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Q6IE52

- MUG2_RAT

UniProt

Q6IE52 - MUG2_RAT

Protein

Murinoglobulin-2

Gene

Mug2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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.Curated

    GO - Molecular functioni

    1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Murinoglobulin-2
    Gene namesi
    Name:Mug2Imported
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi1302962. Mug2.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular space Source: InterPro

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 14481424Murinoglobulin-2Sequence AnalysisPRO_0000271252Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi48 ↔ 86By similarity
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi245 ↔ 277By similarity
    Disulfide bondi263 ↔ 289By similarity
    Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi462 ↔ 556By similarity
    Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi588 ↔ 748By similarity
    Disulfide bondi636 ↔ 681By similarity
    Glycosylationi751 – 7511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi824 ↔ 860By similarity
    Glycosylationi846 – 8461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi898 ↔ 1295By similarity
    Cross-linki949 ↔ 952Isoglutamyl cysteine thioester (Cys-Gln)By similarity
    Glycosylationi968 – 9681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1056 ↔ 1101By similarity
    Glycosylationi1114 – 11141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1285 – 12851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1326 ↔ 1441By similarity
    Glycosylationi1398 – 13981N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Thioester bond

    Proteomic databases

    PRIDEiQ6IE52.

    Expressioni

    Gene expression databases

    GenevestigatoriQ6IE52.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000040516.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6IE52.
    SMRiQ6IE52. Positions 125-221, 1315-1447.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni678 – 70932Bait regionBy similarityAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Bait region, Signal

    Phylogenomic databases

    HOGENOMiHOG000220939.
    HOVERGENiHBG000039.

    Family and domain databases

    Gene3Di1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProiIPR009048. 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]
    PfamiPF00207. 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]
    SUPFAMiSSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6IE52-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWKNREAQLC LFSVLLAFLP SASLLFGNSK YMVLVPSQLY TETPEKICLH     50
    LYHLNETVTV TASLISQRGT RKLFDEPVVD KDLFHCVSFI PRLPSSEEEE 100
    SLDINIEGAK HKFSKRHVVL VKNKESVVFV QTDKPMYKPG QSVKFRVVSM 150
    DKNLYPLKEL VQDPKMNRIM QWQDVKTENG LKQLSFSLSA EPIQGPYKIV 200
    VLKQSGVKEE HSFTVMEFVL PRFGVDVKVP NAISVYDEII SVTACDRYTY 250
    GKPVLGRVKV RLCHGNPSFS SETKSACKEE NSQLDNNGCS TQEVNITEFQ 300
    LKENYLKVRQ AFHVNATVTE EGTGMEFGGY GRIEVERTRN KFLFLKADSH 350
    FRHGIPFFVK VRLVDIKGDP IPNEQVFIKA QEAGYTNATT TDQHGLAKFS 400
    IDTSSISGYS LNIKVYHKEE NLCIHSSCTA ERHAEAHHTA YAVYSLSKSY 450
    IYLDTEAGVL PCNQIHTVQA HFILKGQVLG VLPQIVFHYL VMAQGSILQT 500
    GNHTHQVESG APVQGNFALE IPVEFSMVPM AKMLIYTILP DGEVIADSVK 550
    FQVEKCLRNK VHLSFSPSQS LPASQTHMRV TASPQSLCGL RAVDQSVLLL 600
    RPEAELSPSL IYDLPGMQDS NFIPRSHHPF EDEDDCLMYQ PRDTEELTYS 650
    VPYGREKDVY RYVDMGLTAF TNLKIKHPTY CYDLPKEPPR KDPPRKDPEP 700
    KDTVVETIRN YFPETWVWDL VTVSSSGVTE VEMTVPDTIT EWKAGALCLS 750
    NDTGLGLSSV ATLQAFQPFF VELTMPYSVI RGEAFTLKAT VMNYLPTSLQ 800
    MTVQLEASPD FTAVPVGNDQ DSYCLGANGR HTSSWLVTPK SLGNVNFSVS 850
    VEAQQSPEPC GSEVATVPET GRKDTVIKVL IVEPEGIKKE HTFSSLLCAS 900
    DAELSETLSL LLPPRVVKDS ARAHFSVMGD ILSSAIKNTQ NLIQMPYGCG 950
    EQNMVLFAPN IYVLKYLNET QQLTENIKSK ALGYLRAGYQ RELNYKHKDG 1000
    SYSAFGDHNG QGQGNTWLTA FVLKSFAQAR AFIFIDESHI TDAFTWLSKQ 1050
    QKDSGCFRSS GSLFNNAMKG GVDDEITLSA YITMALLESS LPPVVSKALG 1100
    CLEASWETIE QGRNGSFVYT KALMAYAFTL AGNQEKRNEI LKSLDKEAIK 1150
    EDNSIHWERP QKPMKSEHYL YTPQASSVEV EMSAYVVLAR LTAHPAPSPE 1200
    DLALSTGTIK WLTKQQNSHG GFSSTQDTVV ALDALSKYGA ATFSKSQKTP 1250
    SVTVQSSGSF SQKFQVDKSN RLLLQQVSLP DIPGNYTIRV SGEGCVYAQT 1300
    TLRYNLPLEK QQPAFALKVK TVPLTCNNPK GQNSFQISLE ISYTGSRPAS 1350
    NMVIADVKML SGFIPLKPTV KKLERLEHVS RTEVTTNNVL LYLDQVTNQT 1400
    LSFSFIIQQD IPVKNLQPAI VKVYDYYETD EVAFAEYSSP CSSDKQNV 1448
    Length:1,448
    Mass (Da):161,589
    Last modified:July 5, 2004 - v1
    Checksum:i7690C1C75F7D75B0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC113675 Genomic DNA. No translation available.
    BN000341 mRNA. Translation: CAE51393.1.
    RefSeqiNP_001002826.1. NM_001002826.1.
    UniGeneiRn.198690.

    Genome annotation databases

    GeneIDi408236.
    KEGGirno:408236.
    UCSCiRGD:1302962. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC113675 Genomic DNA. No translation available.
    BN000341 mRNA. Translation: CAE51393.1 .
    RefSeqi NP_001002826.1. NM_001002826.1.
    UniGenei Rn.198690.

    3D structure databases

    ProteinModelPortali Q6IE52.
    SMRi Q6IE52. Positions 125-221, 1315-1447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000040516.

    Proteomic databases

    PRIDEi Q6IE52.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 408236.
    KEGGi rno:408236.
    UCSCi RGD:1302962. rat.

    Organism-specific databases

    CTDi 17837.
    RGDi 1302962. Mug2.

    Phylogenomic databases

    HOGENOMi HOG000220939.
    HOVERGENi HBG000039.

    Miscellaneous databases

    NextBioi 696498.

    Gene expression databases

    Genevestigatori Q6IE52.

    Family and domain databases

    Gene3Di 1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProi IPR009048. 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 ]
    Pfami PF00207. 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 ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiMUG2_RAT
    AccessioniPrimary (citable) accession number: Q6IE52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3