Full text data of LAP3
LAP3
(LAPEP, PEPS)
[Confidence: low (only semi-automatic identification from reviews)]
Cytosol aminopeptidase; 3.4.11.1 (Leucine aminopeptidase 3; LAP-3; Leucyl aminopeptidase; Peptidase S; Proline aminopeptidase; 3.4.11.5; Prolyl aminopeptidase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cytosol aminopeptidase; 3.4.11.1 (Leucine aminopeptidase 3; LAP-3; Leucyl aminopeptidase; Peptidase S; Proline aminopeptidase; 3.4.11.5; Prolyl aminopeptidase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P28838
ID AMPL_HUMAN Reviewed; 519 AA.
AC P28838; B3KMQ3; Q6IAM6; Q6P0L6; Q9UQE3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 143.
DE RecName: Full=Cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase 3;
DE Short=LAP-3;
DE AltName: Full=Leucyl aminopeptidase;
DE AltName: Full=Peptidase S;
DE AltName: Full=Proline aminopeptidase;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase;
GN Name=LAP3; Synonyms=LAPEP, PEPS;
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] (ISOFORM 1).
RA Mao M., Liu T., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J.,
RA Yu Y., Wang Z., Chen S., Chen Z.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and 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 [5]
RP PROTEIN SEQUENCE OF 33-54.
RC TISSUE=Liver;
RX PubMed=1908238; DOI=10.1016/0006-291X(91)91057-J;
RA Matsushima M., Takahashi T., Ichinose M., Miki K., Kurokawa K.,
RA Takahashi K.;
RT "Structural and immunological evidence for the identity of prolyl
RT aminopeptidase with leucyl aminopeptidase.";
RL Biochem. Biophys. Res. Commun. 178:1459-1464(1991).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASS
RP SPECTROMETRY.
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).
CC -!- FUNCTION: Presumably involved in the processing and regular
CC turnover of intracellular proteins. Catalyzes the removal of
CC unsubstituted N-terminal amino acids from various peptides.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC acid amides and methyl esters are also readily hydrolyzed, but
CC rates on arylamides are exceedingly low.
CC -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide.
CC -!- COFACTOR: Binds 2 zinc ions per subunit. One zinc ion is tightly
CC bound and essential for enzyme activity, while the second metal
CC coordination site can be occupied by zinc, magnesium or manganese
CC to give enzymes of different activities (By similarity).
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P28838-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28838-2; Sequence=VSP_022631;
CC Note=Initiator Met-1 is removed;
CC -!- SIMILARITY: Belongs to the peptidase M17 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; AF061738; AAD17527.1; -; mRNA.
DR EMBL; CR457128; CAG33409.1; -; mRNA.
DR EMBL; AK022055; BAG51065.1; -; mRNA.
DR EMBL; AK298613; BAG60795.1; -; mRNA.
DR EMBL; BC065564; AAH65564.1; -; mRNA.
DR EMBL; BC006199; AAH06199.3; -; mRNA.
DR PIR; PT0431; PT0431.
DR RefSeq; NP_056991.2; NM_015907.2.
DR UniGene; Hs.570791; -.
DR ProteinModelPortal; P28838; -.
DR SMR; P28838; 33-516.
DR IntAct; P28838; 7.
DR MINT; MINT-2802173; -.
DR STRING; 9606.ENSP00000226299; -.
DR BindingDB; P28838; -.
DR ChEMBL; CHEMBL3965; -.
DR MEROPS; M17.001; -.
DR PhosphoSite; P28838; -.
DR DMDM; 124028615; -.
DR REPRODUCTION-2DPAGE; IPI00789806; -.
DR REPRODUCTION-2DPAGE; P28838; -.
DR UCD-2DPAGE; P28838; -.
DR PaxDb; P28838; -.
DR PRIDE; P28838; -.
DR Ensembl; ENST00000226299; ENSP00000226299; ENSG00000002549.
