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Q8VCT3

- AMPB_MOUSE

UniProt

Q8VCT3 - AMPB_MOUSE

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Protein
Aminopeptidase B
Gene
Rnpep
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi325 – 3251Zinc; catalytic By similarity
Active sitei326 – 3261Proton acceptor By similarity
Metal bindingi329 – 3291Zinc; catalytic By similarity
Metal bindingi348 – 3481Zinc; catalytic By similarity
Sitei414 – 4141Transition state stabilizer By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. metallopeptidase activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. leukotriene biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase B (EC:3.4.11.6)
Short name:
AP-B
Alternative name(s):
Arginine aminopeptidase
Arginyl aminopeptidase
Cytosol aminopeptidase IV
Gene namesi
Name:Rnpep
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2384902. Rnpep.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: InterPro
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 650649Aminopeptidase B
PRO_0000095089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei446 – 4461N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8VCT3.
PaxDbiQ8VCT3.
PRIDEiQ8VCT3.

PTM databases

PhosphoSiteiQ8VCT3.

Expressioni

Gene expression databases

ArrayExpressiQ8VCT3.
BgeeiQ8VCT3.
CleanExiMM_RNPEP.
GenevestigatoriQ8VCT3.

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

BioGridi229640. 1 interaction.
IntActiQ8VCT3. 2 interactions.
MINTiMINT-4087642.
STRINGi10090.ENSMUSP00000076564.

Structurei

3D structure databases

ProteinModelPortaliQ8VCT3.
SMRiQ8VCT3. Positions 61-608.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 3025Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00530000063003.
HOGENOMiHOG000293296.
HOVERGENiHBG001274.
InParanoidiQ3TX27.
KOiK01260.
OMAiPPGNVKK.
OrthoDBiEOG7SJD42.
TreeFamiTF300758.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR015571. Pept_M1_aminopeptidase-B.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PTHR11533:SF153. PTHR11533:SF153. 1 hit.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8VCT3-1 [UniParc]FASTAAdd to Basket

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MESGGPGNYS AAARRPLHSA QAVDVASASS FRAFEILHLH LDLRAEFGPP    50
GPGPGSRGLS GTATLELRCL LPEGASELRL DSHSCLEVTA ATLRRGQPGD 100
QQAPAEPVPF HTQPFSHYGQ ALCVAFRQPC GAADRFELEL TYRVGEGPGV 150
CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP CFDTPAVKCT YSALIEVPDG 200
FTAVMSADTW EKRGPNKFFF QMSHPIPSYL IALAIGDLAS AEVGPRSRVW 250
AEPCLIEAAK EEYSGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM 300
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF 350
TMYAQRRIST ILFGAAYTCL EAATGRALLR QHMNVSGEEN PLNKLRVKIE 400
PGVDPDDTYN ETPYEKGYCF VSYLAHLVGD QDQFDKFLKA YVDEFKFQSI 450
LAEDFLEFYL EYFPELKKKG VDSIPGFEFD RWLNTPGWPP YLPDLSPGDS 500
LMKPAEELAE LWVTSEPDMQ AIEAVAISTW KTYQLVYFLD KILQKSPLPP 550
GNVKKLGETY PKISNAQNAE LRLRWGQIIL KNDYQEEFQK VKDFLQSQGK 600
QKYTLPLYHA MMGGSEMART LAKDTFAATA SQLHSNVVNY VQQILAPKDS 650
Length:650
Mass (Da):72,416
Last modified:July 27, 2011 - v2
Checksum:i95138D47E57E3C61
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → G in AAH19200. 1 Publication
Sequence conflicti127 – 1271R → P in AAH19200. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS15317.1.
RefSeqiNP_001153096.1. NM_001159624.1.
NP_663392.2. NM_145417.3.
UniGeneiMm.291048.

Genome annotation databases

EnsembliENSMUST00000077340; ENSMUSP00000076564; ENSMUSG00000041926.
GeneIDi215615.
KEGGimmu:215615.
UCSCiuc007csy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS15317.1.
RefSeqi NP_001153096.1. NM_001159624.1.
NP_663392.2. NM_145417.3.
UniGenei Mm.291048.

3D structure databases

ProteinModelPortali Q8VCT3.
SMRi Q8VCT3. Positions 61-608.
ModBasei Search...

Protein-protein interaction databases

BioGridi 229640. 1 interaction.
IntActi Q8VCT3. 2 interactions.
MINTi MINT-4087642.
STRINGi 10090.ENSMUSP00000076564.

Chemistry

BindingDBi Q8VCT3.
ChEMBLi CHEMBL2836.

Protein family/group databases

MEROPSi M01.014.

PTM databases

PhosphoSitei Q8VCT3.

Proteomic databases

MaxQBi Q8VCT3.
PaxDbi Q8VCT3.
PRIDEi Q8VCT3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000077340 ; ENSMUSP00000076564 ; ENSMUSG00000041926 .
GeneIDi 215615.
KEGGi mmu:215615.
UCSCi uc007csy.2. mouse.

Organism-specific databases

CTDi 6051.
MGIi MGI:2384902. Rnpep.

Phylogenomic databases

eggNOGi COG0308.
GeneTreei ENSGT00530000063003.
HOGENOMi HOG000293296.
HOVERGENi HBG001274.
InParanoidi Q3TX27.
KOi K01260.
OMAi PPGNVKK.
OrthoDBi EOG7SJD42.
TreeFami TF300758.

Miscellaneous databases

NextBioi 374775.
PROi Q8VCT3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8VCT3.
Bgeei Q8VCT3.
CleanExi MM_RNPEP.
Genevestigatori Q8VCT3.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR015571. Pept_M1_aminopeptidase-B.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
PTHR11533:SF153. PTHR11533:SF153. 1 hit.
Pfami PF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiAMPB_MOUSE
AccessioniPrimary (citable) accession number: Q8VCT3
Secondary accession number(s): Q3TX27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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