Full text data of DNPEP
DNPEP
(ASPEP, DAP)
[Confidence: low (only semi-automatic identification from reviews)]
Aspartyl aminopeptidase; 3.4.11.21
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Aspartyl aminopeptidase; 3.4.11.21
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9ULA0
ID DNPEP_HUMAN Reviewed; 475 AA.
AC Q9ULA0; Q9BW44; Q9NUV5;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Aspartyl aminopeptidase;
DE EC=3.4.11.21;
GN Name=DNPEP; Synonyms=ASPEP, DAP;
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], AND CHARACTERIZATION.
RX PubMed=9632644; DOI=10.1074/jbc.273.26.15961;
RA Wilk S., Wilk E., Magnusson R.P.;
RT "Purification, characterization, and cloning of a cytosolic aspartyl
RT aminopeptidase.";
RL J. Biol. Chem. 273:15961-15970(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-468 IN COMPLEX WITH
RP SUBSTRATE ANALOG, ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, AND
RP SUBUNIT.
RX PubMed=22720794; DOI=10.1186/1472-6807-12-14;
RA Chaikuad A., Pilka E.S., Riso A.D., Delft F.V., Kavanagh K.L.,
RA Venien-Bryan C., Oppermann U., Yue W.W.;
RT "Structure of human aspartyl aminopeptidase complexed with substrate
RT analogue: insight into catalytic mechanism, substrate specificity and
RT M18 peptidase family.";
RL BMC Struct. Biol. 12:14-14(2012).
CC -!- FUNCTION: Aminopeptidase with specificity towards an acidic amino
CC acid at the N-terminus. Likely to play an important role in
CC intracellular protein and peptide metabolism.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal aspartate or
CC glutamate from a peptide, with a preference for aspartate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit.
CC -!- ENZYME REGULATION: One of the zinc ions is readily exchangeable
CC with other divalent cations such as manganese, which strongly
CC stimulates the enzymatic activity (By similarity).
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six
CC homodimers.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92014.1; Type=Erroneous initiation;
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; AF005050; AAD01211.2; -; mRNA.
DR EMBL; AK001977; BAA92014.1; ALT_INIT; mRNA.
DR EMBL; AC053503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000653; AAH00653.2; -; mRNA.
DR RefSeq; NP_036232.2; NM_012100.2.
DR UniGene; Hs.258551; -.
DR PDB; 4DYO; X-ray; 2.20 A; A=1-468.
DR PDBsum; 4DYO; -.
DR ProteinModelPortal; Q9ULA0; -.
DR SMR; Q9ULA0; 7-472.
DR IntAct; Q9ULA0; 3.
DR STRING; 9606.ENSP00000273075; -.
DR BindingDB; Q9ULA0; -.
DR ChEMBL; CHEMBL2761; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR MEROPS; M18.002; -.
DR DMDM; 17367145; -.
DR PaxDb; Q9ULA0; -.
DR PRIDE; Q9ULA0; -.
DR DNASU; 23549; -.
DR Ensembl; ENST00000273075; ENSP00000273075; ENSG00000123992.
DR GeneID; 23549; -.
DR KEGG; hsa:23549; -.
DR UCSC; uc002vle.2; human.
DR CTD; 23549; -.
DR GeneCards; GC02M220238; -.
DR HGNC; HGNC:2981; DNPEP.
DR HPA; HPA036398; -.
DR HPA; HPA044860; -.
DR MIM; 611367; gene.
DR neXtProt; NX_Q9ULA0; -.
DR PharmGKB; PA27448; -.
DR eggNOG; COG1362; -.
DR HOVERGEN; HBG051386; -.
DR InParanoid; Q9ULA0; -.
DR KO; K01267; -.
DR OrthoDB; EOG789CB1; -.
DR GeneWiki; DNPEP; -.
DR GenomeRNAi; 23549; -.
DR NextBio; 46092; -.
DR PRO; PR:Q9ULA0; -.
DR ArrayExpress; Q9ULA0; -.
DR Bgee; Q9ULA0; -.
DR CleanEx; HS_DAP; -.
DR CleanEx; HS_DNPEP; -.
DR Genevestigator; Q9ULA0; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0004177; F:aminopeptidase activity; TAS:ProtInc.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminopeptidase; Complete proteome;
KW Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1 475 Aspartyl aminopeptidase.
FT /FTId=PRO_0000173451.
FT METAL 94 94 Zinc 1.
FT METAL 264 264 Zinc 1.
FT METAL 264 264 Zinc 2.
FT METAL 302 302 Zinc 2.
FT METAL 346 346 Zinc 1.
FT METAL 440 440 Zinc 2.
FT BINDING 170 170 Substrate.
FT BINDING 301 301 Substrate.
FT BINDING 346 346 Substrate.
