Full text data of RNPEP
RNPEP
(APB)
[Confidence: low (only semi-automatic identification from reviews)]
Aminopeptidase B; AP-B; 3.4.11.6 (Arginine aminopeptidase; Arginyl aminopeptidase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Aminopeptidase B; AP-B; 3.4.11.6 (Arginine aminopeptidase; Arginyl aminopeptidase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H4A4
ID AMPB_HUMAN Reviewed; 650 AA.
AC Q9H4A4; Q9BVM9; Q9H1D4; Q9NPT7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-MAR-2002, sequence version 2.
DT 22-JAN-2014, entry version 121.
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;
GN Name=RNPEP; Synonyms=APB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Piesse C., Tymms M., Garrafa E., Gouzy C., Lacasa M., Cadel S.,
RA Foulon T., Cohen P.;
RT "Human aminopeptidase B on chromosome 1q32.2: cDNA, genomic structure
RT and expression.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Kristensen T.;
RT "Human aminopeptidase B cDNA cloning.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-650.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-7, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Exopeptidase which selectively removes arginine and/or
CC lysine residues from the N-terminus of several peptide substrates
CC including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-
CC 1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4)
CC into leukotriene B4 (LTB-4) (By similarity).
CC -!- CATALYTIC ACTIVITY: Release of N-terminal Arg and Lys from
CC oligopeptides when P1' is not Pro. Also acts on arylamides of Arg
CC and Lys.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ242586; CAC12957.1; -; mRNA.
DR EMBL; AJ296161; CAC14047.1; -; mRNA.
DR EMBL; BC001064; AAH01064.1; -; mRNA.
DR EMBL; BC012166; AAH12166.1; -; mRNA.
DR EMBL; AL390139; CAB99087.1; -; mRNA.
DR PIR; T51870; T51870.
DR RefSeq; NP_064601.3; NM_020216.3.
DR RefSeq; XP_005245477.1; XM_005245420.1.
DR RefSeq; XP_005245478.1; XM_005245421.1.
DR UniGene; Hs.497391; -.
DR ProteinModelPortal; Q9H4A4; -.
DR SMR; Q9H4A4; 8-643.
DR IntAct; Q9H4A4; 1.
DR MINT; MINT-1182309; -.
DR STRING; 9606.ENSP00000295640; -.
DR BindingDB; Q9H4A4; -.
DR ChEMBL; CHEMBL2432; -.
DR MEROPS; M01.014; -.
DR PhosphoSite; Q9H4A4; -.
DR DMDM; 20137480; -.
DR PaxDb; Q9H4A4; -.
DR PRIDE; Q9H4A4; -.
DR DNASU; 6051; -.
DR Ensembl; ENST00000295640; ENSP00000295640; ENSG00000176393.
DR GeneID; 6051; -.
DR KEGG; hsa:6051; -.
DR UCSC; uc001gxd.3; human.
DR CTD; 6051; -.
DR GeneCards; GC01P201951; -.
DR H-InvDB; HIX0023896; -.
DR HGNC; HGNC:10078; RNPEP.
DR HPA; HPA036075; -.
DR MIM; 602675; gene.
DR neXtProt; NX_Q9H4A4; -.
DR PharmGKB; PA34451; -.
DR eggNOG; COG0308; -.
DR HOVERGEN; HBG001274; -.
DR InParanoid; Q9H4A4; -.
DR KO; K01260; -.
DR OMA; RAFEILH; -.
DR OrthoDB; EOG7SJD42; -.
DR PhylomeDB; Q9H4A4; -.
DR ChiTaRS; RNPEP; human.
DR GeneWiki; RNPEP; -.
DR GenomeRNAi; 6051; -.
DR NextBio; 23595; -.
DR PRO; PR:Q9H4A4; -.
DR ArrayExpress; Q9H4A4; -.
DR Bgee; Q9H4A4; -.
DR CleanEx; HS_RNPEP; -.
DR Genevestigator; Q9H4A4; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004301; F:epoxide hydrolase activity; NAS:UniProtKB.