DR Ensembl; ENST00000606142; ENSP00000476028; ENSG00000002549.
DR GeneID; 51056; -.
DR KEGG; hsa:51056; -.
DR UCSC; uc003gph.1; human.
DR CTD; 51056; -.
DR GeneCards; GC04P017578; -.
DR H-InvDB; HIX0004121; -.
DR HGNC; HGNC:18449; LAP3.
DR HPA; HPA029606; -.
DR HPA; HPA029607; -.
DR MIM; 170250; gene.
DR neXtProt; NX_P28838; -.
DR PharmGKB; PA38537; -.
DR eggNOG; COG0260; -.
DR HOGENOM; HOG000243129; -.
DR HOVERGEN; HBG003320; -.
DR InParanoid; P28838; -.
DR KO; K11142; -.
DR OMA; ESLMSVM; -.
DR OrthoDB; EOG7F24SG; -.
DR PhylomeDB; P28838; -.
DR ChiTaRS; LAP3; human.
DR GenomeRNAi; 51056; -.
DR NextBio; 53624; -.
DR PRO; PR:P28838; -.
DR ArrayExpress; P28838; -.
DR Bgee; P28838; -.
DR CleanEx; HS_LAP3; -.
DR Genevestigator; P28838; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0004177; F:aminopeptidase activity; NAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; NAS:UniProtKB.
DR GO; GO:0008235; F:metalloexopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963:SF3; PTHR11963:SF3; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Aminopeptidase;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Phosphoprotein; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1 519 Cytosol aminopeptidase.
FT /FTId=PRO_0000165825.
FT ACT_SITE 294 294 By similarity.
FT ACT_SITE 368 368 By similarity.
FT METAL 282 282 Zinc 2 (By similarity).
FT METAL 287 287 Zinc 1 (By similarity).
FT METAL 287 287 Zinc 2 (By similarity).
FT METAL 305 305 Zinc 2 (By similarity).
FT METAL 364 364 Zinc 1 (By similarity).
FT METAL 366 366 Zinc 1 (By similarity).
FT METAL 366 366 Zinc 2 (By similarity).
FT MOD_RES 180 180 Phosphoserine (By similarity).
FT MOD_RES 221 221 N6-acetyllysine.
FT MOD_RES 238 238 Phosphoserine.
FT MOD_RES 455 455 N6-acetyllysine (By similarity).
FT MOD_RES 489 489 N6-acetyllysine (By similarity).
FT VAR_SEQ 1 31 Missing (in isoform 2).
FT /FTId=VSP_022631.
FT CONFLICT 20 20 R -> V (in Ref. 1; AAD17527).
FT CONFLICT 22 22 F -> S (in Ref. 1; AAD17527).
FT CONFLICT 29 29 T -> A (in Ref. 2; CAG33409).
SQ SEQUENCE 519 AA; 56166 MW; D960F8F5B9024585 CRC64;
MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD
KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN
IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS
GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI
EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV
DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE
ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL
DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA
//
ID AMPL_HUMAN Reviewed; 519 AA.
AC P28838; B3KMQ3; Q6IAM6; Q6P0L6; Q9UQE3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 143.
DE RecName: Full=Cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase 3;
DE Short=LAP-3;
DE AltName: Full=Leucyl aminopeptidase;
DE AltName: Full=Peptidase S;
DE AltName: Full=Proline aminopeptidase;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase;
GN Name=LAP3; Synonyms=LAPEP, PEPS;
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] (ISOFORM 1).
RA Mao M., Liu T., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J.,
RA Yu Y., Wang Z., Chen S., Chen Z.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and 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 [5]
RP PROTEIN SEQUENCE OF 33-54.
RC TISSUE=Liver;
RX PubMed=1908238; DOI=10.1016/0006-291X(91)91057-J;
RA Matsushima M., Takahashi T., Ichinose M., Miki K., Kurokawa K.,
RA Takahashi K.;
RT "Structural and immunological evidence for the identity of prolyl
RT aminopeptidase with leucyl aminopeptidase.";
RL Biochem. Biophys. Res. Commun. 178:1459-1464(1991).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASS
RP SPECTROMETRY.
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).
CC -!- FUNCTION: Presumably involved in the processing and regular
CC turnover of intracellular proteins. Catalyzes the removal of
CC unsubstituted N-terminal amino acids from various peptides.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC acid amides and methyl esters are also readily hydrolyzed, but
CC rates on arylamides are exceedingly low.
CC -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide.
CC -!- COFACTOR: Binds 2 zinc ions per subunit. One zinc ion is tightly
CC bound and essential for enzyme activity, while the second metal
CC coordination site can be occupied by zinc, magnesium or manganese
CC to give enzymes of different activities (By similarity).
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P28838-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28838-2; Sequence=VSP_022631;
CC Note=Initiator Met-1 is removed;
CC -!- SIMILARITY: Belongs to the peptidase M17 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; AF061738; AAD17527.1; -; mRNA.
DR EMBL; CR457128; CAG33409.1; -; mRNA.
DR EMBL; AK022055; BAG51065.1; -; mRNA.
DR EMBL; AK298613; BAG60795.1; -; mRNA.
DR EMBL; BC065564; AAH65564.1; -; mRNA.
DR EMBL; BC006199; AAH06199.3; -; mRNA.
DR PIR; PT0431; PT0431.
DR RefSeq; NP_056991.2; NM_015907.2.
DR UniGene; Hs.570791; -.
DR ProteinModelPortal; P28838; -.
DR SMR; P28838; 33-516.
DR IntAct; P28838; 7.
DR MINT; MINT-2802173; -.
DR STRING; 9606.ENSP00000226299; -.
DR BindingDB; P28838; -.
DR ChEMBL; CHEMBL3965; -.
DR MEROPS; M17.001; -.
DR PhosphoSite; P28838; -.
DR DMDM; 124028615; -.
DR REPRODUCTION-2DPAGE; IPI00789806; -.
DR REPRODUCTION-2DPAGE; P28838; -.
DR UCD-2DPAGE; P28838; -.
DR PaxDb; P28838; -.
DR PRIDE; P28838; -.
DR Ensembl; ENST00000226299; ENSP00000226299; ENSG00000002549.
DR Ensembl; ENST00000606142; ENSP00000476028; ENSG00000002549.
DR GeneID; 51056; -.
DR KEGG; hsa:51056; -.
DR UCSC; uc003gph.1; human.
DR CTD; 51056; -.
DR GeneCards; GC04P017578; -.
DR H-InvDB; HIX0004121; -.
DR HGNC; HGNC:18449; LAP3.
DR HPA; HPA029606; -.
DR HPA; HPA029607; -.
DR MIM; 170250; gene.
DR neXtProt; NX_P28838; -.
DR PharmGKB; PA38537; -.
DR eggNOG; COG0260; -.
DR HOGENOM; HOG000243129; -.
DR HOVERGEN; HBG003320; -.
DR InParanoid; P28838; -.
DR KO; K11142; -.
DR OMA; ESLMSVM; -.
DR OrthoDB; EOG7F24SG; -.
DR PhylomeDB; P28838; -.
DR ChiTaRS; LAP3; human.
DR GenomeRNAi; 51056; -.
DR NextBio; 53624; -.
DR PRO; PR:P28838; -.
DR ArrayExpress; P28838; -.
DR Bgee; P28838; -.
DR CleanEx; HS_LAP3; -.
DR Genevestigator; P28838; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0004177; F:aminopeptidase activity; NAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; NAS:UniProtKB.
DR GO; GO:0008235; F:metalloexopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963:SF3; PTHR11963:SF3; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Aminopeptidase;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Phosphoprotein; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1 519 Cytosol aminopeptidase.
FT /FTId=PRO_0000165825.
FT ACT_SITE 294 294 By similarity.
FT ACT_SITE 368 368 By similarity.
FT METAL 282 282 Zinc 2 (By similarity).
FT METAL 287 287 Zinc 1 (By similarity).
FT METAL 287 287 Zinc 2 (By similarity).
FT METAL 305 305 Zinc 2 (By similarity).
FT METAL 364 364 Zinc 1 (By similarity).
FT METAL 366 366 Zinc 1 (By similarity).
FT METAL 366 366 Zinc 2 (By similarity).
FT MOD_RES 180 180 Phosphoserine (By similarity).
FT MOD_RES 221 221 N6-acetyllysine.
FT MOD_RES 238 238 Phosphoserine.
FT MOD_RES 455 455 N6-acetyllysine (By similarity).
FT MOD_RES 489 489 N6-acetyllysine (By similarity).
FT VAR_SEQ 1 31 Missing (in isoform 2).
FT /FTId=VSP_022631.
FT CONFLICT 20 20 R -> V (in Ref. 1; AAD17527).
FT CONFLICT 22 22 F -> S (in Ref. 1; AAD17527).
FT CONFLICT 29 29 T -> A (in Ref. 2; CAG33409).
SQ SEQUENCE 519 AA; 56166 MW; D960F8F5B9024585 CRC64;
MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD
KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN
IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS
GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI
EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV
DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE
ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL
DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA
//
MIM
170250
*RECORD*
*FIELD* NO
170250
*FIELD* TI
*170250 LEUCINE AMINOPEPTIDASE 3; LAP3
;;PEPTIDASE S; PEPS
*FIELD* TX
CLONING
Matsushima et al. (1991) presented evidence that prolyl aminopeptidases
read more(EC 3.4.11.5) purified from pig small intestine mucosa and human liver
and leucyl aminopeptidase (EC 3.4.11.1) purified from pig kidney were
identical. Both pig enzymes were indistinguishable in their molecular
mass (about 300 kD), subunit composition (6 identical 55-kD subunits),
chromatographic behavior, catalysis of synthetic N-terminal leucyl and
prolyl peptides, pH dependence, susceptibility to proteinase inhibitors,
and activation by manganese and magnesium.
MAPPING
By somatic cell hybridization, Shows et al. (1978) assigned the gene for
peptidase S to chromosome 4. Schmutz and Simpson (1983) measured
leukocyte PEPS in 3 patients with Wolf-Hirschhorn syndrome (4p-) and in
50 controls. They also compared PEPS in 5 control fibroblast lines and 8
fibroblast lines with chromosome 4 aberrations including partial
monosomies and partial trisomies. PEPS levels did not differ from
controls in any. This experience permitted exclusion mapping of PEPS to
4p11-4q13; combined with previously reported data, the assignment
becomes 4p11-4q12.
*FIELD* SA
Brown et al. (1978); Francke and Brown (1979); Lewis and Harris (1967)
*FIELD* RF
1. Brown, S.; Lalley, P. A.; Francke, U.; Minna, J. D.: Assignment
of the locus for peptidase S (PEPS) to chromosome 4 in man and confirmation
of peptidase D (PEPD) assignment to chromosome 19. Cytogenet. Cell
Genet. 22: 167-171, 1978.
2. Francke, U.; Brown, S.: Regional assignment of genes for phosphoglucomutase-2
and peptidase S to 4pter-4q21 in man. Cytogenet. Cell Genet. 22:
401-405, 1979.
3. Lewis, W. H.; Harris, H.: Human red cell peptidases. Nature 215:
351-355, 1967.
4. Matsushima, M.; Takahashi, T.; Ichinose, M.; Miki, K.; Kurokawa,
K.; Takahashi, K.: Structural and immunological evidence for the
identity of prolyl aminopeptidase with leucyl aminopeptidase. Biochem.
Biophys. Res. Commun. 178: 1459-1464, 1991.
5. Schmutz, S. M.; Simpson, N. E.: Suggested assignment of peptidase
S (PEPS) to 4p11-4q12 by exclusion using gene dosage, accounting for
variability in fibroblasts. Hum. Genet. 64: 134-138, 1983.
