TM177_MOUSE
ID TM177_MOUSE Reviewed; 311 AA.
AC Q8BPE4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Transmembrane protein 177;
GN Name=Tmem177;
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].
RC STRAIN=C57BL/6J;
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].
RC STRAIN=C57BL/6J; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in the early steps of cytochrome c oxidase
CC subunit II (MT-CO2/COX2) maturation and is required for the
CC stabilization of COX20 and the newly synthesized MT-CO2/COX2 protein.
CC {ECO:0000250|UniProtKB:Q53S58}.
CC -!- SUBUNIT: Found in a complex with COX20, COA6, MT-CO2/COX2, COX18, SCO1
CC and SCO2. Interacts with COX20. Interacts with COX1, MT-CO2/COX2, SCO1
CC and SCO2 in a COX20-dependent manner. {ECO:0000250|UniProtKB:Q53S58}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q53S58}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TMEM177 family. {ECO:0000305}.
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DR EMBL; AK076108; BAC36188.1; -; mRNA.
DR EMBL; BC094344; AAH94344.1; -; mRNA.
DR EMBL; BC131993; AAI31994.1; -; mRNA.
DR EMBL; BC132021; AAI32022.1; -; mRNA.
DR CCDS; CCDS15228.1; -.
DR RefSeq; NP_780315.1; NM_175106.3.
DR AlphaFoldDB; Q8BPE4; -.
DR BioGRID; 211399; 1.
DR STRING; 10090.ENSMUSP00000042416; -.
DR iPTMnet; Q8BPE4; -.
DR PhosphoSitePlus; Q8BPE4; -.
DR EPD; Q8BPE4; -.
DR jPOST; Q8BPE4; -.
DR MaxQB; Q8BPE4; -.
DR PaxDb; Q8BPE4; -.
DR PeptideAtlas; Q8BPE4; -.
DR PRIDE; Q8BPE4; -.
DR ProteomicsDB; 259541; -.
DR Antibodypedia; 58266; 62 antibodies from 14 providers.
DR DNASU; 66343; -.
DR Ensembl; ENSMUST00000037906; ENSMUSP00000042416; ENSMUSG00000036975.
DR GeneID; 66343; -.
DR KEGG; mmu:66343; -.
DR UCSC; uc007cja.2; mouse.
DR CTD; 80775; -.
DR MGI; MGI:1913593; Tmem177.
DR VEuPathDB; HostDB:ENSMUSG00000036975; -.
DR eggNOG; ENOG502QPPU; Eukaryota.
DR GeneTree; ENSGT00390000010354; -.
DR HOGENOM; CLU_074208_0_0_1; -.
DR InParanoid; Q8BPE4; -.
DR OMA; HTFGLKY; -.
DR OrthoDB; 1039066at2759; -.
DR PhylomeDB; Q8BPE4; -.
DR TreeFam; TF328369; -.
DR BioGRID-ORCS; 66343; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8BPE4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BPE4; protein.
DR Bgee; ENSMUSG00000036975; Expressed in interventricular septum and 172 other tissues.
DR Genevisible; Q8BPE4; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR InterPro; IPR026620; TMEM177.
DR PANTHER; PTHR21824; PTHR21824; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="Transmembrane protein 177"
FT /id="PRO_0000282647"
FT TOPO_DOM 1..17
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..164
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..190
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..311
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34067 MW; 7DB7E30C29866F76 CRC64;
MAGPLWRAAA FIQRHRTSLL VGSCAGLFGV QISFHLFPDP IVQWLYQYWP QGQPAPLSPH
LWSLFQEVLK DIGVPSGHCY KPFTAFTFQP VSAGFPRLPA GAVVGIPAIF LGGPVTNIEH
SVIIHGQRVD WQSPAGTRLR DALTMSHNAQ KFALAKEVVY LESGVAALQT LPAPACLAGT
WAISVGAKHA LGLYGGPMSL RTAFNLVAIV VGYVAYTFSK DSLTLALEGW LDRRTASLSA
AYVQGGVEFY EKILSGNLAL RSLLGRQGEK LYTPSGNIVP RHWFRINHLP YTTRRDSLQQ
MWRATVSPGR F
