Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Peptidase M)

 MAP2_CANAL              Reviewed;         446 AA.
Q59LF9; A0A1D8PQC1;
03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 2.
07-NOV-2018, entry version 92.
RecName: Full=Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175};
Short=MAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
Short=MetAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03175};
AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_03175};
Name=MAP2 {ECO:0000255|HAMAP-Rule:MF_03175};
OrderedLocusNames=CAALFM_C604080WA; ORFNames=CaO19.1214, CaO19.8802;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
-!- FUNCTION: Cotranslationally 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). {ECO:0000255|HAMAP-
Rule:MF_03175}.
-!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
preferentially methionine, from peptides and arylamides.
{ECO:0000255|HAMAP-Rule:MF_03175}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
Note=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 Fe(2+)-
metalloproteases under physiological conditions, and the
catalytically relevant metal-binding site has been assigned to the
histidine-containing high-affinity site. {ECO:0000255|HAMAP-
Rule:MF_03175};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}.
-!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
aminopeptidase eukaryotic type 2 subfamily. {ECO:0000255|HAMAP-
Rule:MF_03175}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; CP017628; AOW30329.1; -; Genomic_DNA.
RefSeq; XP_710564.2; XM_705472.2.
ProteinModelPortal; Q59LF9; -.
SMR; Q59LF9; -.
PRIDE; Q59LF9; -.
EnsemblFungi; AOW30329; AOW30329; CAALFM_C604080WA.
GeneID; 3647837; -.
KEGG; cal:CAALFM_C604080WA; -.
CGD; CAL0000186537; orf19.1214.
InParanoid; Q59LF9; -.
KO; K01265; -.
OrthoDB; EOG092C3NQP; -.
PRO; PR:Q59LF9; -.
Proteomes; UP000000559; Chromosome 6.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
CDD; cd01088; MetAP2; 1.
Gene3D; 1.10.10.10; -; 1.
HAMAP; MF_03175; MetAP_2_euk; 1.
InterPro; IPR036005; Creatinase/aminopeptidase-like.
InterPro; IPR000994; Pept_M24.
InterPro; IPR001714; Pept_M24_MAP.
InterPro; IPR002468; Pept_M24A_MAP2.
InterPro; IPR018349; Pept_M24A_MAP2_BS.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00557; Peptidase_M24; 1.
PRINTS; PR00599; MAPEPTIDASE.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF55920; SSF55920; 1.
TIGRFAMs; TIGR00501; met_pdase_II; 1.
PROSITE; PS01202; MAP_2; 1.
3: Inferred from homology;
Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase;
Metal-binding; Protease; Reference proteome.
CHAIN 1 446 Methionine aminopeptidase 2.
/FTId=PRO_0000407646.
COMPBIAS 70 84 Lys-rich. {ECO:0000255|HAMAP-
Rule:MF_03175}.
METAL 217 217 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 228 228 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 228 228 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 299 299 Divalent metal cation 2; catalytic; via
tele nitrogen. {ECO:0000255|HAMAP-
Rule:MF_03175}.
METAL 332 332 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 427 427 Divalent metal cation 1.
{ECO:0000255|HAMAP-Rule:MF_03175}.
METAL 427 427 Divalent metal cation 2; catalytic.
{ECO:0000255|HAMAP-Rule:MF_03175}.
BINDING 197 197 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175}.
BINDING 307 307 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03175}.
SEQUENCE 446 AA; 50379 MW; 16950E829808285B CRC64;
MAGVTEGEDT KVIESKINEL NIDKPKLEDN NEAKGNGNGN ESGDDDDDDK EEDDDNEITE
PSTSTASGDE KKKKNKNKKK KKKKIVSIDS SYPEGIFPEG QWMEYPLEDI NSYRTTSEEK
RYLDRQQNNK WQDFRKGAEI HRRVRHKAQS SIRPGMTMIE IANLIEDSVR NYSGNDHTLK
AGIGFPTGLS LNHVAAHYTP NTGDKLILKK DDIMKVDIGV HVNGRICDSA FTMTFNEDGK
YDTIMQAVKE ATYTGIKESG IDVRLNDIGA AIQEVMESYE MEENGKTYPI KCIKNLNGHN
IDDFVIHSGK SVPIIANGDM TKMEEGETFA IETFGSTGNG YVLPEGECSH YAMNKGVEHL
KPPSERSKQL LETIKQNFGT LPWCRRYLER TGEEKYLFAL NQLVRHGIVE EYPPIVDKRG
SYTAQFEHTI LLHPHKKEVV TKGDDY


Related products :

Catalog number Product name Quantity
E0536b ELISA kit Bos taurus,Bovine,Cytosol aminopeptidase,LAP3,LAP-3,Leucine aminopeptidase 3,Leucyl aminopeptidase,Peptidase S,Proline aminopeptidase,Prolyl aminopeptidase 96T
E0536b ELISA Bos taurus,Bovine,Cytosol aminopeptidase,LAP3,LAP-3,Leucine aminopeptidase 3,Leucyl aminopeptidase,Peptidase S,Proline aminopeptidase,Prolyl aminopeptidase 96T
U0536b CLIA Bos taurus,Bovine,Cytosol aminopeptidase,LAP3,LAP-3,Leucine aminopeptidase 3,Leucyl aminopeptidase,Peptidase S,Proline aminopeptidase,Prolyl aminopeptidase 96T
E0536h ELISA Cytosol aminopeptidase,Homo sapiens,Human,LAP3,LAP-3,LAPEP,Leucine aminopeptidase 3,Leucyl aminopeptidase,PEPS,Peptidase S,Proline aminopeptidase,Prolyl aminopeptidase 96T
U0536h CLIA Cytosol aminopeptidase,Homo sapiens,Human,LAP3,LAP-3,LAPEP,Leucine aminopeptidase 3,Leucyl aminopeptidase,PEPS,Peptidase S,Proline aminopeptidase,Prolyl aminopeptidase 96T
E0536h ELISA kit Cytosol aminopeptidase,Homo sapiens,Human,LAP3,LAP-3,LAPEP,Leucine aminopeptidase 3,Leucyl aminopeptidase,PEPS,Peptidase S,Proline aminopeptidase,Prolyl aminopeptidase 96T
18-271-81043 MAP2 - Chicken Anti MAP2; EC 3.4.11.18; MetAP 2; Peptidase M 2 Polyclonal 0.1 mg
18-272-196630 Methionine Aminopeptidase 2 - Rabbit polyclonal to Methionine Aminopeptidase 2; Polyclonal 0.05 mg
EIAAB30744 5-oxoprolyl-peptidase,Homo sapiens,Human,PAP-I,PGPEP1,PGPI,PGP-I,Pyroglutamyl aminopeptidase I,Pyroglutamyl-peptidase 1,Pyroglutamyl-peptidase I,Pyrrolidone-carboxylate peptidase
EIAAB30743 5-oxoprolyl-peptidase,Mouse,Mus musculus,PAP-I,Pgpep1,Pgpi,PGP-I,Pyroglutamyl aminopeptidase I,Pyroglutamyl-peptidase 1,Pyroglutamyl-peptidase I,Pyrrolidone-carboxylate peptidase
EIAAB30745 5-oxoprolyl-peptidase,PAP-I,Pgpep1,PGP-I,Pyroglutamyl aminopeptidase I,Pyroglutamyl-peptidase 1,Pyroglutamyl-peptidase I,Pyrrolidone-carboxylate peptidase,Rat,Rattus norvegicus
EIAAB11849 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,DPP6,DPPX,Homo sapiens,Hum
EIAAB11848 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,Dpp6,DPPX,Rat,Rattus norve
EIAAB11851 Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,Dpp6,Dpp-6,DPPX,Mouse,Mus
EIAAB11850 Bos taurus,Bovine,Dipeptidyl aminopeptidase-like protein 6,Dipeptidyl aminopeptidase-related protein,Dipeptidyl peptidase 6,Dipeptidyl peptidase IV-like protein,Dipeptidyl peptidase VI,DPP VI,DPP6,DPP
EIAAB46562 Aminoacylproline aminopeptidase,App,Cytosolic aminopeptidase P,Rat,Rattus norvegicus,sAmp,Soluble aminopeptidase P,Xaa-Pro aminopeptidase 1,Xpnpep1,X-Pro aminopeptidase 1,X-prolyl aminopeptidase 1, so
EIAAB11842 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,DPP2,DPP7,Homo sapiens,Human,QPP,Quiescent cell proline dipeptidase
EIAAB11844 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,Dpp2,Dpp7,Mouse,Mus musculus,Qpp,Quiescent cell proline dipeptidase
EIAAB11843 Dipeptidyl aminopeptidase II,Dipeptidyl peptidase 2,Dipeptidyl peptidase 7,Dipeptidyl peptidase II,DPP II,Dpp2,Dpp7,Quiescent cell proline dipeptidase,Rat,Rattus norvegicus
E0536m ELISA kit Cytosol aminopeptidase,Lap3,LAP-3,Lapep,Leucine aminopeptidase 3,Leucyl aminopeptidase,Mouse,Mus musculus,Proline aminopeptidase,Prolyl aminopeptidase 96T
E0536m ELISA Cytosol aminopeptidase,Lap3,LAP-3,Lapep,Leucine aminopeptidase 3,Leucyl aminopeptidase,Mouse,Mus musculus,Proline aminopeptidase,Prolyl aminopeptidase 96T
U0536m CLIA Cytosol aminopeptidase,Lap3,LAP-3,Lapep,Leucine aminopeptidase 3,Leucyl aminopeptidase,Mouse,Mus musculus,Proline aminopeptidase,Prolyl aminopeptidase 96T
U0536r CLIA Cytosol aminopeptidase,Lap3,LAP-3,Leucine aminopeptidase 3,Leucyl aminopeptidase,Proline aminopeptidase,Prolyl aminopeptidase,Rat,Rattus norvegicus 96T
E0536r ELISA Cytosol aminopeptidase,Lap3,LAP-3,Leucine aminopeptidase 3,Leucyl aminopeptidase,Proline aminopeptidase,Prolyl aminopeptidase,Rat,Rattus norvegicus 96T
E0536r ELISA kit Cytosol aminopeptidase,Lap3,LAP-3,Leucine aminopeptidase 3,Leucyl aminopeptidase,Proline aminopeptidase,Prolyl aminopeptidase,Rat,Rattus norvegicus 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur