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Q8N6M6 (AMPO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase O

Short name=AP-O
EC=3.4.11.-
Gene names
Name:AOPEP
Synonyms:C9orf3, ONPEP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length819 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart. Ref.1

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Strongly inhibited by ophenanthroline, a metalloprotease inhibitor. Inhibited by arphamenine A, a potent inhibitor of aminopeptidases. Not affected by AEBSF and E-64, which are common inhibitors of serine- and cysteine-proteases, respectively. Ref.1

Subcellular location

Cytoplasm Potential.

Tissue specificity

Predominantly expressed in pancreas, placenta, liver, testis and heart. Expressed at lower level in brain, lung and kidney. Ref.1

Sequence similarities

Belongs to the peptidase M1 family.

Biophysicochemical properties

Kinetic parameters:

KM=6 µM for Arg-AMC Ref.1

Sequence caution

The sequence AAH20194.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB55210.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processleukotriene biosynthetic process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionaminopeptidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

metallopeptidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N6M6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N6M6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     455-553: Missing.
Isoform 3 (identifier: Q8N6M6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     555-565: PSKDKTGHTSD → FPHVGGCSGSFS
     566-819: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8N6M6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     455-553: Missing.
     774-784: AMGVYLYGELM → VGVIFQQMGIL
     785-819: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 819819Aminopeptidase O
PRO_0000095091

Sites

Active site4801Proton acceptor By similarity
Metal binding4791Zinc; catalytic By similarity
Metal binding4831Zinc; catalytic By similarity
Metal binding5021Zinc; catalytic By similarity
Site5861Transition state stabilizer By similarity

Natural variations

Alternative sequence455 – 55399Missing in isoform 2 and isoform 4.
VSP_013161
Alternative sequence555 – 56511PSKDKTGHTSD → FPHVGGCSGSFS in isoform 3.
VSP_013162
Alternative sequence566 – 819254Missing in isoform 3.
VSP_013163
Alternative sequence774 – 78411AMGVYLYGELM → VGVIFQQMGIL in isoform 4.
VSP_013164
Alternative sequence785 – 81935Missing in isoform 4.
VSP_013165
Natural variant1791V → A.
Corresponds to variant rs16911679 [ dbSNP | Ensembl ].
VAR_021511
Natural variant1791V → I.
Corresponds to variant rs16911679 [ dbSNP | Ensembl ].
VAR_057053
Natural variant2551R → Q.
Corresponds to variant rs16911681 [ dbSNP | Ensembl ].
VAR_057054
Natural variant3861R → C.
Corresponds to variant rs34557833 [ dbSNP | Ensembl ].
VAR_057055

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: 9EB4F19295B92674

FASTA81993,572
        10         20         30         40         50         60 
MDIQLDPARD DLPLMANTSH ILVKHYVLDL DVDFESQVIE GTIVLFLEDG NRFKKQNSSI 

        70         80         90        100        110        120 
EEACQSESNK ACKFGMPEPC HIPVTNARTF SSEMEYNDFA ICSKGEKDTS DKDGNHDNQE 

       130        140        150        160        170        180 
HASGISSSKY CCDTGNHGSE DFLLVLDCCD LSVLKVEEVD VAAVPGLEKF TRSPELTVVS 

       190        200        210        220        230        240 
EEFRNQIVRE LVTLPANRWR EQLDYYARCS QAPGCGELLF DTDTWSLQIR KTGAQTATDF 

       250        260        270        280        290        300 
PHAIRIWYKT KPEGRSVTWT SDQSGRPCVY TVGSPINNRA LFPCQEPPVA MSTWQATVRA 

       310        320        330        340        350        360 
AASFVVLMSG ENSAKPTQLW EECSSWYYYV TMPMPASTFT IAVGCWTEMK METWSSNDLA 

       370        380        390        400        410        420 
TERPFSPSEA NFRHVGVCSH MEYPCRFQNA SATTQEIIPH RVFAPVCLTG ACQETLLRLI 

       430        440        450        460        470        480 
PPCLSAAHSV LGAHPFSRLD VLIVPANFPS LGMASPHIMF LSQSILTGGN HLCGTRLCHE 

       490        500        510        520        530        540 
IAHAWFGLAI GARDWTEEWL SEGFATHLED VFWATAQQLA PYEAREQQEL RACLRWRRLQ 

       550        560        570        580        590        600 
DEMQCSPEEM QVLRPSKDKT GHTSDSGASV IKHGLNPEKI FMQVHYLKGY FLLRFLAKRL 

       610        620        630        640        650        660 
GDETYFSFLR KFVHTFHGQL ILSQDFLQML LENIPEEKRL ELSVENIYQD WLESSGIPKP 

       670        680        690        700        710        720 
LQRERRAGAE CGLARQVRAE VTKWIGVNRR PRKRKRREKE EVFEKLLPDQ LVLLLEHLLE 

       730        740        750        760        770        780 
QKTLSPRTLQ SLQRTYHLQD QDAEVRHRWC ELIVKHKFTK AYKSVERFLQ EDQAMGVYLY 

       790        800        810 
GELMVSEDAR QQQLARRCFE RTKEQMDRSS AQVVAEMLF 

« Hide

Isoform 2 [UniParc].

