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Q8VCT3 (AMPB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 105. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase B

Short name=AP-B
EC=3.4.11.6
Alternative name(s):
Arginine aminopeptidase
Arginyl aminopeptidase
Cytosol aminopeptidase IV
Gene names
Name:Rnpep
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) By similarity.

Catalytic activity

Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 650649Aminopeptidase B
PRO_0000095089

Regions

Region298 – 3025Substrate binding By similarity

Sites

Active site3261Proton acceptor By similarity
Metal binding3251Zinc; catalytic By similarity
Metal binding3291Zinc; catalytic By similarity
Metal binding3481Zinc; catalytic By similarity
Site4141Transition state stabilizer By similarity

Amino acid modifications

Modified residue4461N6-acetyllysine By similarity

Experimental info

Sequence conflict111A → G in AAH19200. Ref.3
Sequence conflict1271R → P in AAH19200. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8VCT3 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 95138D47E57E3C61

FASTA65072,416
        10         20         30         40         50         60 
MESGGPGNYS AAARRPLHSA QAVDVASASS FRAFEILHLH LDLRAEFGPP GPGPGSRGLS 

        70         80         90        100        110        120 
GTATLELRCL LPEGASELRL DSHSCLEVTA ATLRRGQPGD QQAPAEPVPF HTQPFSHYGQ 

       130        140        150        160        170        180 
ALCVAFRQPC GAADRFELEL TYRVGEGPGV CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP 

       190        200        210        220        230        240 
CFDTPAVKCT YSALIEVPDG FTAVMSADTW EKRGPNKFFF QMSHPIPSYL IALAIGDLAS 

       250        260        270        280        290        300 
AEVGPRSRVW AEPCLIEAAK EEYSGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM 

       310        320        330        340        350        360 
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF TMYAQRRIST 

       370        380        390        400        410        420 
ILFGAAYTCL EAATGRALLR QHMNVSGEEN PLNKLRVKIE PGVDPDDTYN ETPYEKGYCF 

       430        440        450        460        470        480 
VSYLAHLVGD QDQFDKFLKA YVDEFKFQSI LAEDFLEFYL EYFPELKKKG VDSIPGFEFD 

       490        500        510        520        530        540 
RWLNTPGWPP YLPDLSPGDS LMKPAEELAE LWVTSEPDMQ AIEAVAISTW KTYQLVYFLD 

       550        560        570        580        590        600 
KILQKSPLPP GNVKKLGETY PKISNAQNAE LRLRWGQIIL KNDYQEEFQK VKDFLQSQGK 

       610        620        630        640        650 
QKYTLPLYHA MMGGSEMART LAKDTFAATA SQLHSNVVNY VQQILAPKDS 

« Hide

References

[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK159195 mRNA. Translation: BAE34890.1.
AK159445 mRNA. Translation: BAE35089.1.
AK159625 mRNA. Translation: BAE35239.1.
CH466520 Genomic DNA. Translation: EDL39584.1.
BC019200 mRNA. Translation: AAH19200.1.
RefSeqNP_001153096.1. NM_001159624.1.
NP_663392.2. NM_145417.3.
UniGeneMm.291048.

3D structure databases

ProteinModelPortalQ8VCT3.
SMRQ8VCT3. Positions 22-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8VCT3. 2 interactions.
MINTMINT-4087642.
STRING10090.ENSMUSP00000076564.

Chemistry

BindingDBQ8VCT3.
ChEMBLCHEMBL2836.

Protein family/group databases

MEROPSM01.014.

PTM databases

PhosphoSiteQ8VCT3.

Proteomic databases

PaxDbQ8VCT3.
PRIDEQ8VCT3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077340; ENSMUSP00000076564; ENSMUSG00000041926.
GeneID215615.
KEGGmmu:215615.
UCSCuc007csy.2. mouse.

Organism-specific databases

CTD6051.
MGIMGI:2384902. Rnpep.

Phylogenomic databases

eggNOGCOG0308.
GeneTreeENSGT00530000063003.
HOGENOMHOG000293296.
HOVERGENHBG001274.
InParanoidQ3TX27.
KOK01260.
OMARAFEILH.
OrthoDBEOG7SJD42.
TreeFamTF300758.

Gene expression databases

ArrayExpressQ8VCT3.
BgeeQ8VCT3.
CleanExMM_RNPEP.
GenevestigatorQ8VCT3.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR015571. Pept_M1_aminopeptidase-B.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PTHR11533:SF5. PTHR11533:SF5. 1 hit.
PfamPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio374775.
PROQ8VCT3.
SOURCESearch...

Entry information

Entry nameAMPB_MOUSE
AccessionPrimary (citable) accession number: Q8VCT3
Secondary accession number(s): Q3TX27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 105 of the entry and version 2 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

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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