MAP2_HUMAN
ID MAP2_HUMAN Reviewed; 478 AA.
AC P50579; B2RDI8; B4DUX5; G3XA91; Q8NB11;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=MAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=MetAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03175};
DE AltName: Full=Initiation factor 2-associated 67 kDa glycoprotein {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=p67 {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=p67eIF2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_03175};
GN Name=METAP2 {ECO:0000255|HAMAP-Rule:MF_03175}; Synonyms=MNPEP, P67EIF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7644482; DOI=10.1073/pnas.92.17.7714;
RA Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E.,
RA Matthews B.W., Bradshaw R.A.;
RT "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent
RT enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7714-7718(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=7873610; DOI=10.1016/0167-4781(94)00227-t;
RA Li X., Chang Y.;
RT "Molecular cloning of a human complementary DNA encoding an initiation
RT factor 2-associated protein (p67).";
RL Biochim. Biophys. Acta 1260:333-336(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Heart, Placenta, and Small intestine;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION IN EIF2S1 PROTECTION, AND GLYCOSYLATION.
RX PubMed=2511207; DOI=10.1016/s0021-9258(19)47108-1;
RA Datta B., Ray M.K., Chakrabarti D., Wylie D.E., Gupta N.K.;
RT "Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-
RT associated 67-kDa polypeptide (p67) and its possible role in the inhibition
RT of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 alpha-subunit.";
RL J. Biol. Chem. 264:20620-20624(1989).
RN [8]
RP COFACTOR.
RX PubMed=12718546; DOI=10.1021/bi020670c;
RA Wang J., Sheppard G.S., Lou P., Kawai M., Park C., Egan D.A., Schneider A.,
RA Bouska J., Lesniewski R., Henkin J.;
RT "Physiologically relevant metal cofactor for methionine aminopeptidase-2 is
RT manganese.";
RL Biochemistry 42:5035-5042(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-60; SER-63 AND
RP SER-74, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20521764; DOI=10.1021/bi1005464;
RA Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D.;
RT "Protein N-terminal processing: substrate specificity of Escherichia coli
RT and human methionine aminopeptidases.";
RL Biochemistry 49:5588-5599(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-74, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=21537465; DOI=10.4331/wjbc.v1.i10.313;
RA Wu S.;
RT "Localization and function of a eukaryotic-initiation-factor-2-associated
RT 67-kDa glycoprotein.";
RL World J. Biol. Chem. 1:313-320(2010).
RN [14]
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., Buerckstuemmer T.,
RA 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-63 AND SER-74, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FUMAGILLIN, AND
RP COFACTOR.
RX PubMed=9812898; DOI=10.1126/science.282.5392.1324;
RA Liu S., Widom J., Kemp C.W., Crews C.M., Clardy J.;
RT "Structure of human methionine aminopeptidase-2 complexed with
RT fumagillin.";
RL Science 282:1324-1327(1998).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COBALT IONS AND
RP BENGAMIDE, AND FUNCTION.
RX PubMed=14534293; DOI=10.1074/jbc.m309039200;
RA Towbin H., Bair K.W., DeCaprio J.A., Eck M.J., Kim S., Kinder F.R.,
RA Morollo A., Mueller D.R., Schindler P., Song H.K., van Oostrum J.,
RA Versace R.W., Voshol H., Wood J., Zabludoff S., Phillips P.E.;
RT "Proteomics-based target identification: bengamides as a new class of
RT methionine aminopeptidase inhibitors.";
RL J. Biol. Chem. 278:52964-52971(2003).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH INHIBITOR
RP A-357300.
RX PubMed=15012983; DOI=10.1016/j.bmcl.2003.12.031;
RA Sheppard G.S., Wang J., Kawai M., BaMaung N.Y., Craig R.A., Erickson S.A.,
RA Lynch L., Patel J., Yang F., Searle X.B., Lou P., Park C., Kim K.H.,
RA Henkin J., Lesniewski R.;
RT "3-amino-2-hydroxyamides and related compounds as inhibitors of methionine
RT aminopeptidase-2.";
RL Bioorg. Med. Chem. Lett. 14:865-868(2004).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH
RP 4-ARYL-1,2,3-TRIAZOLE AND COBALT IONS.
