MUG1_MOUSE
ID MUG1_MOUSE Reviewed; 1476 AA.
AC P28665; Q3UNE7; Q80XE6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Murinoglobulin-1;
DE Short=MuG1;
DE Flags: Precursor;
GN Name=Mug1; Synonyms=Mug-1;
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], AND PROTEIN SEQUENCE OF 28-57.
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Gall bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-776; ASN-993 AND ASN-1142.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-313; ASN-871; ASN-993 AND
RP ASN-1142.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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; M65736; AAA73048.1; -; mRNA.
DR EMBL; AK144255; BAE25800.1; -; mRNA.
DR EMBL; AK144541; BAE25930.1; -; mRNA.
DR EMBL; BC051037; AAH51037.1; -; mRNA.
DR CCDS; CCDS39618.1; -.
DR PIR; A41185; A41185.
DR RefSeq; NP_032671.2; NM_008645.3.
DR AlphaFoldDB; P28665; -.
DR SMR; P28665; -.
DR BioGRID; 201613; 4.
DR IntAct; P28665; 1.
DR MINT; P28665; -.
DR STRING; 10090.ENSMUSP00000032228; -.
DR MEROPS; I39.004; -.
DR MEROPS; I39.005; -.
DR CarbonylDB; P28665; -.
DR GlyConnect; 747; 3 N-Linked glycans (2 sites).
DR GlyGen; P28665; 11 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; P28665; -.
DR PhosphoSitePlus; P28665; -.
DR SwissPalm; P28665; -.
DR CPTAC; non-CPTAC-3658; -.
DR jPOST; P28665; -.
DR MaxQB; P28665; -.
DR PaxDb; P28665; -.
DR PeptideAtlas; P28665; -.
DR PRIDE; P28665; -.
DR ProteomicsDB; 287525; -.
DR DNASU; 17836; -.
DR Ensembl; ENSMUST00000032228; ENSMUSP00000032228; ENSMUSG00000059908.
DR GeneID; 17836; -.
DR KEGG; mmu:17836; -.
DR UCSC; uc009dor.1; mouse.
DR CTD; 17836; -.
DR MGI; MGI:99837; Mug1.
DR VEuPathDB; HostDB:ENSMUSG00000059908; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000164557; -.
DR HOGENOM; CLU_001634_0_1_1; -.
DR InParanoid; P28665; -.
DR OMA; THISHAF; -.
DR OrthoDB; 354230at2759; -.
DR PhylomeDB; P28665; -.
DR TreeFam; TF313285; -.
DR BioGRID-ORCS; 17836; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Mug1; mouse.
DR PRO; PR:P28665; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P28665; protein.
DR Bgee; ENSMUSG00000059908; Expressed in liver and 22 other tissues.
DR Genevisible; P28665; 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 GO; GO:0007566; P:embryo implantation; IGI:MGI.
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; 1.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:1840592"
FT CHAIN 28..1476
FT /note="Murinoglobulin-1"
FT /id="PRO_0000000059"
FT REGION 677..734
FT /note="Bait region"
FT REGION 710..729
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:0000269|PubMed:17330941"
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:0000269|PubMed:16944957"
FT CARBOHYD 871
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 1142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1426
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..1323
FT /evidence="ECO:0000250"
FT DISULFID 1081..1129
FT /evidence="ECO:0000250"
FT DISULFID 1354..1469
FT /evidence="ECO:0000250"
FT CROSSLNK 974..977
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT CONFLICT 894
FT /note="E -> A (in Ref. 1; AAA73048)"
FT /evidence="ECO:0000305"
FT CONFLICT 935..937
FT /note="LVL -> SGP (in Ref. 1; AAA73048)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="L -> P (in Ref. 1; AAA73048)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="N -> S (in Ref. 2; BAE25800)"
FT /evidence="ECO:0000305"
FT CONFLICT 1407
FT /note="V -> E (in Ref. 2; BAE25800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1476 AA; 165298 MW; AA43460E473096E1 CRC64;
MWKSRRAQLC LFSVLLAFLH SASLLNGDSK YMVLVPSQLY TETPEKICLH LYQLNETVTV
TASLVSQSGR KNLFDELVLD KDLFQCVSFI IPRLSSSDEE DFLYVDIKGP THEFSKRKAV
LVKNKESVVF VQTDKPVYKP GQSVKFRVVS MDKMLRPLNE LLPLAYIEDP KKNRIMQWRD
IKTENGLKQM SFSLAAEPIQ GPYKIVVHKE SGEKEEHSFT VMEFVLPRFN VDLKVPNAMS
VNDEVLSVTA CGKYTYGKPV PGHVKINVCR ETETGCREVN SQLDNNGCST QEVNITELQS
KKRNYEVQLF HVNATVTEEG TGLEFSRSGT TKIERITNKL IFLKADSHFR HGIPFFVKVR
LVDIKGDPIP NEKVFIKAQE LSYTSATTTD QHGLAEFSID TTCISGSSLH IKVNHKEEDS
CSYFYCMEER HASAKHVAYA VYSLSKSYIY LDTETSSILP CNQIHTVQAH FILKGDLGVL
KELIFYYLVM AQGSIIQTGN HTHQVEPGEA PVKGKFALEI PVEFSMVPMA KMLIYTILPD
GEVIADSVNF EIEKCLRNKV DLRFSTSQSL PASQTRLQVT ASPQSLCGLR AVDQSVLLLK
PESELSPSWI YNLPGMQQNK FVPSSRLSED QEDCILYSSW LAEKHTNLVP HGTEKDVYRY
VEDMGLTAFT NLMIKLPIIC FDYGMVPISA PRVEFDLAFT PEISWSLRTT LSKRPEEPPR
KDPSSNDPLT ETIRKYFPET WVWDIVTVNS TGLAEVEMTV PDTITEWKAG ALCLSNDTGL
GLSSVVPLQA FKPFFVEVSL PYSVVRGEAF MLKATVMNYL PTSMQMSVQL EASPDFTAVP
VGDDQDSYCL SANGRHTSSW LVTPKSLGNV NFSVSAEAQQ SSEPCGSEVA TVPETGRKDT
VVKVLIVEPE GIKQEHTFSS LFCASDAEIS EKMSLVLPPT VVKDSARAHF SVMGDILSSA
IRNTQNLLHM PYGCGEQNMV LFAPNIYVLK YLNETQQLTQ KIKTKALGFL RAGYQRELNY
KHKDGSYSAF GDQNGEREGN TWLTAFVLKS FAQARAFIFI DESHITHAFT WLSQKQKDNG
CFRSSGSLFN NAMKGGVDDE MTLSAYITMA LLESSLPATH PVVSKALSCL ESSWKTIEQE
RNASFVYTKA LMAYAFALAG NQNKRDEILK SLDEEAIKEN NSIHWKRPQK SRKSEHHLYK
PQASSAEVEM NAYVVLARLT AQPAPSPEDL TLSMSTIMWL TKQQNSNGGF SSTQDTVVAL
DALSKYGAVT FSRSQKTTLV TIQSTGSFSQ KFQVENSNRL LLQQVALPDI PGDYTISVSG
EGCVYAQTML RYNMHLEKQL SAFAIWVQTV PLTCNNPKGH NSFQISLEIS YTGSRPASNM
VIADVKMLSG FIPLKPTVKK LERLEHVSRT EVSNNNVLIY LDQVTNQTLA FSFIIQQDIP
VRNLQPAIVK VYDYYETDEM AFAEYSSPCS TDKQNV
