Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aminopeptidase B

Gene

Rnpep

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

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

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi325 – 3251Zinc; catalytic
Active sitei326 – 3261Proton acceptorPROSITE-ProRule annotation
Metal bindingi329 – 3291Zinc; catalytic
Metal bindingi348 – 3481Zinc; catalytic
Sitei414 – 4141Transition state stabilizerBy similarity

GO - Molecular functioni

  • aminopeptidase activity Source: UniProtKB
  • cobalt ion binding Source: RGD
  • copper ion binding Source: RGD
  • metalloaminopeptidase activity Source: RGD
  • peptide binding Source: RGD
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • aging Source: RGD
  • negative regulation of blood pressure Source: RGD
  • peptide catabolic process Source: GO_Central
  • protein processing Source: UniProtKB
  • proteolysis Source: UniProtKB
  • retina development in camera-type eye Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.6. 5301.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621137. Rnpep.

Subcellular locationi

GO - Cellular componenti

  • external side of plasma membrane Source: RGD
  • extracellular region Source: UniProtKB
  • extracellular space Source: RGD
  • Golgi apparatus Source: UniProtKB
  • neuron projection Source: RGD
  • plasma membrane Source: UniProtKB
  • secretory granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2452.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 650649Aminopeptidase BPRO_0000095090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71PhosphoserineBy similarity
Modified residuei446 – 4461N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO09175.
PRIDEiO09175.

2D gel databases

World-2DPAGE0004:O09175.

PTM databases

iPTMnetiO09175.
PhosphoSiteiO09175.

Expressioni

Tissue specificityi

Widely expressed.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009198.

Chemistry

BindingDBiO09175.

Structurei

3D structure databases

ProteinModelPortaliO09175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiKOG1047. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000293296.
HOVERGENiHBG001274.
InParanoidiO09175.
KOiK01260.
PhylomeDBiO09175.

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.
SMARTiSM01263. Leuk-A4-hydro_C. 1 hit.
[Graphical view]
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.

O09175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESSGPSSCH SAARRPLHSA QAVDVASASS FRAFEILHLH LDLRAEFGPP
60 70 80 90 100
GPGPGSRGLN GKATLELRCL LPEGASELRL DSHSCLEVMA ATLLRGQPGD
110 120 130 140 150
QQQLTEPVPF HTQPFSHYGQ ALCVVFPKPC CAAERFRLEL TYRVGEGPGV
160 170 180 190 200
CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP CFDTPAVKCT YSALVEVPDG
210 220 230 240 250
FTAVMSASTW ERRGPNKFFF QMSQPIPSYL IALAIGDLAS AEVGPRSRVW
260 270 280 290 300
AEPCLIEAAK EEYNGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM
310 320 330 340 350
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF
360 370 380 390 400
TMYAQRRIST ILFGAAYTCL EAATGRALLR QHMDVSGEEN PLNKLRVKIE
410 420 430 440 450
PGVDPDDTYN ETPYEKGYCF VSYLAHLVGD QEQFDKFLKA YVDEFKFQSI
460 470 480 490 500
LAEDFLEFYL EYFPELKKKG VDSIPGFEFN RWLNTPGWPP YLPDLSPGDS
510 520 530 540 550
LMKPAEELAE LWAASEPDMQ AIEAVAISTW KTYQLVYFLD KILQKSPLPP
560 570 580 590 600
GNVKKLGETY PKISNAQNAE LRLRWGQIIL KNDHQEEFWK VKDFLQSQGK
610 620 630 640 650
QKYTLPLYHA MMGGSEMART LAKETFSATA SQLHSNVVNY VQQILAPKGS
Length:650
Mass (Da):72,620
Last modified:July 11, 2002 - v2
Checksum:i032BE2F4F50B58E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 482FG → L in AAB52971 (PubMed:9096329).Curated
Sequence conflicti74 – 741Missing in BAA13413 (PubMed:8940051).Curated
Sequence conflicti250 – 2512WA → T in AAB52971 (PubMed:9096329).Curated
Sequence conflicti627 – 6271S → A in BAA13413 (PubMed:8940051).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61696 mRNA. Translation: AAB52971.1.
D87515 mRNA. Translation: BAA13413.1.
RefSeqiNP_112359.1. NM_031097.1.
UniGeneiRn.10979.

Genome annotation databases

GeneIDi81761.
KEGGirno:81761.
UCSCiRGD:621137. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61696 mRNA. Translation: AAB52971.1.
D87515 mRNA. Translation: BAA13413.1.
RefSeqiNP_112359.1. NM_031097.1.
UniGeneiRn.10979.

3D structure databases

ProteinModelPortaliO09175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009198.

Chemistry

BindingDBiO09175.
ChEMBLiCHEMBL2452.

Protein family/group databases

MEROPSiM01.014.

PTM databases

iPTMnetiO09175.
PhosphoSiteiO09175.

2D gel databases

World-2DPAGE0004:O09175.

Proteomic databases

PaxDbiO09175.
PRIDEiO09175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81761.
KEGGirno:81761.
UCSCiRGD:621137. rat.

Organism-specific databases

CTDi6051.
RGDi621137. Rnpep.

Phylogenomic databases

eggNOGiKOG1047. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000293296.
HOVERGENiHBG001274.
InParanoidiO09175.
KOiK01260.
PhylomeDBiO09175.

Enzyme and pathway databases

BRENDAi3.4.11.6. 5301.

Miscellaneous databases

PROiO09175.

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.
SMARTiSM01263. Leuk-A4-hydro_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMPB_RAT
AccessioniPrimary (citable) accession number: O09175
Secondary accession number(s): P97530
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2002
Last modified: July 6, 2016
This is version 124 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.