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
//