DR GO; GO:0008235; F:metalloexopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IC:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015571; Pept_M1_aminopeptidase-B.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_N.
DR PANTHER; PTHR11533; PTHR11533; 1.
DR PANTHER; PTHR11533:SF5; PTHR11533:SF5; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Complete proteome; Hydrolase;
KW Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism;
KW Protease; Reference proteome; Secreted; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 650 Aminopeptidase B.
FT /FTId=PRO_0000095088.
FT REGION 298 302 Substrate binding (By similarity).
FT ACT_SITE 326 326 Proton acceptor (By similarity).
FT METAL 325 325 Zinc; catalytic (By similarity).
FT METAL 329 329 Zinc; catalytic (By similarity).
FT METAL 348 348 Zinc; catalytic (By similarity).
FT SITE 414 414 Transition state stabilizer (By
FT similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 7 7 Phosphoserine.
FT MOD_RES 446 446 N6-acetyllysine.
FT VARIANT 579 579 V -> I (in dbSNP:rs3820439).
FT /FTId=VAR_051566.
FT CONFLICT 2 2 A -> V (in Ref. 2; CAC14047).
FT CONFLICT 11 14 GAAR -> ARPGGRCTPRRL (in Ref. 1;
FT CAC12957).
FT CONFLICT 149 149 G -> R (in Ref. 1; CAC12957).
FT CONFLICT 153 153 L -> V (in Ref. 1; CAC12957).
FT CONFLICT 208 210 STW -> RPG (in Ref. 1; CAC12957).
FT CONFLICT 262 262 Missing (in Ref. 1; CAC12957).
SQ SEQUENCE 650 AA; 72596 MW; 4C04FE09689F2487 CRC64;
MASGEHSPGS GAARRPLHSA QAVDVASASN FRAFELLHLH LDLRAEFGPP GPGAGSRGLS
GTAVLDLRCL EPEGAAELRL DSHPCLEVTA AALRRERPGS EEPPAEPVSF YTQPFSHYGQ
ALCVSFPQPC RAAERLQVLL TYRVGEGPGV CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP
CFDTPAVKYK YSALIEVPDG FTAVMSASTW EKRGPNKFFF QMCQPIPSYL IALAIGDLVS
AEVGPRSRVW AEPCLIDAAK EEYNGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF TMYAQRRIST
ILFGAAYTCL EAATGRALLR QHMDITGEEN PLNKLRVKIE PGVDPDDTYN ETPYEKGFCF
VSYLAHLVGD QDQFDSFLKA YVHEFKFRSI LADDFLDFYL EYFPELKKKR VDIIPGFEFD
RWLNTPGWPP YLPDLSPGDS LMKPAEELAQ LWAAEELDMK AIEAVAISPW KTYQLVYFLD
KILQKSPLPP GNVKKLGDTY PSISNARNAE LRLRWGQIVL KNDHQEDFWK VKEFLHNQGK
QKYTLPLYHA MMGGSEVAQT LAKETFASTA SQLHSNVVNY VQQIVAPKGS
//
ID AMPB_HUMAN Reviewed; 650 AA.
AC Q9H4A4; Q9BVM9; Q9H1D4; Q9NPT7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-MAR-2002, sequence version 2.
DT 22-JAN-2014, entry version 121.
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;
GN Name=RNPEP; Synonyms=APB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Piesse C., Tymms M., Garrafa E., Gouzy C., Lacasa M., Cadel S.,
RA Foulon T., Cohen P.;
RT "Human aminopeptidase B on chromosome 1q32.2: cDNA, genomic structure
RT and expression.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Kristensen T.;
RT "Human aminopeptidase B cDNA cloning.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-650.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-7, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Exopeptidase which selectively removes arginine and/or
CC lysine residues from the N-terminus of several peptide substrates
CC including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-
CC 1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4)
CC into leukotriene B4 (LTB-4) (By similarity).
