MPEG1_PONAB
ID MPEG1_PONAB Reviewed; 716 AA.
AC Q5RBP9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 54.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 ---------------------------------------------------------------------------
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; CR858589; CAH90811.1; -; mRNA.
DR RefSeq; NP_001125461.1; NM_001131989.1.
DR AlphaFoldDB; Q5RBP9; -.
DR SMR; Q5RBP9; -.
DR STRING; 9601.ENSPPYP00000003725; -.
DR GeneID; 100172369; -.
DR KEGG; pon:100172369; -.
DR CTD; 219972; -.
DR eggNOG; ENOG502QRKR; Eukaryota.
DR InParanoid; Q5RBP9; -.
DR OrthoDB; 235876at2759; -.
DR Proteomes; UP000001595; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..716
FT /note="Macrophage-expressed gene 1 protein"
FT /id="PRO_0000324144"
FT TOPO_DOM 21..655
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..345
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT REGION 693..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
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 716 AA; 78832 MW; 2EF7C5644B2DC10E CRC64;
MNNFRATILF WAVAAWVTSG KPLGEMDEVG VQKCKNALKL PVLEVLPGGG WDNLRNVDMG
RVMELTYSNC RTTEDGQYII PDEIFTIPQK QSNLEMNSEI LESWANYQSS TSYSINTELS
LFSKVNGKFS TEFQRMKTLQ LKDQAITTRV QVRNLIYTVK INPALELNWS FRKELLDISD
RLENNQTRMA TYLAELLVLN YGTHVITSVD AGAALIQEDH IRASFLQDSQ SSRSAVTASA
GLAFQNTVNF KFEENYTSQN VLTKSYLSNR TNSRVQSIGG VPFYPGITLQ AWQQGITNHL
VAIDRSGLPL HFFINPNMLP DLPGPLVKKV SKTVETAVKR YYTFNTYPGC TDLNSPNFNF
QANTDDGSCE GKMTNFSFGG VYQECTQLSG NRDVLLCQKL EQKNPLTGDF SCPSGYSPVR
LLSQIHEEGY NHLECHRKCT LLVFCKTVCE DVFQVAKAEF RAFWCVASSQ VPENSGLLFG
GLFSSKSINP MTNAQSCPAG YFPLSLFENL KVCVSQDYEL GSRFAVPFGG FFSCTVGNPL
VDPAISRDLG VPSLKKCPGG FSQHLALISD GCQVSYCVKS GLFTGGSLPP ARLPPFTRPP
LMSQAATNTV IVTNSENARS WIKDSQTHQW RLGEPIELRR AMNDIHGDGG GLSGGAAAGV
TLGVTTILAV VITLAIYGTR KFKKKAYQAI EERQSLVPGT AATGDTTYQE QGQSPA