6. Shows, T. B.; Brown, J. A.; Eddy, R. L.; Byers, M. G.; Haley, L.
L.; Cooper, E. S.; Goggin, A. P.: Assignment of peptidase S (PEPS)
to chromosome 4 in man using somatic cell hybrids. Hum. Genet. 43:
119-125, 1978.
*FIELD* CN
Patricia A. Hartz - updated: 11/5/2004
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
mgross: 11/09/2004
mgross: 11/9/2004
terry: 11/5/2004
carol: 11/12/1993
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 10/18/1986
*RECORD*
*FIELD* NO
170250
*FIELD* TI
*170250 LEUCINE AMINOPEPTIDASE 3; LAP3
;;PEPTIDASE S; PEPS
*FIELD* TX
CLONING
Matsushima et al. (1991) presented evidence that prolyl aminopeptidases
read more(EC 3.4.11.5) purified from pig small intestine mucosa and human liver
and leucyl aminopeptidase (EC 3.4.11.1) purified from pig kidney were
identical. Both pig enzymes were indistinguishable in their molecular
mass (about 300 kD), subunit composition (6 identical 55-kD subunits),
chromatographic behavior, catalysis of synthetic N-terminal leucyl and
prolyl peptides, pH dependence, susceptibility to proteinase inhibitors,
and activation by manganese and magnesium.
MAPPING
By somatic cell hybridization, Shows et al. (1978) assigned the gene for
peptidase S to chromosome 4. Schmutz and Simpson (1983) measured
leukocyte PEPS in 3 patients with Wolf-Hirschhorn syndrome (4p-) and in
50 controls. They also compared PEPS in 5 control fibroblast lines and 8
fibroblast lines with chromosome 4 aberrations including partial
monosomies and partial trisomies. PEPS levels did not differ from
controls in any. This experience permitted exclusion mapping of PEPS to
4p11-4q13; combined with previously reported data, the assignment
becomes 4p11-4q12.
*FIELD* SA
Brown et al. (1978); Francke and Brown (1979); Lewis and Harris (1967)
*FIELD* RF
1. Brown, S.; Lalley, P. A.; Francke, U.; Minna, J. D.: Assignment
of the locus for peptidase S (PEPS) to chromosome 4 in man and confirmation
of peptidase D (PEPD) assignment to chromosome 19. Cytogenet. Cell
Genet. 22: 167-171, 1978.
2. Francke, U.; Brown, S.: Regional assignment of genes for phosphoglucomutase-2
and peptidase S to 4pter-4q21 in man. Cytogenet. Cell Genet. 22:
401-405, 1979.
3. Lewis, W. H.; Harris, H.: Human red cell peptidases. Nature 215:
351-355, 1967.
4. Matsushima, M.; Takahashi, T.; Ichinose, M.; Miki, K.; Kurokawa,
K.; Takahashi, K.: Structural and immunological evidence for the
identity of prolyl aminopeptidase with leucyl aminopeptidase. Biochem.
Biophys. Res. Commun. 178: 1459-1464, 1991.
5. Schmutz, S. M.; Simpson, N. E.: Suggested assignment of peptidase
S (PEPS) to 4p11-4q12 by exclusion using gene dosage, accounting for
variability in fibroblasts. Hum. Genet. 64: 134-138, 1983.
6. Shows, T. B.; Brown, J. A.; Eddy, R. L.; Byers, M. G.; Haley, L.
L.; Cooper, E. S.; Goggin, A. P.: Assignment of peptidase S (PEPS)
to chromosome 4 in man using somatic cell hybrids. Hum. Genet. 43:
119-125, 1978.
*FIELD* CN
Patricia A. Hartz - updated: 11/5/2004
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
mgross: 11/09/2004
mgross: 11/9/2004
terry: 11/5/2004
carol: 11/12/1993
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 10/18/1986