CC -!- CATALYTIC ACTIVITY: Release of N-terminal Arg and Lys from
CC oligopeptides when P1' is not Pro. Also acts on arylamides of Arg
CC and Lys.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ242586; CAC12957.1; -; mRNA.
DR EMBL; AJ296161; CAC14047.1; -; mRNA.
DR EMBL; BC001064; AAH01064.1; -; mRNA.
DR EMBL; BC012166; AAH12166.1; -; mRNA.
DR EMBL; AL390139; CAB99087.1; -; mRNA.
DR PIR; T51870; T51870.
DR RefSeq; NP_064601.3; NM_020216.3.
DR RefSeq; XP_005245477.1; XM_005245420.1.
DR RefSeq; XP_005245478.1; XM_005245421.1.
DR UniGene; Hs.497391; -.
DR ProteinModelPortal; Q9H4A4; -.
DR SMR; Q9H4A4; 8-643.
DR IntAct; Q9H4A4; 1.
DR MINT; MINT-1182309; -.
DR STRING; 9606.ENSP00000295640; -.
DR BindingDB; Q9H4A4; -.
DR ChEMBL; CHEMBL2432; -.
DR MEROPS; M01.014; -.
DR PhosphoSite; Q9H4A4; -.
DR DMDM; 20137480; -.
DR PaxDb; Q9H4A4; -.
DR PRIDE; Q9H4A4; -.
DR DNASU; 6051; -.
DR Ensembl; ENST00000295640; ENSP00000295640; ENSG00000176393.
DR GeneID; 6051; -.
DR KEGG; hsa:6051; -.
DR UCSC; uc001gxd.3; human.
DR CTD; 6051; -.
DR GeneCards; GC01P201951; -.
DR H-InvDB; HIX0023896; -.
DR HGNC; HGNC:10078; RNPEP.
DR HPA; HPA036075; -.
DR MIM; 602675; gene.
DR neXtProt; NX_Q9H4A4; -.
DR PharmGKB; PA34451; -.
DR eggNOG; COG0308; -.
DR HOVERGEN; HBG001274; -.
DR InParanoid; Q9H4A4; -.
DR KO; K01260; -.
DR OMA; RAFEILH; -.
DR OrthoDB; EOG7SJD42; -.
DR PhylomeDB; Q9H4A4; -.
DR ChiTaRS; RNPEP; human.
DR GeneWiki; RNPEP; -.
DR GenomeRNAi; 6051; -.
DR NextBio; 23595; -.
DR PRO; PR:Q9H4A4; -.
DR ArrayExpress; Q9H4A4; -.
DR Bgee; Q9H4A4; -.
DR CleanEx; HS_RNPEP; -.
DR Genevestigator; Q9H4A4; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004301; F:epoxide hydrolase activity; NAS:UniProtKB.
DR GO; GO:0008235; F:metalloexopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IC:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015571; Pept_M1_aminopeptidase-B.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_N.
DR PANTHER; PTHR11533; PTHR11533; 1.
DR PANTHER; PTHR11533:SF5; PTHR11533:SF5; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Complete proteome; Hydrolase;
KW Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism;
KW Protease; Reference proteome; Secreted; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 650 Aminopeptidase B.
FT /FTId=PRO_0000095088.
FT REGION 298 302 Substrate binding (By similarity).
FT ACT_SITE 326 326 Proton acceptor (By similarity).
FT METAL 325 325 Zinc; catalytic (By similarity).
FT METAL 329 329 Zinc; catalytic (By similarity).
FT METAL 348 348 Zinc; catalytic (By similarity).
FT SITE 414 414 Transition state stabilizer (By
FT similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 7 7 Phosphoserine.
FT MOD_RES 446 446 N6-acetyllysine.
FT VARIANT 579 579 V -> I (in dbSNP:rs3820439).
FT /FTId=VAR_051566.
FT CONFLICT 2 2 A -> V (in Ref. 2; CAC14047).
FT CONFLICT 11 14 GAAR -> ARPGGRCTPRRL (in Ref. 1;
FT CAC12957).