FT BINDING 349 349 Substrate.
FT BINDING 374 374 Substrate.
FT BINDING 381 381 Substrate.
FT MOD_RES 1 1 N-acetylmethionine.
FT CONFLICT 119 119 E -> V (in Ref. 2; BAA92014).
FT HELIX 8 26
FT HELIX 31 44
FT STRAND 63 68
FT TURN 69 71
FT STRAND 72 78
FT STRAND 88 94
FT STRAND 99 110
FT STRAND 113 123
FT HELIX 126 129
FT STRAND 134 143
FT TURN 145 147
FT STRAND 150 156
FT HELIX 169 171
FT TURN 173 177
FT TURN 183 186
FT STRAND 190 193
FT HELIX 194 200
FT HELIX 218 228
FT HELIX 232 234
FT STRAND 235 244
FT STRAND 249 251
FT TURN 252 255
FT STRAND 257 260
FT HELIX 263 279
FT TURN 283 288
FT STRAND 291 299
FT HELIX 301 303
FT HELIX 315 324
FT HELIX 332 336
FT HELIX 337 339
FT STRAND 341 345
FT HELIX 356 358
FT STRAND 372 374
FT TURN 377 380
FT HELIX 385 398
FT STRAND 403 405
FT HELIX 417 425
FT STRAND 428 433
FT STRAND 435 438
FT STRAND 441 448
FT HELIX 449 468
SQ SEQUENCE 475 AA; 52428 MW; A02BDCFB516BD081 CRC64;
MQVAMNGKAR KEAVQTAAKE LLKFVNRSPS PFHAVAECRN RLLQAGFSEL KETEKWNIKP
ESKYFMTRNS STIIAFAVGG QYVPGNGFSL IGAHTDSPCL RVKRRSRRSQ VGFQQVGVET
YGGGIWSTWF DRDLTLAGRV IVKCPTSGRL EQQLVHVERP ILRIPHLAIH LQRNINENFG
PNTEMHLVPI LATAIQEELE KGTPEPGPLN AVDERHHSVL MSLLCAHLGL SPKDIVEMEL
CLADTQPAVL GGAYDEFIFA PRLDNLHSCF CALQALIDSC AGPGSLATEP HVRMVTLYDN
EEVGSESAQG AQSLLTELVL RRISASCQHP TAFEEAIPKS FMISADMAHA VHPNYLDKHE
ENHRPLFHKG PVIKVNSKQR YASNAVSEAL IREVANKVKV PLQDLMVRND TPCGTTIGPI
LASRLGLRVL DLGSPQLAMH SIREMACTTG VLQTLTLFKG FFELFPSLSH NLLVD
//
ID DNPEP_HUMAN Reviewed; 475 AA.
AC Q9ULA0; Q9BW44; Q9NUV5;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Aspartyl aminopeptidase;
DE EC=3.4.11.21;
GN Name=DNPEP; Synonyms=ASPEP, DAP;
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], AND CHARACTERIZATION.
RX PubMed=9632644; DOI=10.1074/jbc.273.26.15961;
RA Wilk S., Wilk E., Magnusson R.P.;
RT "Purification, characterization, and cloning of a cytosolic aspartyl
RT aminopeptidase.";
RL J. Biol. Chem. 273:15961-15970(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-468 IN COMPLEX WITH
RP SUBSTRATE ANALOG, ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, AND
RP SUBUNIT.
RX PubMed=22720794; DOI=10.1186/1472-6807-12-14;
RA Chaikuad A., Pilka E.S., Riso A.D., Delft F.V., Kavanagh K.L.,
RA Venien-Bryan C., Oppermann U., Yue W.W.;
RT "Structure of human aspartyl aminopeptidase complexed with substrate
RT analogue: insight into catalytic mechanism, substrate specificity and
RT M18 peptidase family.";
RL BMC Struct. Biol. 12:14-14(2012).
CC -!- FUNCTION: Aminopeptidase with specificity towards an acidic amino
CC acid at the N-terminus. Likely to play an important role in
CC intracellular protein and peptide metabolism.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal aspartate or
CC glutamate from a peptide, with a preference for aspartate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit.
CC -!- ENZYME REGULATION: One of the zinc ions is readily exchangeable
CC with other divalent cations such as manganese, which strongly
CC stimulates the enzymatic activity (By similarity).
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six
CC homodimers.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92014.1; Type=Erroneous initiation;
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; AF005050; AAD01211.2; -; mRNA.
DR EMBL; AK001977; BAA92014.1; ALT_INIT; mRNA.
DR EMBL; AC053503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000653; AAH00653.2; -; mRNA.
DR RefSeq; NP_036232.2; NM_012100.2.
DR UniGene; Hs.258551; -.
DR PDB; 4DYO; X-ray; 2.20 A; A=1-468.
DR PDBsum; 4DYO; -.
DR ProteinModelPortal; Q9ULA0; -.
DR SMR; Q9ULA0; 7-472.
DR IntAct; Q9ULA0; 3.
DR STRING; 9606.ENSP00000273075; -.
DR BindingDB; Q9ULA0; -.
DR ChEMBL; CHEMBL2761; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR MEROPS; M18.002; -.
DR DMDM; 17367145; -.
DR PaxDb; Q9ULA0; -.
DR PRIDE; Q9ULA0; -.
DR DNASU; 23549; -.
DR Ensembl; ENST00000273075; ENSP00000273075; ENSG00000123992.
DR GeneID; 23549; -.
DR KEGG; hsa:23549; -.
DR UCSC; uc002vle.2; human.
DR CTD; 23549; -.
DR GeneCards; GC02M220238; -.
DR HGNC; HGNC:2981; DNPEP.
DR HPA; HPA036398; -.
DR HPA; HPA044860; -.
DR MIM; 611367; gene.
DR neXtProt; NX_Q9ULA0; -.
DR PharmGKB; PA27448; -.
DR eggNOG; COG1362; -.
DR HOVERGEN; HBG051386; -.
DR InParanoid; Q9ULA0; -.
DR KO; K01267; -.
DR OrthoDB; EOG789CB1; -.
DR GeneWiki; DNPEP; -.
DR GenomeRNAi; 23549; -.
DR NextBio; 46092; -.
DR PRO; PR:Q9ULA0; -.
DR ArrayExpress; Q9ULA0; -.
DR Bgee; Q9ULA0; -.
DR CleanEx; HS_DAP; -.
DR CleanEx; HS_DNPEP; -.
DR Genevestigator; Q9ULA0; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0004177; F:aminopeptidase activity; TAS:ProtInc.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminopeptidase; Complete proteome;
KW Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1 475 Aspartyl aminopeptidase.
FT /FTId=PRO_0000173451.
FT METAL 94 94 Zinc 1.
FT METAL 264 264 Zinc 1.
FT METAL 264 264 Zinc 2.
FT METAL 302 302 Zinc 2.
FT METAL 346 346 Zinc 1.
FT METAL 440 440 Zinc 2.
FT BINDING 170 170 Substrate.
FT BINDING 301 301 Substrate.
FT BINDING 346 346 Substrate.
FT BINDING 349 349 Substrate.
FT BINDING 374 374 Substrate.
FT BINDING 381 381 Substrate.
FT MOD_RES 1 1 N-acetylmethionine.
FT CONFLICT 119 119 E -> V (in Ref. 2; BAA92014).
FT HELIX 8 26
FT HELIX 31 44
FT STRAND 63 68
FT TURN 69 71
FT STRAND 72 78
FT STRAND 88 94
FT STRAND 99 110
FT STRAND 113 123
FT HELIX 126 129
FT STRAND 134 143
FT TURN 145 147
FT STRAND 150 156
FT HELIX 169 171
FT TURN 173 177
FT TURN 183 186
FT STRAND 190 193
FT HELIX 194 200
FT HELIX 218 228
FT HELIX 232 234
FT STRAND 235 244
FT STRAND 249 251
FT TURN 252 255
FT STRAND 257 260
FT HELIX 263 279
FT TURN 283 288
FT STRAND 291 299
FT HELIX 301 303
FT HELIX 315 324
FT HELIX 332 336
FT HELIX 337 339
FT STRAND 341 345
FT HELIX 356 358
FT STRAND 372 374
FT TURN 377 380
FT HELIX 385 398
FT STRAND 403 405
FT HELIX 417 425
FT STRAND 428 433
FT STRAND 435 438
FT STRAND 441 448
FT HELIX 449 468
SQ SEQUENCE 475 AA; 52428 MW; A02BDCFB516BD081 CRC64;
MQVAMNGKAR KEAVQTAAKE LLKFVNRSPS PFHAVAECRN RLLQAGFSEL KETEKWNIKP
ESKYFMTRNS STIIAFAVGG QYVPGNGFSL IGAHTDSPCL RVKRRSRRSQ VGFQQVGVET
YGGGIWSTWF DRDLTLAGRV IVKCPTSGRL EQQLVHVERP ILRIPHLAIH LQRNINENFG
PNTEMHLVPI LATAIQEELE KGTPEPGPLN AVDERHHSVL MSLLCAHLGL SPKDIVEMEL
CLADTQPAVL GGAYDEFIFA PRLDNLHSCF CALQALIDSC AGPGSLATEP HVRMVTLYDN
EEVGSESAQG AQSLLTELVL RRISASCQHP TAFEEAIPKS FMISADMAHA VHPNYLDKHE
ENHRPLFHKG PVIKVNSKQR YASNAVSEAL IREVANKVKV PLQDLMVRND TPCGTTIGPI
LASRLGLRVL DLGSPQLAMH SIREMACTTG VLQTLTLFKG FFELFPSLSH NLLVD
//
MIM
611367
*RECORD*
*FIELD* NO
611367
*FIELD* TI
*611367 ASPARTYL AMINOPEPTIDASE; DNPEP
;;ASPEP; DAP
*FIELD* TX
DESCRIPTION
Aspartyl aminopeptidase (EC 3.4.11.21) catalyzes the hydrolysis of
read moreN-terminal aspartyl and glutamyl residues (Wilk et al., 1998).
