MUG2_MOUSE
ID MUG2_MOUSE Reviewed; 1451 AA.
AC P28666;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Murinoglobulin-2;
DE Short=MuG2;
DE Flags: Precursor;
GN Name=Mug2; Synonyms=Mug-2;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=1840592; DOI=10.1016/s0021-9258(18)55388-6;
RA Overbergh L., Torrekens S., van Leuven F., van den Berghe H.;
RT "Molecular characterization of the murinoglobulins.";
RL J. Biol. Chem. 266:16903-16910(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and 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: A proteinase activates the inhibitor by specific proteolysis
CC in the bait region, which, by an unknown mechanism leads to reaction at
CC the cysteinyl-glutamyl internal thiol ester site and to a
CC conformational change, whereby the proteinase is trapped and/or
CC covalently bound to the inhibitor. While in the tetrameric proteinase
CC inhibitors steric inhibition is sufficiently strong, monomeric forms
CC need a covalent linkage between the activated glutamyl residue of the
CC original thiol ester and a terminal amino group of a lysine or another
CC nucleophilic group on the proteinase, for inhibition to be effective.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
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DR EMBL; M65238; AAA73041.1; -; mRNA.
DR EMBL; AC153582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39619.1; -.
DR PIR; B41185; B41185.
DR RefSeq; NP_032672.2; NM_008646.3.
DR AlphaFoldDB; P28666; -.
DR SMR; P28666; -.
DR BioGRID; 201614; 7.
DR STRING; 10090.ENSMUSP00000080469; -.
DR MEROPS; I39.005; -.
DR CarbonylDB; P28666; -.
DR GlyGen; P28666; 8 sites.
DR iPTMnet; P28666; -.
DR PhosphoSitePlus; P28666; -.
DR CPTAC; non-CPTAC-3657; -.
DR jPOST; P28666; -.
DR MaxQB; P28666; -.
DR PaxDb; P28666; -.
DR PeptideAtlas; P28666; -.
DR PRIDE; P28666; -.
DR ProteomicsDB; 287331; -.
DR DNASU; 17837; -.
DR Ensembl; ENSMUST00000081777; ENSMUSP00000080469; ENSMUSG00000030131.
DR GeneID; 17837; -.
DR KEGG; mmu:17837; -.
DR UCSC; uc009dos.1; mouse.
DR CTD; 17837; -.
DR MGI; MGI:99836; Mug2.
DR VEuPathDB; HostDB:ENSMUSG00000030131; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000164557; -.
DR HOGENOM; CLU_001634_0_1_1; -.
DR InParanoid; P28666; -.
DR OMA; SICHETE; -.
DR OrthoDB; 354230at2759; -.
DR PhylomeDB; P28666; -.
DR TreeFam; TF313285; -.
DR BioGRID-ORCS; 17837; 4 hits in 70 CRISPR screens.
DR PRO; PR:P28666; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P28666; protein.
DR Bgee; ENSMUSG00000030131; Expressed in liver and 14 other tissues.