FT CONFLICT 149 149 G -> R (in Ref. 1; CAC12957).
FT CONFLICT 153 153 L -> V (in Ref. 1; CAC12957).
FT CONFLICT 208 210 STW -> RPG (in Ref. 1; CAC12957).
FT CONFLICT 262 262 Missing (in Ref. 1; CAC12957).
SQ SEQUENCE 650 AA; 72596 MW; 4C04FE09689F2487 CRC64;
MASGEHSPGS GAARRPLHSA QAVDVASASN FRAFELLHLH LDLRAEFGPP GPGAGSRGLS
GTAVLDLRCL EPEGAAELRL DSHPCLEVTA AALRRERPGS EEPPAEPVSF YTQPFSHYGQ
ALCVSFPQPC RAAERLQVLL TYRVGEGPGV CWLAPEQTAG KKKPFVYTQG QAVLNRAFFP
CFDTPAVKYK YSALIEVPDG FTAVMSASTW EKRGPNKFFF QMCQPIPSYL IALAIGDLVS
AEVGPRSRVW AEPCLIDAAK EEYNGVIEEF LATGEKLFGP YVWGRYDLLF MPPSFPFGGM
ENPCLTFVTP CLLAGDRSLA DVIIHEISHS WFGNLVTNAN WGEFWLNEGF TMYAQRRIST
ILFGAAYTCL EAATGRALLR QHMDITGEEN PLNKLRVKIE PGVDPDDTYN ETPYEKGFCF
VSYLAHLVGD QDQFDSFLKA YVHEFKFRSI LADDFLDFYL EYFPELKKKR VDIIPGFEFD
RWLNTPGWPP YLPDLSPGDS LMKPAEELAQ LWAAEELDMK AIEAVAISPW KTYQLVYFLD
KILQKSPLPP GNVKKLGDTY PSISNARNAE LRLRWGQIVL KNDHQEDFWK VKEFLHNQGK
QKYTLPLYHA MMGGSEVAQT LAKETFASTA SQLHSNVVNY VQQIVAPKGS
//
MIM
602675
*RECORD*
*FIELD* NO
602675
*FIELD* TI
*602675 ARGINYL AMINOPEPTIDASE; RNPEP
;;AMINOPEPTIDASE B
*FIELD* TX
Aminopeptidase B (EC 3.4.11.6) was originally defined as an exopeptidase
read morecapable of trimming basic amino acid residues from the NH2 terminus of
peptide substrates (Hopsu et al., 1964). Cadel et al. (1995)
demonstrated that it is a Zn(2+)-dependent exopeptidase that selectively
removes arginine and/or lysine residues from the N terminus of several
peptide substrates. Structurally it is related to leukotriene A4
hydrolase (151570), an important enzyme of the arachidonic acid pathway.
The structural relationship has its functional counterpart in the
capacity of aminopeptidase B to hydrolyze leukotriene A4 (Cadel et al.,
1997). Antibodies raised against the isolated peptidase show that it is
widely distributed in a number of tissues, including endocrine and
nonendocrine cell types. It is secreted by rat PC12 pheochromocytoma
cells and associated with the external face of their plasma membrane.
Together these data strongly argue in favor of participation of this
ubiquitous and in vitro bifunctional enzyme in the final stages of
precursor processing mechanisms occurring either during the
intracellular transport along the secretory pathway or at the plasma
membrane level, or both (Aurich-Costa et al., 1997).
By fluorescence in situ hybridization, Aurich-Costa et al. (1997) mapped
the RNPEP gene to 1q32.1-q32.2.
*FIELD* RF
1. Aurich-Costa, J.; Cadel, S.; Gouzy, C.; Foulon, T.; Cherif, D.;
Cohen, P.: Assignment of the aminopeptidase B gene (RNPEP) to human
chromosome 1 band q32 by in situ hybridization. Cytogenet. Cell Genet. 79:
143-144, 1997.
