TM177_HUMAN
ID TM177_HUMAN Reviewed; 311 AA.
AC Q53S58; Q9BT20;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Transmembrane protein 177;
GN Name=TMEM177;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-32 AND GLU-267.
RC TISSUE=Placenta;
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 FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, IDENTIFICATION IN A COMPLEX WITH
RP COX20; COA6; MT-CO2; COX18; SCO1 AND SCO2, AND INTERACTION WITH COX20;
RP COX1; MT-CO2; SCO1 AND SCO2.
RX PubMed=29154948; DOI=10.1016/j.bbamcr.2017.11.010;
RA Lorenzi I., Oeljeklaus S., Aich A., Ronsoer C., Callegari S., Dudek J.,
RA Warscheid B., Dennerlein S., Rehling P.;
RT "The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.";
RL Biochim. Biophys. Acta 1865:323-333(2017).
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:0000269|PubMed:29154948}.
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:0000269|PubMed:29154948}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:29154948}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TMEM177 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC069154; AAY24148.1; -; Genomic_DNA.
DR EMBL; BC004404; AAH04404.1; -; mRNA.
DR CCDS; CCDS2128.1; -.
DR RefSeq; NP_001098668.1; NM_001105198.1.
DR RefSeq; NP_001098669.1; NM_001105199.1.
DR RefSeq; NP_085054.2; NM_030577.2.
DR AlphaFoldDB; Q53S58; -.
DR BioGRID; 123307; 47.
DR IntAct; Q53S58; 6.
DR STRING; 9606.ENSP00000402661; -.
DR iPTMnet; Q53S58; -.
DR PhosphoSitePlus; Q53S58; -.
DR BioMuta; TMEM177; -.
DR DMDM; 74727288; -.
DR EPD; Q53S58; -.
DR jPOST; Q53S58; -.
DR MassIVE; Q53S58; -.
DR MaxQB; Q53S58; -.
DR PaxDb; Q53S58; -.
DR PeptideAtlas; Q53S58; -.
DR PRIDE; Q53S58; -.
DR ProteomicsDB; 62533; -.
DR Antibodypedia; 58266; 62 antibodies from 14 providers.
DR DNASU; 80775; -.
DR Ensembl; ENST00000272521.7; ENSP00000272521.6; ENSG00000144120.13.
DR Ensembl; ENST00000401466.5; ENSP00000385966.1; ENSG00000144120.13.
DR Ensembl; ENST00000424086.5; ENSP00000402661.1; ENSG00000144120.13.
DR GeneID; 80775; -.
DR KEGG; hsa:80775; -.
DR MANE-Select; ENST00000272521.7; ENSP00000272521.6; NM_030577.3; NP_085054.2.
DR UCSC; uc002tmc.1; human.
DR CTD; 80775; -.
DR DisGeNET; 80775; -.
DR GeneCards; TMEM177; -.
DR HGNC; HGNC:28143; TMEM177.
DR HPA; ENSG00000144120; Low tissue specificity.
DR neXtProt; NX_Q53S58; -.
DR OpenTargets; ENSG00000144120; -.
DR PharmGKB; PA162405985; -.
DR VEuPathDB; HostDB:ENSG00000144120; -.
DR eggNOG; ENOG502QPPU; Eukaryota.
DR GeneTree; ENSGT00390000010354; -.
DR HOGENOM; CLU_074208_0_0_1; -.
DR InParanoid; Q53S58; -.
DR OMA; HTFGLKY; -.
DR OrthoDB; 1039066at2759; -.
DR PhylomeDB; Q53S58; -.
DR TreeFam; TF328369; -.
DR PathwayCommons; Q53S58; -.
DR SignaLink; Q53S58; -.
DR BioGRID-ORCS; 80775; 11 hits in 1081 CRISPR screens.
DR ChiTaRS; TMEM177; human.
DR GenomeRNAi; 80775; -.
DR Pharos; Q53S58; Tdark.
DR PRO; PR:Q53S58; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53S58; protein.
DR Bgee; ENSG00000144120; Expressed in mucosa of transverse colon and 148 other tissues.
DR ExpressionAtlas; Q53S58; baseline and differential.
DR Genevisible; Q53S58; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA: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_0000282646"
FT TOPO_DOM 1..17
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:29154948"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..166
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:29154948"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..197
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:29154948"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..311
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:29154948"
FT VARIANT 29
FT /note="G -> A (in dbSNP:rs11684353)"
FT /id="VAR_031421"
FT VARIANT 32
FT /note="I -> V (in dbSNP:rs13011768)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031422"
FT VARIANT 267
FT /note="D -> E (in dbSNP:rs1983406)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031423"
SQ SEQUENCE 311 AA; 33760 MW; FC9697323D148426 CRC64;
MAGPLWRTAA FVQRHRTGLL VGSCAGLFGV PISYHLFPDP VVQWLYQYWP QGQPAPLPPQ
LQSLFQEVLQ DIGVPSGHCY KPFTTFTFQP VSAGFPRLPA GAVVGIPASF LGDLVINTNH
PVVIHGHTVD WRSPAGARLR ASLTLSREAQ KFALAREVVY LESSTTAVHA LLAPACLAGT
WALGVGAKYT LGLHAGPMNL RAAFSLVAAV AGFVAYAFSQ DSLTHAVESW LDRRTASLSA
AYACGGVEFY EKLLSGNLAL RSLLGKDGEK LYTPSGNIVP RHLFRIKHLP YTTRRDSVLQ
MWRGMLNPGR S
