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MUG1_RAT
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   25-MAY-2022, entry version 123.
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   GlyGen; Q03626; 13 sites, 6 N-linked glycans (1 site).
DR   iPTMnet; Q03626; -.
DR   PhosphoSitePlus; Q03626; -.
DR   PaxDb; Q03626; -.
DR   PRIDE; Q03626; -.
DR   GeneID; 497794; -.
DR   KEGG; rno:497794; -.
DR   UCSC; RGD:621366; rat. [Q03626-1]
DR   CTD; 17836; -.
DR   RGD; 621366; Mug1.
DR   eggNOG; KOG1366; Eukaryota.
DR   InParanoid; Q03626; -.
DR   OrthoDB; 354230at2759; -.
DR   PhylomeDB; Q03626; -.
DR   PRO; PR:Q03626; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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   GO; GO:0006954; P:inflammatory response; IEP:RGD.
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   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
 
 
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