ID MPEG1_RAT Reviewed; 714 AA. AC Q9WV57; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 2. DT 16-OCT-2019, entry version 62. DE RecName: Full=Macrophage-expressed gene 1 protein; DE Short=Macrophage gene 1 protein; DE Short=Mpg-1; DE AltName: Full=Perforin-2 {ECO:0000250|UniProtKB:Q2M385}; DE Short=P-2 {ECO:0000250|UniProtKB:Q2M385}; DE Flags: Precursor; GN Name=Mpeg1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-708. RC STRAIN=Sprague-Dawley; RA Chen S., Garcia G.E., Xia Y., Wilson C.B., Ku G., Feng L.; RT "Immunoneutralization of the macrophage gene-1 product attenuates RT renal injury in experimental glomerulonephritis in WKY rats."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays a key role in the innate immune response following CC bacterial infection by polymerizing and inserting into the CC bacterial surface to form pores (By similarity). By breaching the CC surface of phagocytosed bacteria, allows antimicrobial effectors CC to enter the bacterial periplasmic space and degrade bacterial CC proteins such as superoxide dismutase sodC which contributes to CC bacterial virulence (By similarity). Shows antibacterial activity CC against a wide spectrum of Gram-positive, Gram-negative and acid- CC fast bacteria (By similarity). Reduces the viability of the CC intracytosolic pathogen L.monocytogenes by inhibiting CC acidification of the phagocytic vacuole of host cells which CC restricts bacterial translocation from the vacuole to the cytosol CC (By similarity). Required for the antibacterial activity of CC reactive oxygen species and nitric oxide (By similarity). CC {ECO:0000250|UniProtKB:A1L314}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane CC {ECO:0000250|UniProtKB:A1L314}; Single-pass type I membrane CC protein {ECO:0000255}. Note=Bacterial infection induces CC translocation of the cytoplasmic vesicles to bacterium-containing CC phagocytic vesicles and fusing of the vesicles. CC {ECO:0000250|UniProtKB:A1L314}. CC -!- PTM: Monoubiquitinated in response to bacterial infection; CC ubiquitination is required for vesicular localization and CC antibacterial activity and can be blocked by bacterial cell cycle CC inhibiting factor (cif) (By similarity). CC {ECO:0000250|UniProtKB:A1L314}. CC -!- SIMILARITY: Belongs to the MPEG1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD38417.1; Type=Frameshift; Evidence={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; AABR03005343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF156540; AAD38417.1; ALT_FRAME; mRNA. DR STRING; 10116.ENSRNOP00000066960; -. DR PaxDb; Q9WV57; -. DR PRIDE; Q9WV57; -. DR UCSC; RGD:69275; rat. DR RGD; 69275; Mpeg1. DR eggNOG; ENOG410IER6; Eukaryota. DR eggNOG; ENOG410ZMVS; LUCA. DR InParanoid; Q9WV57; -. DR PhylomeDB; Q9WV57; -. DR PRO; PR:Q9WV57; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0035915; P:pore formation in membrane of other organism; ISS:UniProtKB. DR InterPro; IPR020864; MACPF. DR InterPro; IPR039707; MPEG1. DR PANTHER; PTHR31463; PTHR31463; 1. DR Pfam; PF01823; MACPF; 1. DR SMART; SM00457; MACPF; 1. DR PROSITE; PS51412; MACPF_2; 1. PE 2: Evidence at transcript level; KW Antibiotic; Antimicrobial; Complete proteome; Cytoplasmic vesicle; KW Glycoprotein; Immunity; Innate immunity; Membrane; Reference proteome; KW Signal; Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 714 Macrophage-expressed gene 1 protein. FT /FTId=PRO_0000324145. FT TOPO_DOM 20 653 Lumenal. {ECO:0000255}. FT TRANSMEM 654 674 Helical. {ECO:0000255}. FT TOPO_DOM 675 714 Cytoplasmic. {ECO:0000255}. FT DOMAIN 30 345 MACPF. {ECO:0000255|PROSITE- FT ProRule:PRU00745}. FT CARBOHYD 185 185 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 269 269 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 375 375 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. SQ SEQUENCE 714 AA; 78527 MW; 3235512C40B9DF35 CRC64; MNSFMAIALI WMMIACAEAD KPLRDPGMTG FQTCKDTLKL PVLEVLPGGG WDNLRNIDMG RVIDLTYTNC KTTEDGQYII PDEVYTIPQK ESNLEMNSEI RDSWVNYQST TSFSINTELS LFSKVNGKFS TEFQRMKTLQ VKDQAVTTRV QVRNRIYTVK NSPTSELSFG FTNALMDICD QLEKNQTKMA TYLAELLVLN YGTHVITSVD AGAALVQEDH IRSSFLLDNQ NSENTVTASA GIAFLNIVNF KVETDHTSQT LLTKSYLSNR TNSRVQSFGG IPFYPGITLE TWQKGITNHL VAIDRAGLPL HFFIKPDKLP GLPGGLVKKL SKTVETAVRH YYTFNTHPGC TNVDSPNFNF QANMEDDSCD AKVTNFTFGG LYQECTELSG DALCQNLEQK NLLTGDFSCP SGYTPVHLLS QTHEEGYSRL ECKKKCTLKI FCKTVCEDVF RVAKAQFRAY WCVATGQVPD NSGLLFGGLF TDKSINPMTN AQSCPAGYIP LNLFESLKVC VSLDYELGYK FSVPFGGFFS CIMGNPLVNS DTAKDIGAPS LKKCPGGFSQ HLAVISDGCQ VSYCVKAGIF TGGSLLPVRL PPYTKPPLMS QVATNTVIVT SSETARSWIK DPQTNQWKLG EPLELHKAMT VIHGDGNGMS GGEAAGVTLG VIIALGIVIT LAIYSTRKYK KEKEYQEIEE QESLVGSFAT DASPPNGEQD PCPA //