MPEG1_RAT
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};
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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
