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Q6IE52 (MUG2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Murinoglobulin-2
Gene names
Name:Mug2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1448 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective.

Subunit structure

Monomer By similarity. UniProtKB P14046

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 14481424Murinoglobulin-2
PRO_0000271252

Regions

Region678 – 70932Bait region By similarity UniProtKB P28665

Amino acid modifications

Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Glycosylation7511N-linked (GlcNAc...) Potential
Glycosylation8461N-linked (GlcNAc...) Potential
Glycosylation9681N-linked (GlcNAc...) Potential
Glycosylation11141N-linked (GlcNAc...) Potential
Glycosylation12851N-linked (GlcNAc...) Potential
Glycosylation13981N-linked (GlcNAc...) Potential
Disulfide bond48 ↔ 86 By similarity UniProtKB P01023
Disulfide bond245 ↔ 277 By similarity UniProtKB P01023
Disulfide bond263 ↔ 289 By similarity UniProtKB P01023
Disulfide bond462 ↔ 556 By similarity UniProtKB P01023
Disulfide bond588 ↔ 748 By similarity UniProtKB P01023
Disulfide bond636 ↔ 681 By similarity UniProtKB P01023
Disulfide bond824 ↔ 860 By similarity UniProtKB P01023
Disulfide bond898 ↔ 1295 By similarity UniProtKB P01023
Disulfide bond1056 ↔ 1101 By similarity UniProtKB P01023
Disulfide bond1326 ↔ 1441 By similarity UniProtKB P01023
Cross-link949 ↔ 952Isoglutamyl cysteine thioester (Cys-Gln) By similarity UniProtKB P01023

Sequences

Sequence LengthMass (Da)Tools
Q6IE52 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 7690C1C75F7D75B0

FASTA1,448161,589
        10         20         30         40         50         60 
MWKNREAQLC LFSVLLAFLP SASLLFGNSK YMVLVPSQLY TETPEKICLH LYHLNETVTV 

        70         80         90        100        110        120 
TASLISQRGT RKLFDEPVVD KDLFHCVSFI PRLPSSEEEE SLDINIEGAK HKFSKRHVVL 

       130        140        150        160        170        180 
VKNKESVVFV QTDKPMYKPG QSVKFRVVSM DKNLYPLKEL VQDPKMNRIM QWQDVKTENG 

       190        200        210        220        230        240 
LKQLSFSLSA EPIQGPYKIV VLKQSGVKEE HSFTVMEFVL PRFGVDVKVP NAISVYDEII 

       250        260        270        280        290        300 
SVTACDRYTY GKPVLGRVKV RLCHGNPSFS SETKSACKEE NSQLDNNGCS TQEVNITEFQ 

       310        320        330        340        350        360 
LKENYLKVRQ AFHVNATVTE EGTGMEFGGY GRIEVERTRN KFLFLKADSH FRHGIPFFVK 

       370        380        390        400        410        420 
VRLVDIKGDP IPNEQVFIKA QEAGYTNATT TDQHGLAKFS IDTSSISGYS LNIKVYHKEE 

       430        440        450        460        470        480 
NLCIHSSCTA ERHAEAHHTA YAVYSLSKSY IYLDTEAGVL PCNQIHTVQA HFILKGQVLG 

       490        500        510        520        530        540 
VLPQIVFHYL VMAQGSILQT GNHTHQVESG APVQGNFALE IPVEFSMVPM AKMLIYTILP 

       550        560        570        580        590        600 
DGEVIADSVK FQVEKCLRNK VHLSFSPSQS LPASQTHMRV TASPQSLCGL RAVDQSVLLL 

       610        620        630        640        650        660 
RPEAELSPSL IYDLPGMQDS NFIPRSHHPF EDEDDCLMYQ PRDTEELTYS VPYGREKDVY 

       670        680        690        700        710        720 
RYVDMGLTAF TNLKIKHPTY CYDLPKEPPR KDPPRKDPEP KDTVVETIRN YFPETWVWDL 

       730        740        750        760        770        780 
VTVSSSGVTE VEMTVPDTIT EWKAGALCLS NDTGLGLSSV ATLQAFQPFF VELTMPYSVI 

       790        800        810        820        830        840 
RGEAFTLKAT VMNYLPTSLQ MTVQLEASPD FTAVPVGNDQ DSYCLGANGR HTSSWLVTPK 

       850        860        870        880        890        900 
SLGNVNFSVS VEAQQSPEPC GSEVATVPET GRKDTVIKVL IVEPEGIKKE HTFSSLLCAS 

       910        920        930        940        950        960 
DAELSETLSL LLPPRVVKDS ARAHFSVMGD ILSSAIKNTQ NLIQMPYGCG EQNMVLFAPN 

       970        980        990       1000       1010       1020 
IYVLKYLNET QQLTENIKSK ALGYLRAGYQ RELNYKHKDG SYSAFGDHNG QGQGNTWLTA 

      1030       1040       1050       1060       1070       1080 
FVLKSFAQAR AFIFIDESHI TDAFTWLSKQ QKDSGCFRSS GSLFNNAMKG GVDDEITLSA 

      1090       1100       1110       1120       1130       1140 
YITMALLESS LPPVVSKALG CLEASWETIE QGRNGSFVYT KALMAYAFTL AGNQEKRNEI 

      1150       1160       1170       1180       1190       1200 
LKSLDKEAIK EDNSIHWERP QKPMKSEHYL YTPQASSVEV EMSAYVVLAR LTAHPAPSPE 

      1210       1220       1230       1240       1250       1260 
DLALSTGTIK WLTKQQNSHG GFSSTQDTVV ALDALSKYGA ATFSKSQKTP SVTVQSSGSF 

      1270       1280       1290       1300       1310       1320 
SQKFQVDKSN RLLLQQVSLP DIPGNYTIRV SGEGCVYAQT TLRYNLPLEK QQPAFALKVK 

      1330       1340       1350       1360       1370       1380 
TVPLTCNNPK GQNSFQISLE ISYTGSRPAS NMVIADVKML SGFIPLKPTV KKLERLEHVS 

      1390       1400       1410       1420       1430       1440 
RTEVTTNNVL LYLDQVTNQT LSFSFIIQQD IPVKNLQPAI VKVYDYYETD EVAFAEYSSP 


CSSDKQNV 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 873-878, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"A genomic analysis of rat proteases and protease inhibitors."
Puente X.S., Lopez-Otin C.
Genome Res. 14:609-622(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC113675 Genomic DNA. No translation available.
BN000341 mRNA. Translation: CAE51393.1.
RefSeqNP_001002826.1. NM_001002826.1.
UniGeneRn.198690.

3D structure databases

ProteinModelPortalQ6IE52.
SMRQ6IE52. Positions 125-221, 1315-1447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000040516.

Proteomic databases

PRIDEQ6IE52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID408236.
KEGGrno:408236.
UCSCRGD:1302962. rat.

Organism-specific databases

CTD17837.
RGD1302962. Mug2.

Phylogenomic databases

HOGENOMHOG000220939.
HOVERGENHBG000039.

Gene expression databases

GenevestigatorQ6IE52.

Family and domain databases

Gene3D1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR014756. Ig_E-set.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR010916. TonB_box_CS.
[Graphical view]
PfamPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio696498.

Entry information

Entry nameMUG2_RAT
AccessionPrimary (citable) accession number: Q6IE52
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families