR3; -.
DR   STRING; 10090.ENSMUSP00000005053; -.
DR   PhosphoSitePlus; Q8VCR3; -.
DR   EPD; Q8VCR3; -.
DR   PaxDb; Q8VCR3; -.
DR   PeptideAtlas; Q8VCR3; -.
DR   PRIDE; Q8VCR3; -.
DR   ProteomicsDB; 259414; -. [Q8VCR3-1]
DR   ProteomicsDB; 259415; -. [Q8VCR3-2]
DR   ProteomicsDB; 259416; -. [Q8VCR3-3]
DR   Antibodypedia; 49845; 43 antibodies from 8 providers.
DR   DNASU; 70544; -.
DR   Ensembl; ENSMUST00000005053; ENSMUSP00000005053; ENSMUSG00000004945. [Q8VCR3-1]
DR   Ensembl; ENSMUST00000185896; ENSMUSP00000139712; ENSMUSG00000004945. [Q8VCR3-2]
DR   Ensembl; ENSMUST00000188282; ENSMUSP00000139629; ENSMUSG00000004945. [Q8VCR3-3]
DR   GeneID; 70544; -.
DR   KEGG; mmu:70544; -.
DR   UCSC; uc008afa.1; mouse. [Q8VCR3-1]
DR   UCSC; uc008afc.1; mouse. [Q8VCR3-3]
DR   UCSC; uc008afd.1; mouse. [Q8VCR3-2]
DR   CTD; 729515; -.
DR   MGI; MGI:1917794; Tmem242.
DR   VEuPathDB; HostDB:ENSMUSG00000004945; -.
DR   eggNOG; ENOG502S2GB; Eukaryota.
DR   GeneTree; ENSGT00390000008642; -.
DR   HOGENOM; CLU_115460_0_0_1; -.
DR   InParanoid; Q8VCR3; -.
DR   OMA; YAVMGTG; -.
DR   OrthoDB; 1365284at2759; -.
DR   PhylomeDB; Q8VCR3; -.
DR   TreeFam; TF323317; -.
DR   BioGRID-ORCS; 70544; 10 hits in 74 CRISPR screens.
DR   ChiTaRS; Tmem242; mouse.
DR   PRO; PR:Q8VCR3; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8VCR3; protein.
DR   Bgee; ENSMUSG00000004945; Expressed in hindlimb stylopod muscle and 246 other tissues.
DR   Genevisible; Q8VCR3; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR   GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; ISO:MGI.
DR   InterPro; IPR009792; TMEM242.
DR   PANTHER; PTHR13141; PTHR13141; 1.
DR   Pfam; PF07096; DUF1358; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..140
FT                   /note="Transmembrane protein 242"
FT                   /id="PRO_0000295849"
FT   TOPO_DOM        1..28
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..80
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..140
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NWH2"
FT   VAR_SEQ         109..140
FT                   /note="MKDFRSKMQSIFPPIPKNHESAEEWEEVLKWK -> VSTSPCESCLSTLCCL
FT                   KFLVFKFAYILVPVF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027110"
FT   VAR_SEQ         109..118
FT                   /note="MKDFRSKMQS -> ALFDCREETR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027111"
FT   VAR_SEQ         119..140
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027112"
FT   CONFLICT        18
FT                   /note="G -> R (in Ref. 1; BAC40103/BAE33193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="H -> R (in Ref. 1; BAC40103/BAE33193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  14916 MW;  AF42EC70C1AED3D8 CRC64;
     METSGPGPGE SSELEAPGSP DDRLFLVKGG IFLGSAAAAG MLAGFVTTLS LAKKKSPEWF
     NKGTMATAAL PESGSSLALR ALGWGSLYAW CGVGVISFAV WKALGVHSMK DFRSKMQSIF
     PPIPKNHESA EEWEEVLKWK
 
 
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