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Q400C8 (AMZ2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Archaemetzincin-2

EC=3.-.-.-
Alternative name(s):
Archeobacterial metalloproteinase-like protein 2
Gene names
Name:Amz2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Zinc metalloprotease. Exhibits activity against angiotensin-3 in vitro. Does not hydrolyze neurogranin nor angiotensin-2 By similarity.

Enzyme regulation

Inhibited by the general metalloprotease inhibitors o-phenanthroline and batimastat. Also significantly inhibited by amastatin, which is an inhibitor of aminopeptidases. Not inhibited by 4-(2-aminoethyl)-benzenesulfonyl fluoride, E-64, and TIMPS (tissue inhibitors of metalloproteinases), which are inhibitors of serine, cysteine, and matrix metalloproteases, respectively By similarity.

Sequence similarities

Belongs to the peptidase M54 family.

Sequence caution

The sequence AAH25087.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB23148.1 differs from that shown. Reason: Frameshift at positions 47 and 147.

The sequence BAC35928.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC36674.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q400C8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q400C8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     310-321: ALVKWIDDESCN → MNEERLQQQLQI
     322-359: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Archaemetzincin-2
PRO_0000159619

Sites

Active site2551 By similarity
Metal binding2541Zinc; catalytic By similarity
Metal binding2581Zinc; catalytic By similarity
Metal binding2651Zinc; catalytic Potential

Natural variations

Alternative sequence310 – 32112ALVKW…DESCN → MNEERLQQQLQI in isoform 2.
VSP_016984
Alternative sequence322 – 35938Missing in isoform 2.
VSP_016985

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 909A226405DBDF4B

FASTA35941,341
        10         20         30         40         50         60 
MQVLRHSEHT LKTALLSKNP VLVSQYEKLD AGEQRLMNEA FQPRSNLFEP ITVHSQSDWI 

        70         80         90        100        110        120 
SSHPEAPQDF EQFFSDRYRK APCPKKHIIY IQSIGSLGNT RVISEEYIKW LKGYCEAFFY 

       130        140        150        160        170        180 
GLKVKFLEPV SVSETKCSFR VNEHTQNLQI HTGHILAFLK KNKPEDAFCI VGITMIDLYP 

       190        200        210        220        230        240 
RDSWNFVFGQ ASLSSGVGIF SFARYGKDFY TSKYEGNVTS LQLTSPTDYS IFDNYYIPEI 

       250        260        270        280        290        300 
TSVLLLRSCK TLTHEIGHIL GLRHCQWLAC LMQGSNHLEE SDRRPLNVCP ICLRKLQSAI 

       310        320        330        340        350 
GFNIVERYRA LVKWIDDESC NESGATPKSS SEHAHLPKPV EAFKDWREWL MRCIALLEK 

« Hide

Isoform 2 [UniParc].

Checksum: 4AF1AF1B9B24AE7B
Show »

FASTA32137,117

References

« Hide 'large scale' references
[1]"Identification and characterization of human archaemetzincin-1 and - 2, two novel members of a family of metalloproteases widely distributed in Archaea."
Diaz-Perales A., Quesada V., Peinado J.R., Ugalde A.P., Alvarez J., Suarez M.F., Gomis-Rueth X., Lopez-Otin C.
J. Biol. Chem. 280:30367-30375(2005) [PubMed: 15972818] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: 129.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ879914 mRNA. Translation: CAI53759.1.
AK004062 mRNA. Translation: BAB23148.1. Frameshift.
AK075748 mRNA. Translation: BAC35928.1. Different initiation.
AK077195 mRNA. Translation: BAC36674.1. Different initiation.
BC025087 mRNA. Translation: AAH25087.1. Different initiation.
IPIIPI00336976.
IPI00625349.
RefSeqNP_001239122.1. NM_001252193.1.
NP_079551.3. NM_025275.4.
UniGeneMm.211850.
Mm.265874.

3D structure databases

ProteinModelPortalQ400C8.
SMRQ400C8. Positions 83-301.
ModBaseSearch...

Protein family/group databases

MEROPSM54.002.

Proteomic databases

PRIDEQ400C8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13929.
KEGGmmu:13929.

Organism-specific databases

CTD51321.
MGIMGI:104837. Amz2.

Phylogenomic databases

eggNOGroNOG15496.
GeneTreeENSGT00530000063996.
HOVERGENHBG080165.
InParanoidQ400C8.
OrthoDBEOG4HT8TQ.

Gene expression databases

ArrayExpressQ400C8.
BgeeQ400C8.
CleanExMM_AMZ2.
GenevestigatorQ400C8.
GermOnlineENSMUSG00000020610. Mus musculus.

Family and domain databases

InterProIPR024079. MetalloPept_cat_dom.
IPR012962. Pept_M54_archaemetzincn.
[Graphical view]
Gene3DG3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
KOK06974.
PfamPF07998. Peptidase_M54. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameAMZ2_MOUSE
AccessionPrimary (citable) accession number: Q400C8
Secondary accession number(s): Q8BVM5, Q8K3B9, Q9D121
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 27, 2005
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families