| Tag | Content |
|---|
| CPLM ID | CPLM-018145 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aminopeptidase B |
Protein Synonyms/Alias | AP-B; Arginine aminopeptidase; Arginyl aminopeptidase; Cytosol aminopeptidase IV |
Gene Name | Rnpep |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 398 | PLNKLRVKIEPGVDP | ubiquitination | [1] | | 592 | QEEFQKVKDFLQSQG | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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). |
Sequence Annotation | REGION 298 302 Substrate binding (By similarity).
ACT_SITE 326 326 Proton acceptor (By similarity).
METAL 325 325 Zinc; catalytic (By similarity).
METAL 329 329 Zinc; catalytic (By similarity).
METAL 348 348 Zinc; catalytic (By similarity).
MOD_RES 446 446 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Aminopeptidase; Complete proteome; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 650 AA |
Protein Sequence | MESGGPGNYS AAARRPLHSA QAVDVASASS FRAFEILHLH LDLRAEFGPP GPGPGSRGLS 60
GTATLELRCL LPEGASELRL DSHSCLEVTA ATLRRGQPGD QQAPAEPVPF HTQPFSHYGQ 120
ALCVAFRQPC GAADRFELEL TYRVGEGPGV CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP 180
CFDTPAVKCT YSALIEVPDG FTAVMSADTW EKRGPNKFFF QMSHPIPSYL IALAIGDLAS 240
AEVGPRSRVW AEPCLIEAAK EEYSGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM 300
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF TMYAQRRIST 360
ILFGAAYTCL EAATGRALLR QHMNVSGEEN PLNKLRVKIE PGVDPDDTYN ETPYEKGYCF 420
VSYLAHLVGD QDQFDKFLKA YVDEFKFQSI LAEDFLEFYL EYFPELKKKG VDSIPGFEFD 480
RWLNTPGWPP YLPDLSPGDS LMKPAEELAE LWVTSEPDMQ AIEAVAISTW KTYQLVYFLD 540
KILQKSPLPP GNVKKLGETY PKISNAQNAE LRLRWGQIIL KNDYQEEFQK VKDFLQSQGK 600
QKYTLPLYHA MMGGSEMART LAKDTFAATA SQLHSNVVNY VQQILAPKDS 650 |
Gene Ontology | GO:0005576; C:extracellular region; ISS:UniProtKB. GO:0005615; C:extracellular space; IEA:InterPro. GO:0005886; C:plasma membrane; ISS:UniProtKB. GO:0004177; F:aminopeptidase activity; ISS:UniProtKB. GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0019370; P:leukotriene biosynthetic process; IEA:InterPro. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |