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 03-AUG-2022, entry version 69. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., 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., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., 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., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT 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 renal RT 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 inserting into the bacterial surface to form CC pores (By similarity). By breaching the surface of phagocytosed CC bacteria, allows antimicrobial effectors to enter the bacterial CC periplasmic space and degrade bacterial proteins such as superoxide CC dismutase sodC which contributes to bacterial virulence (By CC similarity). Shows antibacterial activity against a wide spectrum of CC Gram-positive, Gram-negative and acid-fast bacteria (By similarity). CC Reduces the viability of the intracytosolic pathogen L.monocytogenes by CC inhibiting acidification of the phagocytic vacuole of host cells which CC restricts bacterial translocation from the vacuole to the cytosol (By CC similarity). Required for the antibacterial activity of reactive oxygen CC 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 protein CC {ECO:0000255}. Note=Bacterial infection induces translocation of the CC cytoplasmic vesicles to bacterium-containing phagocytic vesicles and CC fusing of the vesicles. {ECO:0000250|UniProtKB:A1L314}. CC -!- PTM: Monoubiquitinated in response to bacterial infection; CC ubiquitination is required for vesicular localization and antibacterial CC activity and can be blocked by bacterial cell cycle inhibiting factor CC (cif) (By similarity). {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 AlphaFoldDB; Q9WV57; -. DR SMR; Q9WV57; -. DR STRING; 10116.ENSRNOP00000066960; -. DR GlyGen; Q9WV57; 3 sites. DR PaxDb; Q9WV57; -. DR PRIDE; Q9WV57; -. DR UCSC; RGD:69275; rat. DR RGD; 69275; Mpeg1. DR eggNOG; ENOG502QRKR; Eukaryota. 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; ISS:UniProtKB. 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 another 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; Cytoplasmic vesicle; Glycoprotein; Immunity; KW Innate immunity; Membrane; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..714 FT /note="Macrophage-expressed gene 1 protein" FT /id="PRO_0000324145" FT TOPO_DOM 20..653 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 654..674 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 675..714 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 30..345 FT /note="MACPF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745" FT REGION 690..714 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 185 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 269 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 375 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="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 //