ID   MUG2_RAT                Reviewed;        1448 AA.
AC   Q6IE52;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-NOV-2023, entry version 103.
DE   RecName: Full=Murinoglobulin-2;
DE   Flags: Precursor;
GN   Name=Mug2 {ECO:0000312|EMBL:CAE51393.1};
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}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 873-878, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [3] {ECO:0000312|EMBL:CAE51393.1}
RP   IDENTIFICATION.
RX   PubMed=15060002; DOI=10.1101/gr.1946304;
RA   Puente X.S., Lopez-Otin C.;
RT   "A genomic analysis of rat proteases and protease inhibitors.";
RL   Genome Res. 14:609-622(2004).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC       macroglobulin) family. {ECO:0000255}.
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DR   EMBL; AC113675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000341; CAE51393.1; -; mRNA.
DR   RefSeq; NP_001002826.1; NM_001002826.1.
DR   AlphaFoldDB; Q6IE52; -.
DR   SMR; Q6IE52; -.
DR   MEROPS; I39.004; -.
DR   CarbonylDB; Q6IE52; -.
DR   GlyCosmos; Q6IE52; 11 sites, No reported glycans.
DR   GlyGen; Q6IE52; 11 sites.
DR   iPTMnet; Q6IE52; -.
DR   PhosphoSitePlus; Q6IE52; -.
DR   jPOST; Q6IE52; -.
DR   PeptideAtlas; Q6IE52; -.
DR   KEGG; rno:408236; -.
DR   UCSC; RGD:1302962; rat.
DR   AGR; RGD:1302962; -.
DR   CTD; 17837; -.
DR   RGD; 1302962; Mug2.
DR   InParanoid; Q6IE52; -.
DR   OrthoDB; 2970602at2759; -.
DR   PRO; PR:Q6IE52; -.
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: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; 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   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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1448
FT                   /note="Murinoglobulin-2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000271252"
FT   REGION          678..709
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        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        751
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        846
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        968
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..86
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        245..277
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        263..289
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        462..556
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        588..748
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        636..681
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        824..860
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        898..1295
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        1056..1101
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   DISULFID        1326..1441
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
FT   CROSSLNK        949..952
FT                   /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT                   /evidence="ECO:0000250|UniProtKB:P01023"
SQ   SEQUENCE   1448 AA;  161589 MW;  7690C1C75F7D75B0 CRC64;
     MWKNREAQLC LFSVLLAFLP SASLLFGNSK YMVLVPSQLY TETPEKICLH LYHLNETVTV
     TASLISQRGT RKLFDEPVVD KDLFHCVSFI PRLPSSEEEE SLDINIEGAK HKFSKRHVVL
     VKNKESVVFV QTDKPMYKPG QSVKFRVVSM DKNLYPLKEL VQDPKMNRIM QWQDVKTENG
     LKQLSFSLSA EPIQGPYKIV VLKQSGVKEE HSFTVMEFVL PRFGVDVKVP NAISVYDEII
     SVTACDRYTY GKPVLGRVKV RLCHGNPSFS SETKSACKEE NSQLDNNGCS TQEVNITEFQ
     LKENYLKVRQ AFHVNATVTE EGTGMEFGGY GRIEVERTRN KFLFLKADSH FRHGIPFFVK
     VRLVDIKGDP IPNEQVFIKA QEAGYTNATT TDQHGLAKFS IDTSSISGYS LNIKVYHKEE
     NLCIHSSCTA ERHAEAHHTA YAVYSLSKSY IYLDTEAGVL PCNQIHTVQA HFILKGQVLG
     VLPQIVFHYL VMAQGSILQT GNHTHQVESG APVQGNFALE IPVEFSMVPM AKMLIYTILP
     DGEVIADSVK FQVEKCLRNK VHLSFSPSQS LPASQTHMRV TASPQSLCGL RAVDQSVLLL
     RPEAELSPSL IYDLPGMQDS NFIPRSHHPF EDEDDCLMYQ PRDTEELTYS VPYGREKDVY
     RYVDMGLTAF TNLKIKHPTY CYDLPKEPPR KDPPRKDPEP KDTVVETIRN YFPETWVWDL
     VTVSSSGVTE VEMTVPDTIT EWKAGALCLS NDTGLGLSSV ATLQAFQPFF VELTMPYSVI
     RGEAFTLKAT VMNYLPTSLQ MTVQLEASPD FTAVPVGNDQ DSYCLGANGR HTSSWLVTPK
     SLGNVNFSVS VEAQQSPEPC GSEVATVPET GRKDTVIKVL IVEPEGIKKE HTFSSLLCAS
     DAELSETLSL LLPPRVVKDS ARAHFSVMGD ILSSAIKNTQ NLIQMPYGCG EQNMVLFAPN
     IYVLKYLNET QQLTENIKSK ALGYLRAGYQ RELNYKHKDG SYSAFGDHNG QGQGNTWLTA
     FVLKSFAQAR AFIFIDESHI TDAFTWLSKQ QKDSGCFRSS GSLFNNAMKG GVDDEITLSA
     YITMALLESS LPPVVSKALG CLEASWETIE QGRNGSFVYT KALMAYAFTL AGNQEKRNEI
     LKSLDKEAIK EDNSIHWERP QKPMKSEHYL YTPQASSVEV EMSAYVVLAR LTAHPAPSPE
     DLALSTGTIK WLTKQQNSHG GFSSTQDTVV ALDALSKYGA ATFSKSQKTP SVTVQSSGSF
     SQKFQVDKSN RLLLQQVSLP DIPGNYTIRV SGEGCVYAQT TLRYNLPLEK QQPAFALKVK
     TVPLTCNNPK GQNSFQISLE ISYTGSRPAS NMVIADVKML SGFIPLKPTV KKLERLEHVS
     RTEVTTNNVL LYLDQVTNQT LSFSFIIQQD IPVKNLQPAI VKVYDYYETD EVAFAEYSSP
     CSSDKQNV
//