CLONING
By database analysis using tryptic peptide sequences from purified
rabbit brain cytosol aspartyl aminopeptidase as probe, Wilk et al.
(1998) identified and subsequently sequenced human aspartyl
aminopeptidase (DNPEP) as well as homologs in mouse and other species.
The deduced 490-amino acid human protein has a calculated molecular mass
of approximately 52 kD and shares similarity with S. cerevisiae
aminopeptidase I, a zinc metalloproteinase found in the vacuole.
Sequence analysis of the DNPEP protein in various species revealed
several conserved residues including 3 histidines, 3 glutamates, and 5
aspartates. Northern blot analysis of rat tissues detected a 1.9-kb
Dnpep transcript in all tissues examined, with highest expression in
testis, intermediate expression in kidney and lung, and lesser but
significant expression in spleen, liver, and brain.
GENE FUNCTION
Using recombinant DNPEP expressed in E. coli, Wilk et al. (1998) showed
that human DNPEP catalyzed the dipeptidylpeptidase IV (DPP4;
102720)-dependent hydrolysis of the Asp-Ala bond in the substrate
Asp-Ala-Pro-SM at a specific activity of 5.5-47.6 units/mg. DNPEP
activity was inhibited by 0.4 mM Zn(2+), was not affected by addition of
puromycin, and was significantly reduced when a beta-carboxyl-blocked
substrate was substituted.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DNPEP
gene to chromosome 2q (TMAP SHGC-32022).
*FIELD* RF
1. Wilk, S.; Wilk, E.; Magnusson, R. P.: Purification, characterization,
and cloning of a cytosolic aspartyl aminopeptidase. J. Biol. Chem. 273:
15961-15970, 1998.
*FIELD* CD
Dorothy S. Reilly: 8/22/2007
*FIELD* ED
carol: 08/22/2007
carol: 8/22/2007
*RECORD*
*FIELD* NO
611367
*FIELD* TI
*611367 ASPARTYL AMINOPEPTIDASE; DNPEP
;;ASPEP; DAP
*FIELD* TX
DESCRIPTION
Aspartyl aminopeptidase (EC 3.4.11.21) catalyzes the hydrolysis of
read moreN-terminal aspartyl and glutamyl residues (Wilk et al., 1998).
CLONING
By database analysis using tryptic peptide sequences from purified
rabbit brain cytosol aspartyl aminopeptidase as probe, Wilk et al.
(1998) identified and subsequently sequenced human aspartyl
aminopeptidase (DNPEP) as well as homologs in mouse and other species.
The deduced 490-amino acid human protein has a calculated molecular mass
of approximately 52 kD and shares similarity with S. cerevisiae
aminopeptidase I, a zinc metalloproteinase found in the vacuole.
Sequence analysis of the DNPEP protein in various species revealed
several conserved residues including 3 histidines, 3 glutamates, and 5
aspartates. Northern blot analysis of rat tissues detected a 1.9-kb
Dnpep transcript in all tissues examined, with highest expression in
testis, intermediate expression in kidney and lung, and lesser but
significant expression in spleen, liver, and brain.
GENE FUNCTION
Using recombinant DNPEP expressed in E. coli, Wilk et al. (1998) showed
that human DNPEP catalyzed the dipeptidylpeptidase IV (DPP4;
102720)-dependent hydrolysis of the Asp-Ala bond in the substrate
Asp-Ala-Pro-SM at a specific activity of 5.5-47.6 units/mg. DNPEP
activity was inhibited by 0.4 mM Zn(2+), was not affected by addition of
puromycin, and was significantly reduced when a beta-carboxyl-blocked
substrate was substituted.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DNPEP
gene to chromosome 2q (TMAP SHGC-32022).
*FIELD* RF
1. Wilk, S.; Wilk, E.; Magnusson, R. P.: Purification, characterization,
and cloning of a cytosolic aspartyl aminopeptidase. J. Biol. Chem. 273:
15961-15970, 1998.
*FIELD* CD
Dorothy S. Reilly: 8/22/2007
*FIELD* ED
carol: 08/22/2007
carol: 8/22/2007