RX PubMed=16134930; DOI=10.1021/jm050408c;
RA Kallander L.S., Lu Q., Chen W., Tomaszek T., Yang G., Tew D., Meek T.D.,
RA Hofmann G.A., Schulz-Pritchard C.K., Smith W.W., Janson C.A., Ryan M.D.,
RA Zhang G.-F., Johanson K.O., Kirkpatrick R.B., Ho T.F., Fisher P.W.,
RA Mattern M.R., Johnson R.K., Hansbury M.J., Winkler J.D., Ward K.W.,
RA Veber D.F., Thompson S.K.;
RT "4-aryl-1,2,3-triazole: a novel template for a reversible methionine
RT aminopeptidase 2 inhibitor, optimized to inhibit angiogenesis in vivo.";
RL J. Med. Chem. 48:5644-5647(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH ZINC IONS AND
RP METHIONINE, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=16540317; DOI=10.1016/j.bmcl.2006.02.047;
RA Nonato M.C., Widom J., Clardy J.;
RT "Human methionine aminopeptidase type 2 in complex with L- and D-
RT methionine.";
RL Bioorg. Med. Chem. Lett. 16:2580-2583(2006).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 110-478 IN COMPLEX WITH MANGANESE
RP AND INHIBITOR.
RX PubMed=17350258; DOI=10.1016/j.bmcl.2007.02.062;
RA Wang G.T., Mantei R.A., Kawai M., Tedrow J.S., Barnes D.M., Wang J.,
RA Zhang Q., Lou P., Garcia L.A., Bouska J., Yates M., Park C., Judge R.A.,
RA Lesniewski R., Sheppard G.S., Bell R.L.;
RT "Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors
RT containing sulfonamides of 5,6-disubstituted anthranilic acids.";
RL Bioorg. Med. Chem. Lett. 17:2817-2822(2007).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 110-478 IN COMPLEX WITH COBALT
RP IONS AND INHIBITOR, COFACTOR, AND FUNCTION.
RX PubMed=17636946; DOI=10.1021/jm061182w;
RA Marino J.P. Jr., Fisher P.W., Hofmann G.A., Kirkpatrick R.B., Janson C.A.,
RA Johnson R.K., Ma C., Mattern M., Meek T.D., Ryan M.D., Schulz C.,
RA Smith W.W., Tew D.G., Tomazek T.A. Jr., Veber D.F., Xiong W.C.,
RA Yamamoto Y., Yamashita K., Yang G., Thompson S.K.;
RT "Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-
RT triazole pharmacophore.";
RL J. Med. Chem. 50:3777-3785(2007).
CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC nascent proteins. The N-terminal methionine is often cleaved when the
CC second residue in the primary sequence is small and uncharged (Met-
CC Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human
CC METAP2 toward Met-Val peptides is consistently two orders of magnitude
CC higher than that of METAP1, suggesting that it is responsible for
CC processing proteins containing N-terminal Met-Val and Met-Thr sequences
CC in vivo.
CC -!- FUNCTION: Protects eukaryotic initiation factor EIF2S1 from
CC translation-inhibiting phosphorylation by inhibitory kinases such as
CC EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of
CC protein synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175,
CC ECO:0000269|PubMed:20521764};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175,
CC ECO:0000269|PubMed:12718546, ECO:0000269|PubMed:17636946,
CC ECO:0000269|PubMed:9812898};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175,
CC ECO:0000269|PubMed:12718546, ECO:0000269|PubMed:17636946,
CC ECO:0000269|PubMed:9812898};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175,
CC ECO:0000269|PubMed:12718546, ECO:0000269|PubMed:17636946,
CC ECO:0000269|PubMed:9812898};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175,
CC ECO:0000269|PubMed:12718546, ECO:0000269|PubMed:17636946,
CC ECO:0000269|PubMed:9812898};
CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC and a low affinity metal-binding site. The true nature of the
CC physiological cofactor is under debate. The enzyme is active with
CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC Also manganese has been proposed to be the physiological cofactor for
CC human METAP2. {ECO:0000255|HAMAP-Rule:MF_03175,
CC ECO:0000269|PubMed:12718546, ECO:0000269|PubMed:17636946,
CC ECO:0000269|PubMed:9812898};
CC -!- SUBUNIT: Interacts strongly with the eIF-2 gamma-subunit EIF2S3 (By
CC similarity). Binds EIF2S1 at low magnesium concentrations.
CC {ECO:0000250, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:15012983,
CC ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:17350258,
CC ECO:0000269|PubMed:17636946, ECO:0000269|PubMed:9812898}.
CC -!- INTERACTION:
CC P50579; P21917: DRD4; NbExp=3; IntAct=EBI-2214155, EBI-8592297;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175,
CC ECO:0000269|PubMed:21537465}. Note=About 30% of expressed METAP2
CC associates with polysomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P50579-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50579-2; Sequence=VSP_055467, VSP_055468;
CC Name=3;
CC IsoId=P50579-3; Sequence=VSP_057353;
CC -!- PTM: Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc)
CC residues. O-glycosylation is required for EIF2S1 binding.
CC {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:2511207}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase eukaryotic type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03175}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/METAP2ID46053ch12q22.html";
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DR EMBL; U29607; AAA82930.1; -; mRNA.
DR EMBL; U13261; AAC63402.1; -; mRNA.
DR EMBL; AK091730; BAC03733.1; -; mRNA.
DR EMBL; AK300836; BAG62487.1; -; mRNA.
DR EMBL; AK315559; BAG37935.1; -; mRNA.
DR EMBL; AC018475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97537.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97538.1; -; Genomic_DNA.
DR EMBL; BC013782; AAH13782.1; -; mRNA.
DR CCDS; CCDS81723.1; -. [P50579-3]
DR CCDS; CCDS81725.1; -. [P50579-2]
DR CCDS; CCDS9052.1; -. [P50579-1]
DR PIR; S52112; DPHUM2.
DR RefSeq; NP_001304111.1; NM_001317182.1. [P50579-3]
DR RefSeq; NP_001304112.1; NM_001317183.1. [P50579-2]
DR RefSeq; NP_001317175.1; NM_001330246.1.
DR RefSeq; NP_006829.1; NM_006838.3. [P50579-1]
DR PDB; 1B59; X-ray; 1.80 A; A=109-478.
DR PDB; 1B6A; X-ray; 1.60 A; A=1-478.
DR PDB; 1BN5; X-ray; 1.80 A; A=1-478.
DR PDB; 1BOA; X-ray; 1.80 A; A=1-478.
DR PDB; 1KQ0; X-ray; 2.00 A; A=1-478.
DR PDB; 1KQ9; X-ray; 1.90 A; A=1-478.
DR PDB; 1QZY; X-ray; 1.60 A; A=1-478.
DR PDB; 1R58; X-ray; 1.90 A; A=110-478.
DR PDB; 1R5G; X-ray; 2.00 A; A=110-478.
DR PDB; 1R5H; X-ray; 2.40 A; A=110-478.
DR PDB; 1YW7; X-ray; 1.85 A; A=110-478.
DR PDB; 1YW8; X-ray; 2.65 A; A=110-478.
DR PDB; 1YW9; X-ray; 1.64 A; A=110-478.
DR PDB; 2ADU; X-ray; 1.90 A; A=110-478.
DR PDB; 2EA2; X-ray; 2.50 A; A=110-478.
DR PDB; 2EA4; X-ray; 2.35 A; A=110-478.
DR PDB; 2GA2; X-ray; 1.95 A; A=110-478.
DR PDB; 2OAZ; X-ray; 1.90 A; A=110-478.
DR PDB; 5CLS; X-ray; 1.75 A; A=108-478.
DR PDB; 5D6E; X-ray; 1.49 A; A=108-478.
DR PDB; 5D6F; X-ray; 1.55 A; A=108-478.
DR PDB; 5JFR; X-ray; 1.60 A; A=110-478.
DR PDB; 5JHU; X-ray; 1.80 A; A=110-478.
DR PDB; 5JI6; X-ray; 2.15 A; A=110-478.
DR PDB; 5LYW; X-ray; 1.69 A; A=108-478.
DR PDB; 5LYX; X-ray; 1.90 A; A=108-478.
DR PDB; 6QED; X-ray; 1.80 A; A=108-478.
DR PDB; 6QEF; X-ray; 1.79 A; A=108-478.
DR PDB; 6QEG; X-ray; 2.08 A; A=108-478.
DR PDB; 6QEH; X-ray; 2.17 A; A=108-478.
DR PDB; 6QEI; X-ray; 1.80 A; A=108-478.
DR PDB; 6QEJ; X-ray; 1.62 A; A=108-478.
DR PDB; 7A12; X-ray; 2.00 A; A=108-478.
DR PDB; 7A13; X-ray; 2.04 A; A=108-478.
DR PDB; 7A14; X-ray; 2.14 A; A=108-478.
DR PDB; 7A15; X-ray; 2.15 A; A=108-478.
DR PDB; 7A16; X-ray; 1.90 A; A=108-478.
DR PDBsum; 1B59; -.
DR PDBsum; 1B6A; -.
DR PDBsum; 1BN5; -.
DR PDBsum; 1BOA; -.
DR PDBsum; 1KQ0; -.
DR PDBsum; 1KQ9; -.
DR PDBsum; 1QZY; -.
DR PDBsum; 1R58; -.
DR PDBsum; 1R5G; -.
DR PDBsum; 1R5H; -.
DR PDBsum; 1YW7; -.
DR PDBsum; 1YW8; -.
DR PDBsum; 1YW9; -.
DR PDBsum; 2ADU; -.
DR PDBsum; 2EA2; -.
DR PDBsum; 2EA4; -.
DR PDBsum; 2GA2; -.
DR PDBsum; 2OAZ; -.
DR PDBsum; 5CLS; -.
DR PDBsum; 5D6E; -.
DR PDBsum; 5D6F; -.
DR PDBsum; 5JFR; -.
DR PDBsum; 5JHU; -.
DR PDBsum; 5JI6; -.
DR PDBsum; 5LYW; -.
DR PDBsum; 5LYX; -.
DR PDBsum; 6QED; -.
DR PDBsum; 6QEF; -.
DR PDBsum; 6QEG; -.
DR PDBsum; 6QEH; -.
DR PDBsum; 6QEI; -.
DR PDBsum; 6QEJ; -.
DR PDBsum; 7A12; -.
DR PDBsum; 7A13; -.
DR PDBsum; 7A14; -.
DR PDBsum; 7A15; -.
DR PDBsum; 7A16; -.
DR AlphaFoldDB; P50579; -.
DR SMR; P50579; -.
DR BioGRID; 116184; 114.
DR IntAct; P50579; 35.
DR MINT; P50579; -.
DR STRING; 9606.ENSP00000325312; -.
DR BindingDB; P50579; -.
DR ChEMBL; CHEMBL3922; -.
DR DrugBank; DB03396; (2R,3R,4S,5R,6E)-3,4,5-Trihydroxy-N-[(3S,6R)-6-hydroxy-2-oxo-3-azepanyl]-2-methoxy-8,8-dimethyl-6-nonenamide.
DR DrugBank; DB04108; (2s,3r)-3-Amino-2-Hydroxy-5-(Ethylsulfanyl)Pentanoyl-((S)-(-)-(1-Naphthyl)Ethyl)Amide.
DR DrugBank; DB07322; 2-[(PHENYLSULFONYL)AMINO]-5,6,7,8-TETRAHYDRONAPHTHALENE-1-CARBOXYLIC ACID.
DR DrugBank; DB07323; 2-[({2-[(1Z)-3-(DIMETHYLAMINO)PROP-1-ENYL]-4-FLUOROPHENYL}SULFONYL)AMINO]-5,6,7,8-TETRAHYDRONAPHTHALENE-1-CARBOXYLIC ACID.
DR DrugBank; DB02310; 3,5,6,8-Tetramethyl-N-Methyl Phenanthrolinium.
DR DrugBank; DB07746; 3-ETHYL-6-{[(4-FLUOROPHENYL)SULFONYL]AMINO}-2-METHYLBENZOIC ACID.
DR DrugBank; DB07309; 5-BROMO-2-{[(4-CHLOROPHENYL)SULFONYL]AMINO}BENZOIC ACID.
DR DrugBank; DB07313; 5-METHYL-2-[(PHENYLSULFONYL)AMINO]BENZOIC ACID.
DR DrugBank; DB02893; D-Methionine.
DR DrugBank; DB02640; Fumagillin.
DR DrugBank; DB00134; Methionine.
DR DrugBank; DB07377; N'-((2S,3R)-3-AMINO-2-HYDROXY-5-(ISOPROPYLSULFANYL)PENTANOYL)-N-3-CHLOROBENZOYL HYDRAZIDE.
DR DrugBank; DB03086; N'-(2s,3r)-3-Amino-4-Cyclohexyl-2-Hydroxy-Butano-N-(4-Methylphenyl)Hydrazide.
DR DrugBank; DB01422; Nitroxoline.
DR DrugBank; DB04324; Ovalicin.
DR DrugBank; DB05864; PPI-2458.
DR DrugBank; DB03900; tert-butanol.
DR DrugBank; DB08633; TNP-470.
DR DrugCentral; P50579; -.
DR GuidetoPHARMACOLOGY; 1573; -.
DR MEROPS; M24.002; -.
DR GlyGen; P50579; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P50579; -.
DR MetOSite; P50579; -.
DR PhosphoSitePlus; P50579; -.
DR SwissPalm; P50579; -.
DR BioMuta; METAP2; -.
DR DMDM; 1703273; -.
DR REPRODUCTION-2DPAGE; IPI00033036; -.
DR EPD; P50579; -.
DR jPOST; P50579; -.
DR MassIVE; P50579; -.
DR MaxQB; P50579; -.
DR PaxDb; P50579; -.
DR PeptideAtlas; P50579; -.
DR PRIDE; P50579; -.
DR ProteomicsDB; 33683; -.
DR ProteomicsDB; 5231; -.
DR ProteomicsDB; 56252; -. [P50579-1]
DR TopDownProteomics; P50579-1; -. [P50579-1]
DR Antibodypedia; 4578; 311 antibodies from 34 providers.
DR DNASU; 10988; -.
DR Ensembl; ENST00000261220.13; ENSP00000261220.9; ENSG00000111142.14. [P50579-2]
DR Ensembl; ENST00000323666.10; ENSP00000325312.5; ENSG00000111142.14. [P50579-1]
DR Ensembl; ENST00000546753.5; ENSP00000448169.1; ENSG00000111142.14. [P50579-3]
DR GeneID; 10988; -.
DR KEGG; hsa:10988; -.
DR MANE-Select; ENST00000323666.10; ENSP00000325312.5; NM_006838.4; NP_006829.1.
DR UCSC; uc001tec.4; human. [P50579-1]
DR CTD; 10988; -.
DR DisGeNET; 10988; -.
DR GeneCards; METAP2; -.
DR HGNC; HGNC:16672; METAP2.
DR HPA; ENSG00000111142; Low tissue specificity.
DR MIM; 601870; gene.
DR neXtProt; NX_P50579; -.
DR OpenTargets; ENSG00000111142; -.
DR PharmGKB; PA30765; -.
DR VEuPathDB; HostDB:ENSG00000111142; -.
DR eggNOG; KOG2775; Eukaryota.