DR Genevisible; P28666; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0030414; F:peptidase inhibitor activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041813; A2M_TED.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR010916; TonB_box_CS.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF07678; TED_complement; 2.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 1: Evidence at protein level;
KW Bait region; Disulfide bond; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal;
KW Thioester bond.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..1451
FT /note="Murinoglobulin-2"
FT /id="PRO_0000000060"
FT REGION 677..734
FT /note="Bait region"
FT REGION 703..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 871
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..86
FT /evidence="ECO:0000250"
FT DISULFID 251..276
FT /evidence="ECO:0000250"
FT DISULFID 269..288
FT /evidence="ECO:0000250"
FT DISULFID 461..555
FT /evidence="ECO:0000250"
FT DISULFID 587..773
FT /evidence="ECO:0000250"
FT DISULFID 634..680
FT /evidence="ECO:0000250"
FT DISULFID 849..885
FT /evidence="ECO:0000250"
FT DISULFID 923..1274
FT /evidence="ECO:0000250"
FT DISULFID 1081..1104
FT /evidence="ECO:0000250"
FT DISULFID 1298..1444
FT /evidence="ECO:0000250"
FT CROSSLNK 974..977
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT CONFLICT 386
FT /note="A -> T (in Ref. 1; AAA73041)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="E -> A (in Ref. 1; AAA73041)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="V -> I (in Ref. 1; AAA73041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1451 AA; 162382 MW; 8DB472A6C033C35D CRC64;
MWKSRRAQLC LFSVLLAFLP SASSLNGDSK YMVLVPSQLY TETPEKICLH LYHLNETVTV
TASLVSQTGR RNLFDELVVD KDLFQCVSFI IPTLNSPDEE EFLYVDIKGP THEFSKRNAV
LVKNKESVVF VQTDKPVYKP GQSVKFRVVS MDKTLRPLNE LLPLAYIEDP KKNRIMQWRD
IKTENGLKQM SFSLAAEPIQ GPYKIVVHKQ SGVKEEHSFT VMEFVLPRFN VDLKVPNAIS
VNDEVLQVTV CGKYTYGKPV PGQVKISICH ETEAGCKEVN SKLDNNGCST QEVNITELQS
KKRNYEVQLF HVNATVTEEG TGLEFNGYGT TKIERITNKL IFLKADSHFR HGIPFFVKVR
LVDIKGDPIP NERVFIKAQV LGYTSATTTD QHGLAKFSID TAGFSGSSLH IKVNHKGKDS
CYFFYCMEER YASAEHVAYA VYSLSKSYIY LVKETSSILP CNQIHTVQAH FILKGDLGVL
KELVFYYLVM AQGSIIQTGN HTHQVEPGEA PVKGNFDLEI PVEFSMAPMA KMLIYTILPD
GEVIADSVNF EIEKCLRNKV DLSFSSSQSL PASQTRLQVT ASPQSLCGLR AVDQSVLLLK
PEDELSPSWI YNLPGMQHNK FIPSSSLSED REDCILYSSW VAEKHTDWVP HGREKDVYRY
VEDMDLKAFT NLKIKLPKIC FDSAPMSGPR GKFDLAFSSE VSGTLQKGSS KRPQPEEPPR
EDPPPKDPLA ETIRKYFPET WVWDIVTVNS TGVAEVEMTV PDTITEWKAG ALCLSNDTGL
GLSSVVPLQA FQPFFVEVSL PYSVVRGEAF MLKATVMNYL PTSMRMSVQL EASPDFTAVP
VGDDHDSYCL SANGRHTSSW LVTPKSLGNV NFSVSVEAQQ SSEPCGSEVA TVPETGRKDT
VVKVLIVEPE GIKQEHTFNS LFCASDAEIS EKMSLVLPPT VVKDSARAHF SVMGDILSSA
IKNTQNLLHM PYGCGEQNMV LFAPNIYVLK YLDKTQQLTQ KIKTKALGFL RAGYQRELNY
KHKDGSYSAF GDQNGEREGN TWLTAFVLKS FAQARAFIFI DESHITHAFT WLSQQQKDNG
CFRSSGSLFH NDIKHPVVSK ALSCLESSWK TIEQGRNANF VYTKALMAYA FALAGNQDKR
NEILKSLDEE AIKEDNSIHW ERPQKPRKSE HNLYKPQASS VEVEMNAYVV LARLTAQPAP
SPEDLTLSRS TIMWLTKQQN SNGGFSSTQD TVVALDALSK YGAVTFSRRQ KTSLVTIQST
GSFSQKFQVE NSNCLLLQQV PLPDIPGDYT ISVSGEGCVY AQTTLRYNMH LEKQQSAFAL
RVQTVPLTCN NPKGHNSFQI SLEISYTGSR PASNMVIADV KMLSGFIPLK PTVKKLERLE
HISRTEVSNN NVLLYLDQVT NQTLAFSFII QQDISVRNLQ PAIVKVYDYY ETDEVAYAEY
SSPCSSDKQN V