Checksum: 12A6A6169C56A627
Show »

FASTA72082,105
Isoform 3 [UniParc].

Checksum: 3E9D4D00E45C2A46
Show »

FASTA56663,363
Isoform 4 [UniParc].

Checksum: 57667BB61D258FD2
Show »

FASTA68577,937

References

« Hide 'large scale' references
[1]"Identification of human aminopeptidase O, a novel metalloprotease with structural similarity to aminopeptidase B and leukotriene A4 hydrolase."
Diaz-Perales A., Quesada V., Sanchez L.M., Ugalde A.P., Suarez M.F., Fueyo A., Lopez-Otin C.
J. Biol. Chem. 280:14310-14317(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-819 (ISOFORM 4).
Tissue: Teratocarcinoma and Testis.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-819 (ISOFORM 1).
Tissue: Lung and Muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ560639 mRNA. Translation: CAD90259.1.
AK027581 mRNA. Translation: BAB55210.1. Different initiation.
AK057450 mRNA. Translation: BAB71491.1.
AL157936, AL353768, AL354893 Genomic DNA. Translation: CAI13040.1.
AL353768, AL157936, AL354893 Genomic DNA. Translation: CAI41125.1.
AL354893, AL157936, AL353768 Genomic DNA. Translation: CAI41325.1.
AL157936, AL353768, AL354893 Genomic DNA. Translation: CAI13039.1.
AL353768, AL157936, AL354893 Genomic DNA. Translation: CAI41126.1.
AL354893, AL157936, AL353768 Genomic DNA. Translation: CAI41326.1.
AL157936, AL353768 Genomic DNA. Translation: CAI13037.1.
AL353768, AL157936 Genomic DNA. Translation: CAI41124.1.
AL157936, AL353768, AL354893 Genomic DNA. Translation: CAI13041.1.
AL353768, AL157936, AL354893 Genomic DNA. Translation: CAI41127.1.
AL354893, AL157936, AL353768 Genomic DNA. Translation: CAI41327.1.
AL157936 Genomic DNA. Translation: CAI13038.1.
BC020194 mRNA. Translation: AAH20194.1. Different initiation.
BC029616 mRNA. Translation: AAH29616.1.
CCDSCCDS55327.1. [Q8N6M6-3]
CCDS55328.1. [Q8N6M6-1]
CCDS6713.1. [Q8N6M6-2]
RefSeqNP_001180258.1. NM_001193329.1. [Q8N6M6-1]
NP_001180260.1. NM_001193331.2. [Q8N6M6-3]
NP_116212.3. NM_032823.5. [Q8N6M6-2]
XP_006717369.1. XM_006717306.1. [Q8N6M6-1]
UniGeneHs.434253.

3D structure databases

ProteinModelPortalQ8N6M6.
SMRQ8N6M6. Positions 244-818.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124346. 1 interaction.
STRING9606.ENSP00000297979.

Protein family/group databases

MEROPSM01.028.

PTM databases

PhosphoSiteQ8N6M6.

Polymorphism databases

DMDM61211648.

Proteomic databases

PaxDbQ8N6M6.
PRIDEQ8N6M6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000277198; ENSP00000277198; ENSG00000148120. [Q8N6M6-3]
ENST00000297979; ENSP00000297979; ENSG00000148120. [Q8N6M6-2]
ENST00000375315; ENSP00000364464; ENSG00000148120. [Q8N6M6-1]
GeneID84909.
KEGGhsa:84909.
UCSCuc004aux.2. human. [Q8N6M6-3]
uc004auy.3. human. [Q8N6M6-2]
uc004auz.1. human. [Q8N6M6-4]
uc004ava.3. human. [Q8N6M6-1]

Organism-specific databases

CTD84909.
GeneCardsGC09P097488.
HGNCHGNC:1361. C9orf3.
HPAHPA004633.
neXtProtNX_Q8N6M6.
PharmGKBPA25978.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG122535.
HOVERGENHBG050496.
InParanoidQ8N6M6.
KOK09606.
OMAAIRIWYK.
OrthoDBEOG741Z1Q.
PhylomeDBQ8N6M6.
TreeFamTF332004.

Enzyme and pathway databases

SABIO-RKQ8N6M6.

Gene expression databases

ArrayExpressQ8N6M6.
BgeeQ8N6M6.
CleanExHS_C9orf3.
GenevestigatorQ8N6M6.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

ChiTaRSC9orf3. human.
GenomeRNAi84909.
NextBio75288.
PROQ8N6M6.

Entry information

Entry nameAMPO_HUMAN
AccessionPrimary (citable) accession number: Q8N6M6
Secondary accession number(s): Q5T9B1 expand/collapse secondary AC list , Q5T9B3, Q5T9B4, Q8WUL6, Q96M23, Q96SS1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM