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Q9CPW9

- MAP12_MOUSE

UniProt

Q9CPW9 - MAP12_MOUSE

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Protein

Methionine aminopeptidase 1D, mitochondrial

Gene

Metap1d

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei161 – 1611SubstrateUniRule annotation
Metal bindingi178 – 1781Divalent metal cation 1UniRule annotation
Metal bindingi189 – 1891Divalent metal cation 1UniRule annotation
Metal bindingi189 – 1891Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi252 – 2521Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Metal bindingi284 – 2841Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi315 – 3151Divalent metal cation 1UniRule annotation
Metal bindingi315 – 3151Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.028.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1D, mitochondrialUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1DUniRule annotation
Short name:
MetAP 1DUniRule annotation
Alternative name(s):
Methionyl aminopeptidase type 1D, mitochondrial
Peptidase M 1DUniRule annotation
Gene namesi
Name:Metap1d
Synonyms:Map1d, Metapl1, Mnpepl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1913809. Metap1d.

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionUniRule annotationAdd
BLAST
Chaini20 – 335316Methionine aminopeptidase 1D, mitochondrialPRO_0000314127Add
BLAST

Proteomic databases

MaxQBiQ9CPW9.
PaxDbiQ9CPW9.
PRIDEiQ9CPW9.

PTM databases

PhosphoSiteiQ9CPW9.

Expressioni

Gene expression databases

BgeeiQ9CPW9.
CleanExiMM_METAPL1.
GenevestigatoriQ9CPW9.

Interactioni

Protein-protein interaction databases

IntActiQ9CPW9. 1 interaction.
MINTiMINT-4124719.

Structurei

3D structure databases

ProteinModelPortaliQ9CPW9.
SMRiQ9CPW9. Positions 60-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0024.
GeneTreeiENSGT00390000002284.
HOGENOMiHOG000030427.
HOVERGENiHBG067178.
InParanoidiQ9CPW9.
KOiK01265.
OMAiLNHIYLH.
OrthoDBiEOG786H38.
PhylomeDBiQ9CPW9.
TreeFamiTF325318.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9CPW9-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAPIGVPLL VRGGCQRILS SPLNHIYLHK RSGSQQRRHF FFWRQRDISH
60 70 80 90 100
SVVSPAAVSP AHPVPKRIKK PDYVTTGIVP DWGDSIEVKD EDQIQGLREA
110 120 130 140 150
CRLARHVLLL AGKSLKVDMT TEEIDALVHW EIIRHDAYPS PLGYGRFPKS
160 170 180 190 200
VCTSVNNVLC HGIPDSRPLQ DGDIINIDVT VYYNGYHGDT SETFLVGNVD
210 220 230 240 250
ESGKKLVEVA RRCRDEAIAA CRAGAPFSVI GNTISRITHQ NGLQVCPHFV
260 270 280 290 300
GHGIGSYFHG HPEIWHHAND NDLPMEEGMA FTIEPIITEG SPEFKVLEDA
310 320 330
WTVVSLDNQR SAQFEHTVLI TPRGVEILTK LPQEA
Length:335
Mass (Da):37,262
Last modified:June 1, 2001 - v1
Checksum:iEF270DDD1826E802
GO
Isoform 2 (identifier: Q9CPW9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Show »
Length:217
Mass (Da):24,058
Checksum:i0EE940FF76A74279
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321N → T in CAC88860. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 118118Missing in isoform 2. 2 PublicationsVSP_030210Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ414378 mRNA. Translation: CAC88860.1.
AK005241 mRNA. Translation: BAB23899.1.
AK010067 mRNA. Translation: BAB26680.1.
AL928931 Genomic DNA. Translation: CAM23833.1.
BC051534 mRNA. Translation: AAH51534.1.
CCDSiCCDS16115.1. [Q9CPW9-1]
RefSeqiNP_079909.1. NM_025633.3. [Q9CPW9-1]
XP_006500073.1. XM_006500010.1. [Q9CPW9-2]
UniGeneiMm.152796.
Mm.443051.

Genome annotation databases

EnsembliENSMUST00000037210; ENSMUSP00000048190; ENSMUSG00000041921. [Q9CPW9-1]
GeneIDi66559.
KEGGimmu:66559.
UCSCiuc008kas.1. mouse. [Q9CPW9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ414378 mRNA. Translation: CAC88860.1 .
AK005241 mRNA. Translation: BAB23899.1 .
AK010067 mRNA. Translation: BAB26680.1 .
AL928931 Genomic DNA. Translation: CAM23833.1 .
BC051534 mRNA. Translation: AAH51534.1 .
CCDSi CCDS16115.1. [Q9CPW9-1 ]
RefSeqi NP_079909.1. NM_025633.3. [Q9CPW9-1 ]
XP_006500073.1. XM_006500010.1. [Q9CPW9-2 ]
UniGenei Mm.152796.
Mm.443051.

3D structure databases

ProteinModelPortali Q9CPW9.
SMRi Q9CPW9. Positions 60-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9CPW9. 1 interaction.
MINTi MINT-4124719.

Protein family/group databases

MEROPSi M24.028.

PTM databases

PhosphoSitei Q9CPW9.

Proteomic databases

MaxQBi Q9CPW9.
PaxDbi Q9CPW9.
PRIDEi Q9CPW9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000037210 ; ENSMUSP00000048190 ; ENSMUSG00000041921 . [Q9CPW9-1 ]
GeneIDi 66559.
KEGGi mmu:66559.
UCSCi uc008kas.1. mouse. [Q9CPW9-1 ]

Organism-specific databases

CTDi 254042.
MGIi MGI:1913809. Metap1d.

Phylogenomic databases

eggNOGi COG0024.
GeneTreei ENSGT00390000002284.
HOGENOMi HOG000030427.
HOVERGENi HBG067178.
InParanoidi Q9CPW9.
KOi K01265.
OMAi LNHIYLH.
OrthoDBi EOG786H38.
PhylomeDBi Q9CPW9.
TreeFami TF325318.

Miscellaneous databases

NextBioi 322010.
PROi Q9CPW9.
SOURCEi Search...

Gene expression databases

Bgeei Q9CPW9.
CleanExi MM_METAPL1.
Genevestigatori Q9CPW9.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing and expression of mouse MNPEPL peptidase, a novel member of peptidase family M24."
    Dando P.M., Fortunato M., Rawlings N.D., Barrett A.J.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Spleen.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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).
    Tissue: Mammary gland.

Entry informationi

Entry nameiMAP12_MOUSE
AccessioniPrimary (citable) accession number: Q9CPW9
Secondary accession number(s): Q80WB3, Q91YD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3