DR GeneTree; ENSGT00940000155016; -.
DR InParanoid; P50579; -.
DR OMA; NEIAAHY; -.
DR PhylomeDB; P50579; -.
DR TreeFam; TF300426; -.
DR BioCyc; MetaCyc:HS03371-MON; -.
DR BRENDA; 3.4.11.18; 2681.
DR PathwayCommons; P50579; -.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR SignaLink; P50579; -.
DR BioGRID-ORCS; 10988; 478 hits in 1101 CRISPR screens.
DR ChiTaRS; METAP2; human.
DR EvolutionaryTrace; P50579; -.
DR GeneWiki; METAP2; -.
DR GenomeRNAi; 10988; -.
DR Pharos; P50579; Tchem.
DR PRO; PR:P50579; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P50579; protein.
DR Bgee; ENSG00000111142; Expressed in sural nerve and 202 other tissues.
DR ExpressionAtlas; P50579; baseline and differential.
DR Genevisible; P50579; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008235; F:metalloexopeptidase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031365; P:N-terminal protein amino acid modification; IDA:HGNC-UCL.
DR GO; GO:0018206; P:peptidyl-methionine modification; IDA:HGNC-UCL.
DR GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IDA:HGNC-UCL.
DR CDD; cd01088; MetAP2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_03175; MetAP_2_euk; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002468; Pept_M24A_MAP2.
DR InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00501; met_pdase_II; 1.
DR PROSITE; PS01202; MAP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminopeptidase; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW Phosphoprotein; Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..478
FT /note="Methionine aminopeptidase 2"
FT /id="PRO_0000148982"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:16540317"
FT BINDING 251
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930,
FT ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258,
FT ECO:0000269|PubMed:17636946"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930,
FT ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258,
FT ECO:0000269|PubMed:17636946"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930,
FT ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258,
FT ECO:0000269|PubMed:17636946"
FT BINDING 331
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930,
FT ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258,
FT ECO:0000269|PubMed:17636946"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:16540317"
FT BINDING 364
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930,
FT ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258,
FT ECO:0000269|PubMed:17636946"
FT BINDING 459
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930,
FT ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258,
FT ECO:0000269|PubMed:17636946"
FT BINDING 459
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175,
FT ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930,
FT ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258,
FT ECO:0000269|PubMed:17636946"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 60
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 63
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CARBOHYD 60
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055467"
FT VAR_SEQ 87..109
FT /note="DGDGDGDGATGKKKKKKKKKRGP -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055468"
FT VAR_SEQ 109..132
FT /note="PKVQTDPPSVPICDLYPNGVFPKG -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057353"
FT CONFLICT 434
FT /note="N -> D (in Ref. 3; BAC03733)"
FT /evidence="ECO:0000305"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6QEJ"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1R58"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 163..186
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 193..208
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1QZY"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 360..370
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:5D6E"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:5D6E"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:5D6E"
FT HELIX 429..437
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 455..464
FT /evidence="ECO:0007829|PDB:5D6E"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:5D6E"
SQ SEQUENCE 478 AA; 52892 MW; 5788E4BB83E48F9A CRC64;
MAGVEEVAAS GSHLNGDLDP DDREEGAAST AEEAAKKKRR KKKKSKGPSA AGEQEPDKES
GASVDEVARQ LERSALEDKE RDEDDEDGDG DGDGATGKKK KKKKKKRGPK VQTDPPSVPI
CDLYPNGVFP KGQECEYPPT QDGRTAAWRT TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR
KYVMSWIKPG MTMIEICEKL EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT
VLQYDDICKI DFGTHISGRI IDCAFTVTFN PKYDTLLKAV KDATNTGIKC AGIDVRLCDV
GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGQYRIHA GKTVPIVKGG EATRMEEGEV
YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK HLLNVINENF GTLAFCRRWL
DRLGESKYLM ALKNLCDLGI VDPYPPLCDI KGSYTAQFEH TILLRPTCKE VVSRGDDY