2. Cadel, S.; Foulon, T.; Viron, A.; Balogh, A.; Midol-Monnet, S.;
Noel, N.; Cohen, P.: Aminopeptidase B from the rat testis is a bifunctional
enzyme structurally related to leukotriene-A4 hydrolase. Proc. Nat.
Acad. Sci. 94: 2963-2968, 1997.
3. Cadel, S.; Pierotti, A. R.; Foulton, T.; Creminon, C.; Barre, N.;
Segretain, D.; Cohen, P.: Aminopeptidase-B in the rat testes: isolation,
functional properties and cellular localization in the seminiferous
tubules. Molec. Cell. Endocr. 110: 149-160, 1995.
4. Hopsu, V. K.; Kantonen, U. M.; Glenner, G. G.: A peptidase from
rat tissues selectively hydrolyzing N-terminal arginine and lysine
residues. Life Sci. 3: 1449-1453, 1964.
*FIELD* CD
Victor A. McKusick: 6/2/1998
*FIELD* ED
carol: 05/18/1999
dholmes: 7/2/1998
carol: 6/2/1998
*RECORD*
*FIELD* NO
602675
*FIELD* TI
*602675 ARGINYL AMINOPEPTIDASE; RNPEP
;;AMINOPEPTIDASE B
*FIELD* TX
Aminopeptidase B (EC 3.4.11.6) was originally defined as an exopeptidase
read morecapable of trimming basic amino acid residues from the NH2 terminus of
peptide substrates (Hopsu et al., 1964). Cadel et al. (1995)
demonstrated that it is a Zn(2+)-dependent exopeptidase that selectively
removes arginine and/or lysine residues from the N terminus of several
peptide substrates. Structurally it is related to leukotriene A4
hydrolase (151570), an important enzyme of the arachidonic acid pathway.
The structural relationship has its functional counterpart in the
capacity of aminopeptidase B to hydrolyze leukotriene A4 (Cadel et al.,
1997). Antibodies raised against the isolated peptidase show that it is
widely distributed in a number of tissues, including endocrine and
nonendocrine cell types. It is secreted by rat PC12 pheochromocytoma
cells and associated with the external face of their plasma membrane.
Together these data strongly argue in favor of participation of this
ubiquitous and in vitro bifunctional enzyme in the final stages of
precursor processing mechanisms occurring either during the
intracellular transport along the secretory pathway or at the plasma
membrane level, or both (Aurich-Costa et al., 1997).
By fluorescence in situ hybridization, Aurich-Costa et al. (1997) mapped
the RNPEP gene to 1q32.1-q32.2.
*FIELD* RF
1. Aurich-Costa, J.; Cadel, S.; Gouzy, C.; Foulon, T.; Cherif, D.;
Cohen, P.: Assignment of the aminopeptidase B gene (RNPEP) to human
chromosome 1 band q32 by in situ hybridization. Cytogenet. Cell Genet. 79:
143-144, 1997.
2. Cadel, S.; Foulon, T.; Viron, A.; Balogh, A.; Midol-Monnet, S.;
Noel, N.; Cohen, P.: Aminopeptidase B from the rat testis is a bifunctional
enzyme structurally related to leukotriene-A4 hydrolase. Proc. Nat.
Acad. Sci. 94: 2963-2968, 1997.
3. Cadel, S.; Pierotti, A. R.; Foulton, T.; Creminon, C.; Barre, N.;
Segretain, D.; Cohen, P.: Aminopeptidase-B in the rat testes: isolation,
functional properties and cellular localization in the seminiferous
tubules. Molec. Cell. Endocr. 110: 149-160, 1995.
4. Hopsu, V. K.; Kantonen, U. M.; Glenner, G. G.: A peptidase from
rat tissues selectively hydrolyzing N-terminal arginine and lysine
residues. Life Sci. 3: 1449-1453, 1964.
*FIELD* CD
Victor A. McKusick: 6/2/1998
*FIELD* ED
carol: 05/18/1999
dholmes: 7/2/1998
carol: 6/2/1998