ID   TM164_MOUSE             Reviewed;         296 AA.
AC   Q6PHN7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 116.
DE   RecName: Full=Transmembrane protein 164;
DE   AltName: Full=Arachidonoyl ether phospholipid synthase;
GN   Name=Tmem164;
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   TISSUE=Lung;
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=Lung;
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: Positive regulator of ferroptosis. Involved in the acylation
CC       of ether lysophospholipids with the arachidonoyl chain (5Z,8Z,11Z,14Z-
CC       eicosatetraenoyl; C20:4) of diacylglycerophospholipids, generating
CC       C20:4 ether glycerophospholipids (ePEs) such as 1-(1Z-octadecenyl)-2-
CC       (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine (PE
CC       (P-18:0/20:4)), which promotes ferroptosis. Selectively mediates ATG5-
CC       dependent autophagosome formation during ferroptosis, rather than
CC       during starvation, and regulates the degradation of ferritin, GPX4 and
CC       lipid droplets to increase iron accumulation and lipid peroxidation,
CC       thereby promoting ferroptotic cell death.
CC       {ECO:0000250|UniProtKB:Q5U3C3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(1Z-octadecenyl)-sn-glycero-3-phosphoethanolamine + 1-
CC         octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC         phosphocholine = 1-(1Z-octadecenyl)-2-
CC         (5Z,8Z,11Z,14Z- eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine +
CC         1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:79431,
CC         ChEBI:CHEBI:73858, ChEBI:CHEBI:74965, ChEBI:CHEBI:78342,
CC         ChEBI:CHEBI:229972; Evidence={ECO:0000250|UniProtKB:Q5U3C3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:79432;
CC         Evidence={ECO:0000250|UniProtKB:Q5U3C3};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TMEM164 family. {ECO:0000305}.
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DR   EMBL; AK165839; BAE38406.1; -; mRNA.
DR   EMBL; AK165910; BAE38455.1; -; mRNA.
DR   EMBL; BC056470; AAH56470.1; -; mRNA.
DR   CCDS; CCDS30451.1; -.
DR   RefSeq; NP_001186289.1; NM_001199360.1.
DR   RefSeq; NP_808260.2; NM_177592.4.
DR   AlphaFoldDB; Q6PHN7; -.
DR   SMR; Q6PHN7; -.
DR   FunCoup; Q6PHN7; 190.
DR   STRING; 10090.ENSMUSP00000108517; -.
DR   iPTMnet; Q6PHN7; -.
DR   PhosphoSitePlus; Q6PHN7; -.
DR   PaxDb; 10090-ENSMUSP00000108517; -.
DR   PeptideAtlas; Q6PHN7; -.
DR   ProteomicsDB; 258905; -.
DR   Pumba; Q6PHN7; -.
DR   Antibodypedia; 51401; 23 antibodies from 12 providers.
DR   Ensembl; ENSMUST00000087333.9; ENSMUSP00000084591.3; ENSMUSG00000047045.18.
DR   Ensembl; ENSMUST00000112896.9; ENSMUSP00000108517.3; ENSMUSG00000047045.18.
DR   Ensembl; ENSMUST00000133634.8; ENSMUSP00000138503.2; ENSMUSG00000047045.18.
DR   GeneID; 209497; -.
DR   KEGG; mmu:209497; -.
DR   UCSC; uc009ulx.2; mouse.
DR   AGR; MGI:2148020; -.
DR   CTD; 84187; -.
DR   MGI; MGI:2148020; Tmem164.
DR   VEuPathDB; HostDB:ENSMUSG00000047045; -.
DR   eggNOG; ENOG502QWAJ; Eukaryota.
DR   GeneTree; ENSGT00390000007430; -.
DR   HOGENOM; CLU_072415_0_0_1; -.
DR   InParanoid; Q6PHN7; -.
DR   OMA; FIYIMHG; -.
DR   OrthoDB; 17328at2759; -.
DR   PhylomeDB; Q6PHN7; -.
DR   BioGRID-ORCS; 209497; 3 hits in 76 CRISPR screens.
DR   PRO; PR:Q6PHN7; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q6PHN7; protein.
DR   Bgee; ENSMUSG00000047045; Expressed in paneth cell and 230 other cell types or tissues.
DR   ExpressionAtlas; Q6PHN7; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0160020; P:positive regulation of ferroptosis; ISS:UniProtKB.
DR   InterPro; IPR026508; TMEM164.
DR   InterPro; IPR059250; TMEM164-like.
DR   PANTHER; PTHR20948; TRANSMEMBRANE PROTEIN 164; 1.
DR   PANTHER; PTHR20948:SF2; TRANSMEMBRANE PROTEIN 164; 1.
DR   Pfam; PF14808; TMEM164; 1.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..296
FT                   /note="Transmembrane protein 164"
FT                   /id="PRO_0000259641"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          66..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  33441 MW;  9240EBD6F9F231A9 CRC64;
     MSRYSYQSLL DWLYGGVDPS FAGNGGPDCA AFLSWQQRLL ESVVVLTLAL LEILVALRHI
     LRQKEDGRGG RSSQPQQVTQ RPEEGKESLS KNLLLVALCL IFGVEVGFKF ATKTVIYLLN
     PCHLVTMMHI FLLACPPCPG ATVIFKLQMH MLNGALLALL FPVVNTRLLP FELEIYYIQH
     AMLYVVPVYL LWKGGAYTPE PLCNFQWALL STGLMFFYHF SFLQILGLVT EVNLNNMLCP
     AISDPFYGPW YRIWASGHQT LMTMTHGKLV ILFSYMAGPL CKYLLDLLRL PAKKID
//