AMPB_RAT
ID AMPB_RAT Reviewed; 650 AA.
AC O09175; P97530;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Aminopeptidase B;
DE Short=AP-B;
DE EC=3.4.11.6;
DE AltName: Full=Arginine aminopeptidase;
DE AltName: Full=Arginyl aminopeptidase;
DE AltName: Full=Cytosol aminopeptidase IV;
GN Name=Rnpep;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9096329; DOI=10.1073/pnas.94.7.2963;
RA Cadel S., Foulon T., Viron A., Balogh A., Midol-Monnet S., Noel N.,
RA Cohen P.;
RT "Aminopeptidase B from the rat testis is a bifunctional enzyme structurally
RT related to leukotriene-A4 hydrolase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2963-2968(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8940051; DOI=10.1074/jbc.271.48.30731;
RA Fukasawa K.M., Fukasawa K., Kanai M., Fujii S., Harada M.;
RT "Molecular cloning and expression of rat liver aminopeptidase B.";
RL J. Biol. Chem. 271:30731-30735(1996).
RN [3]
RP REVIEW.
RX PubMed=10467730; DOI=10.1016/s1357-2725(99)00021-7;
RA Foulon T., Cadel S., Cohen P.;
RT "Aminopeptidase B (EC 3.4.11.6).";
RL Int. J. Biochem. Cell Biol. 31:747-750(1999).
CC -!- FUNCTION: Exopeptidase which selectively removes arginine and/or lysine
CC residues from the N-terminus of several peptide substrates including
CC Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-
CC somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene
CC B4 (LTB-4).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1'
CC is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; U61696; AAB52971.1; -; mRNA.
DR EMBL; D87515; BAA13413.1; -; mRNA.
DR RefSeq; NP_112359.1; NM_031097.1.
DR AlphaFoldDB; O09175; -.
DR SMR; O09175; -.
DR BioGRID; 249633; 1.
DR IntAct; O09175; 5.
DR MINT; O09175; -.
DR STRING; 10116.ENSRNOP00000009198; -.
DR BindingDB; O09175; -.
DR ChEMBL; CHEMBL2452; -.
DR DrugCentral; O09175; -.
DR MEROPS; M01.014; -.
DR iPTMnet; O09175; -.
DR PhosphoSitePlus; O09175; -.
DR World-2DPAGE; 0004:O09175; -.
DR jPOST; O09175; -.
DR PaxDb; O09175; -.
DR PRIDE; O09175; -.
DR GeneID; 81761; -.
DR KEGG; rno:81761; -.
DR UCSC; RGD:621137; rat.
DR CTD; 6051; -.
DR RGD; 621137; Rnpep.
DR eggNOG; KOG1047; Eukaryota.
DR InParanoid; O09175; -.
DR PhylomeDB; O09175; -.
DR BRENDA; 3.4.11.6; 5301.
DR PRO; PR:O09175; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR GO; GO:0050897; F:cobalt ion binding; IDA:RGD.
DR GO; GO:0005507; F:copper ion binding; IDA:RGD.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:RGD.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0016485; P:protein processing; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
DR CDD; cd09599; M1_LTA4H; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.40.320; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR015571; Pept_M1_aminopeptidase-B.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; PTHR45726; 1.
DR PANTHER; PTHR45726:SF1; PTHR45726:SF1; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Direct protein sequencing; Hydrolase;
KW Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Secreted; Zinc.
FT CHAIN 1..650
FT /note="Aminopeptidase B"
FT /id="PRO_0000095090"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 298..302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT SITE 414
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A4"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A4"
FT CONFLICT 47..48
FT /note="FG -> L (in Ref. 1; AAB52971)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="Missing (in Ref. 2; BAA13413)"
FT /evidence="ECO:0000305"
FT CONFLICT 250..251
FT /note="WA -> T (in Ref. 1; AAB52971)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="S -> A (in Ref. 2; BAA13413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 72620 MW; 032BE2F4F50B58E0 CRC64;
MESSGPSSCH SAARRPLHSA QAVDVASASS FRAFEILHLH LDLRAEFGPP GPGPGSRGLN
GKATLELRCL LPEGASELRL DSHSCLEVMA ATLLRGQPGD QQQLTEPVPF HTQPFSHYGQ
ALCVVFPKPC CAAERFRLEL TYRVGEGPGV CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP
CFDTPAVKCT YSALVEVPDG FTAVMSASTW ERRGPNKFFF QMSQPIPSYL IALAIGDLAS
AEVGPRSRVW AEPCLIEAAK EEYNGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF TMYAQRRIST
ILFGAAYTCL EAATGRALLR QHMDVSGEEN PLNKLRVKIE PGVDPDDTYN ETPYEKGYCF
VSYLAHLVGD QEQFDKFLKA YVDEFKFQSI LAEDFLEFYL EYFPELKKKG VDSIPGFEFN
RWLNTPGWPP YLPDLSPGDS LMKPAEELAE LWAASEPDMQ AIEAVAISTW KTYQLVYFLD
KILQKSPLPP GNVKKLGETY PKISNAQNAE LRLRWGQIIL KNDHQEEFWK VKDFLQSQGK
QKYTLPLYHA MMGGSEMART LAKETFSATA SQLHSNVVNY VQQILAPKGS
