ID MUG1_RAT Reviewed; 1487 AA.
AC Q03626; Q03310; Q63018; Q63020; Q63023; Q78DZ4; Q9JMK7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 131.
DE RecName: Full=Murinoglobulin-1;
DE AltName: Full=Alpha-1 inhibitor 3 variant I;
DE AltName: Full=Alpha-X protein;
DE Flags: Precursor;
GN Name=Mug1 {ECO:0000312|RGD:621366}; Synonyms=A1i3;
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] {ECO:0000305, ECO:0000312|EMBL:CAA37176.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 1-161, AND INDUCTION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAA37176.1};
RC TISSUE=Liver {ECO:0000312|EMBL:CAA37176.1};
RX PubMed=1709877; DOI=10.1016/0014-5793(91)80515-5;
RA Regler R., Sickinger S., Schweizer M.;
RT "Differential regulation of the two mRNA species of the rodent negative
RT acute phase protein alpha 1-inhibitor 3.";
RL FEBS Lett. 282:368-372(1991).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAA40633.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-409 (ISOFORM 2).
RC STRAIN=Fischer 344 {ECO:0000312|EMBL:AAA40633.1}; TISSUE=Liver;
RX PubMed=2831216; DOI=10.1016/s0021-9258(18)69025-8;
RA Braciak T.A., Northemann W., Hudson G.O., Shiels B.R., Gehring M.R.,
RA Fey G.H.;
RT "Sequence and acute phase regulation of rat alpha 1-inhibitor III messenger
RT RNA.";
RL J. Biol. Chem. 263:3999-4012(1988).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA00750.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1157-1254, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Liver {ECO:0000312|EMBL:BAA00750.1};
RX PubMed=2511184; DOI=10.1111/j.1349-7006.1989.tb01711.x;
RA Sugiyama K., Izumi S., Tomino S., Nagase S.;
RT "Tumor-associated expression of a serum protein, termed alpha X protein
RT (alpha 1-inhibitor III), and its mRNA in rat liver.";
RL Jpn. J. Cancer Res. 80:759-764(1989).
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 {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P14046}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2511184}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:1709877};
CC IsoId=Q03626-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:2831216};
CC IsoId=Q03626-2; Sequence=VSP_052263;
CC -!- TISSUE SPECIFICITY: Plasma. {ECO:0000269|PubMed:2511184}.
CC -!- INDUCTION: Expression level in the liver as well as protein level in
CC plasma down-regulated by up to 70% during acute inflammation or tumor
CC development. {ECO:0000269|PubMed:1709877, ECO:0000269|PubMed:2511184}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000255}.
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DR EMBL; X52984; CAA37176.1; -; mRNA.
DR EMBL; X66454; CAA47070.1; -; Genomic_DNA.
DR EMBL; M22358; AAA40629.1; -; mRNA.
DR EMBL; M22360; AAA40633.1; -; mRNA.
DR EMBL; M22361; AAA40631.1; -; mRNA.
DR EMBL; D00873; BAA00750.1; -; mRNA.
DR PIR; JL0112; JL0112.
DR PIR; S15904; S15904.
DR RefSeq; NP_075591.1; NM_023103.1. [Q03626-1]
DR AlphaFoldDB; Q03626; -.
DR SMR; Q03626; -.
DR BioGRID; 269104; 1.
DR IntAct; Q03626; 1.
DR STRING; 10116.ENSRNOP00000019969; -.
DR MEROPS; I39.004; -.
DR CarbonylDB; Q03626; -.
DR GlyCosmos; Q03626; 13 sites, 6 glycans.
DR GlyGen; Q03626; 14 sites, 6 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q03626; -.
DR PhosphoSitePlus; Q03626; -.
DR PaxDb; 10116-ENSRNOP00000019969; -.
DR Ensembl; ENSRNOT00055019262; ENSRNOP00055015535; ENSRNOG00055011345. [Q03626-1]
DR Ensembl; ENSRNOT00060055392; ENSRNOP00060045836; ENSRNOG00060031936. [Q03626-1]
DR GeneID; 497794; -.
DR KEGG; rno:497794; -.
DR UCSC; RGD:621366; rat. [Q03626-1]
DR AGR; RGD:621366; -.
DR CTD; 17836; -.
DR RGD; 621366; Mug1.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; Q03626; -.
DR OrthoDB; 2970602at2759; -.
DR PhylomeDB; Q03626; -.
DR PRO; PR:Q03626; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0030414; F:peptidase inhibitor activity; TAS:RGD.
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:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR047565; Alpha-macroglob_thiol-ester_cl.
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 PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR PANTHER; PTHR11412:SF133; MURINOGLOBULIN-1-RELATED; 1.
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 SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 2: Evidence at transcript level;
KW Acute phase; Alternative splicing; Bait region; Disulfide bond;
KW Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1487
FT /note="Murinoglobulin-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5000145662"
FT REGION 686..745
FT /note="Bait region"
FT /evidence="ECO:0000250|UniProtKB:P28665"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1004
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..86
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 251..283
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 269..295
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 468..563
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 595..784
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 643..689
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 860..896
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 934..1334
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 1092..1140
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 1365..1480
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT CROSSLNK 985..988
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT VAR_SEQ 263..268
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2831216"
FT /id="VSP_052263"
FT CONFLICT 1157
FT /note="V -> R (in Ref. 3; BAA00750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1252
FT /note="T -> A (in Ref. 3; BAA00750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1487 AA; 165326 MW; BD6ADD927BE2FA8C CRC64;
MKKNREAQLC LFSALLAFLP FASLLNGNSK YMVLVPSQLY TETPEKICLH LYHLNETVTV
TASLISQRGT RKLFDELVVD KDLFHCLSFT IPRLPSSEEE ESLDINIEGA KHKFSERRVV
LVKNKESVVF VQTDKPVYKP GQSVKFRVVS MDKNLHPLNE LFPLAYIEDP KMNRIMQWQD
IKTENGLKQL SFSLSAEPIQ GPYKIVILKQ SGVKEEHSFT VMEFVLPRFG VDVKVPNAIS
VYDEIINVTA CAIYTYGKPV PGHVKISLCH GNPSFSSETK SACKEEDSEL DNNGCSTQEV
NITEFQLKEN YLKMHQAFHV NATVTEEGTG SEFSGSGRIE VERTRNKFLF LKADSHFRHG
IPFFVKIRLV DIKGDPIPNE QVFIKAQEAG YTNATTTDQH GLAKFSIDTS SISGYSLNIK
VYHKEESSCI HSSCTAERHA EEHHTAYAVY SLSKSYIYLD TEAGVLPCNQ IHTVQAHFIL
KGQVLGVLPQ IVFHYLVMAQ GSILQTGNHT HQVEPGVSQV QGNFALEIPV EFSMVPVAKM
LIYTILPDGE VIADSVTFQV EKCLRNKVHL SFSPSQSLPA SQTHMRVTAS PQSLCGLRAV
DQSVLLLKPE AELSPSLIYD LPGMQDSNFI PSSYHPFEDE YDCLMYQPRD TEELTYSVPY
GREKDVYRYV RDMGLTAFTN LKIKHPTYCY EMNMVVLSAP AVESELSPRG GEFEMMPLGV
NKSPLPKEPP RKDPPPKDPV IETIRNYFPE TWIWDLVTVN SSGVTEVEMT VPDTITEWKA
GALCLSNDTG LGLSSVATLQ AFQPFFVELT MPYSVIRGEA FMLKATVMNY LPTSLPMAVQ
LEASPDFTAV PVGNDQDSYC LGANGRHTSS WLVTPKSLGN VNFSVSVEAQ QSPELCGSQV
ATVPETGRKD TVVKVLIVEP EGIKKEHTFS SLLCASDAEL SETLSLLLPP TVVKDSARAH
FSVMGDILSS AIKNTQNLIQ MPYGCGEQNM VLFAPNIYVL KYLNETQQLT EKIKSKALGY
LRAGYQRELN YKHKDGSYSA FGDHNGQGQG NTWLTAFVLK SFAQARAFIF IDESHITDAF
TWLSKQQKDS GCFRSSGSLF NNAMKGGVDD EITLSAYITM ALLESSLPDT DPVVSKALGC
LEASWETIEQ GRNGSFVYTK TLMAYAFALA GNQEKRNEIL KSLDKEAIRE DNSIHWERPQ
KPTKSEGYLY TPQASSAEVE MSAYVVLARL TAQPAPSPED LALSMGTIKW LTKQQNSHGG
FSSTQDTVVA LDALSKYGAA TFSKSQKTPL VTIQSSGSFS QKFQVDNSNR LLLQQVSLPD
IPGNYTVSVS GEGCVYAQTT LRYNMPLEKQ QPAFALKVQT VPLTCNNPKG QNSFQISLEI
SYTGSRPASN MVIADVKMLS GFIPLKPTVK KLERLEHVSR TEVTTNNVLL YLDQVTNQTL
SFSFIIQQDI PVKNLQPAIV KVYDYYETDE VAFAEYSSPC SSDKQNV
//
