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Q6IE52

- MUG2_RAT

UniProt

Q6IE52 - MUG2_RAT

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Protein

Murinoglobulin-2

Gene

Mug2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiQ6IE52.

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

        10         20         30         40         50
MWKNREAQLC LFSVLLAFLP SASLLFGNSK YMVLVPSQLY TETPEKICLH
60 70 80 90 100
LYHLNETVTV TASLISQRGT RKLFDEPVVD KDLFHCVSFI PRLPSSEEEE
110 120 130 140 150
SLDINIEGAK HKFSKRHVVL VKNKESVVFV QTDKPMYKPG QSVKFRVVSM
160 170 180 190 200
DKNLYPLKEL VQDPKMNRIM QWQDVKTENG LKQLSFSLSA EPIQGPYKIV
210 220 230 240 250
VLKQSGVKEE HSFTVMEFVL PRFGVDVKVP NAISVYDEII SVTACDRYTY
260 270 280 290 300
GKPVLGRVKV RLCHGNPSFS SETKSACKEE NSQLDNNGCS TQEVNITEFQ
310 320 330 340 350
LKENYLKVRQ AFHVNATVTE EGTGMEFGGY GRIEVERTRN KFLFLKADSH
360 370 380 390 400
FRHGIPFFVK VRLVDIKGDP IPNEQVFIKA QEAGYTNATT TDQHGLAKFS
410 420 430 440 450
IDTSSISGYS LNIKVYHKEE NLCIHSSCTA ERHAEAHHTA YAVYSLSKSY
460 470 480 490 500
IYLDTEAGVL PCNQIHTVQA HFILKGQVLG VLPQIVFHYL VMAQGSILQT
510 520 530 540 550
GNHTHQVESG APVQGNFALE IPVEFSMVPM AKMLIYTILP DGEVIADSVK
560 570 580 590 600
FQVEKCLRNK VHLSFSPSQS LPASQTHMRV TASPQSLCGL RAVDQSVLLL
610 620 630 640 650
RPEAELSPSL IYDLPGMQDS NFIPRSHHPF EDEDDCLMYQ PRDTEELTYS
660 670 680 690 700
VPYGREKDVY RYVDMGLTAF TNLKIKHPTY CYDLPKEPPR KDPPRKDPEP
710 720 730 740 750
KDTVVETIRN YFPETWVWDL VTVSSSGVTE VEMTVPDTIT EWKAGALCLS
760 770 780 790 800
NDTGLGLSSV ATLQAFQPFF VELTMPYSVI RGEAFTLKAT VMNYLPTSLQ
810 820 830 840 850
MTVQLEASPD FTAVPVGNDQ DSYCLGANGR HTSSWLVTPK SLGNVNFSVS
860 870 880 890 900
VEAQQSPEPC GSEVATVPET GRKDTVIKVL IVEPEGIKKE HTFSSLLCAS
910 920 930 940 950
DAELSETLSL LLPPRVVKDS ARAHFSVMGD ILSSAIKNTQ NLIQMPYGCG
960 970 980 990 1000
EQNMVLFAPN IYVLKYLNET QQLTENIKSK ALGYLRAGYQ RELNYKHKDG
1010 1020 1030 1040 1050
SYSAFGDHNG QGQGNTWLTA FVLKSFAQAR AFIFIDESHI TDAFTWLSKQ
1060 1070 1080 1090 1100
QKDSGCFRSS GSLFNNAMKG GVDDEITLSA YITMALLESS LPPVVSKALG
1110 1120 1130 1140 1150
CLEASWETIE QGRNGSFVYT KALMAYAFTL AGNQEKRNEI LKSLDKEAIK
1160 1170 1180 1190 1200
EDNSIHWERP QKPMKSEHYL YTPQASSVEV EMSAYVVLAR LTAHPAPSPE
1210 1220 1230 1240 1250
DLALSTGTIK WLTKQQNSHG GFSSTQDTVV ALDALSKYGA ATFSKSQKTP
1260 1270 1280 1290 1300
SVTVQSSGSF SQKFQVDKSN RLLLQQVSLP DIPGNYTIRV SGEGCVYAQT
1310 1320 1330 1340 1350
TLRYNLPLEK QQPAFALKVK TVPLTCNNPK GQNSFQISLE ISYTGSRPAS
1360 1370 1380 1390 1400
NMVIADVKML SGFIPLKPTV KKLERLEHVS RTEVTTNNVL LYLDQVTNQT
1410 1420 1430 1440
LSFSFIIQQD IPVKNLQPAI VKVYDYYETD EVAFAEYSSP CSSDKQNV
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.
InParanoidi Q6IE52.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 67 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