NEP_MOUSE
ID NEP_MOUSE Reviewed; 750 AA.
AC Q61391; Q6NXX5; Q8K251;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Neprilysin;
DE EC=3.4.24.11 {ECO:0000250|UniProtKB:P08473};
DE AltName: Full=Atriopeptidase;
DE AltName: Full=Enkephalinase;
DE AltName: Full=Neutral endopeptidase 24.11 {ECO:0000303|PubMed:1374101};
DE Short=NEP;
DE Short=Neutral endopeptidase;
DE AltName: Full=Skin fibroblast elastase {ECO:0000303|PubMed:20876573};
DE Short=SFE {ECO:0000303|PubMed:20876573};
DE AltName: CD_antigen=CD10 {ECO:0000303|PubMed:1374101};
GN Name=Mme {ECO:0000303|PubMed:27588448, ECO:0000312|MGI:MGI:97004};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=1374101;
RA Chen C.Y., Salles G., Seldin M.F., Kister A.E., Reinher E.L., Shipp M.A.;
RT "Murine common acute lymphoblastic leukemia antigen (CD10 neutral
RT endopeptidase 24.11). Molecular characterization, chromosomal localization,
RT and modeling of the active site.";
RL J. Immunol. 148:2817-2825(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Epididymis, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryonic germ cell, and Mammary tumor;
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 [4]
RP PROTEIN SEQUENCE OF 473-479, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145; ASN-285 AND ASN-311.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-6, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP IDENTIFICATION AS SKIN FIBROBLAST ELASTASE, AND FUNCTION.
RX PubMed=20876573; DOI=10.1074/jbc.m110.161547;
RA Morisaki N., Moriwaki S., Sugiyama-Nakagiri Y., Haketa K., Takema Y.,
RA Imokawa G.;
RT "Neprilysin is identical to skin fibroblast elastase: its role in skin
RT aging and UV responses.";
RL J. Biol. Chem. 285:39819-39827(2010).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=27588448; DOI=10.1016/j.ajhg.2016.07.008;
RA Auer-Grumbach M., Toegel S., Schabhuettl M., Weinmann D., Chiari C.,
RA Bennett D.L., Beetz C., Klein D., Andersen P.M., Boehme I., Fink-Puches R.,
RA Gonzalez M., Harms M.B., Motley W., Reilly M.M., Renner W.,
RA Rudnik-Schoeneborn S., Schlotter-Weigel B., Themistocleous A.C.,
RA Weishaupt J.H., Ludolph A.C., Wieland T., Tao F., Abreu L., Windhager R.,
RA Zitzelsberger M., Strom T.M., Walther T., Scherer S.S., Zuechner S.,
RA Martini R., Senderek J.;
RT "Rare variants in MME, encoding metalloprotease neprilysin, are linked to
RT late-onset autosomal-dominant axonal polyneuropathies.";
RL Am. J. Hum. Genet. 99:607-623(2016).
CC -!- FUNCTION: Thermolysin-like specificity, but is almost confined on
CC acting on polypeptides of up to 30 amino acids (By similarity).
CC Biologically important in the destruction of opioid peptides such as
CC Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (By similarity).
CC Catalyzes cleavage of bradykinin, substance P and neurotensin peptides
CC (By similarity). Able to cleave angiotensin-1, angiotensin-2 and
CC angiotensin 1-9 (By similarity). Involved in the degradation of the
CC atrial natriuretic factor (ANF) (By similarity). Displays UV-inducible
CC elastase activity toward skin preelastic and elastic fibers
CC (PubMed:20876573). {ECO:0000250|UniProtKB:P08473,
CC ECO:0000269|PubMed:20876573}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of polypeptides between hydrophobic
CC residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9);
CC Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC ChEBI:CHEBI:190693, ChEBI:CHEBI:190700;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71460;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-
CC 7); Xref=Rhea:RHEA:71467, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC ChEBI:CHEBI:190695, ChEBI:CHEBI:190698;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71468;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11);
CC Xref=Rhea:RHEA:71475, ChEBI:CHEBI:15377, ChEBI:CHEBI:147362,
CC ChEBI:CHEBI:190704, ChEBI:CHEBI:190706;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71476;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neurotensin = L-tyrosyl-L-isoleucyl-L-leucine +
CC neurotensin(1-10); Xref=Rhea:RHEA:71479, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:147362, ChEBI:CHEBI:190705, ChEBI:CHEBI:190707;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71480;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08473};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- PTM: Myristoylation is a determinant of membrane targeting.
CC {ECO:0000250|UniProtKB:P08473}.
CC -!- PTM: Glycosylation at Asn-628 is necessary both for surface expression
CC and neutral endopeptidase activity. {ECO:0000250|UniProtKB:P08473}.
CC -!- DISRUPTION PHENOTYPE: Mice are overtly normal in appearance and size
CC and do not show obvious abnormalities in motor performance or
CC coordination. Nerve conduction studies reveal no significant
CC differences between mutant and control animals.
CC {ECO:0000269|PubMed:27588448}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; M81591; AAA37386.1; -; mRNA.
DR EMBL; AK031446; BAC27410.1; -; mRNA.
DR EMBL; AK033824; BAC28487.1; -; mRNA.
DR EMBL; BC034092; AAH34092.1; -; mRNA.
DR EMBL; BC066840; AAH66840.1; -; mRNA.
DR CCDS; CCDS17381.1; -.
DR RefSeq; NP_001276391.1; NM_001289462.1.
DR RefSeq; NP_001276392.1; NM_001289463.1.
DR RefSeq; NP_032630.2; NM_008604.4.
DR RefSeq; XP_006501158.1; XM_006501095.3.
DR RefSeq; XP_006501161.1; XM_006501098.3.
DR PDB; 2YVC; X-ray; 3.20 A; D/E/F=2-23.
DR PDBsum; 2YVC; -.
DR AlphaFoldDB; Q61391; -.
DR SMR; Q61391; -.
DR BioGRID; 201441; 2.
DR STRING; 10090.ENSMUSP00000029400; -.
DR BindingDB; Q61391; -.
DR ChEMBL; CHEMBL2642; -.
DR MEROPS; M13.001; -.
DR GlyConnect; 2529; 2 N-Linked glycans (2 sites).
DR GlyGen; Q61391; 6 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q61391; -.
DR PhosphoSitePlus; Q61391; -.
DR jPOST; Q61391; -.
DR MaxQB; Q61391; -.
DR PaxDb; Q61391; -.
DR PeptideAtlas; Q61391; -.
DR PRIDE; Q61391; -.
DR ProteomicsDB; 287378; -.
DR Antibodypedia; 3658; 2430 antibodies from 55 providers.
DR DNASU; 17380; -.
DR Ensembl; ENSMUST00000029400; ENSMUSP00000029400; ENSMUSG00000027820.
DR Ensembl; ENSMUST00000194134; ENSMUSP00000142205; ENSMUSG00000027820.
DR Ensembl; ENSMUST00000194150; ENSMUSP00000141544; ENSMUSG00000027820.
DR GeneID; 17380; -.
DR KEGG; mmu:17380; -.
DR UCSC; uc008pjp.2; mouse.
DR CTD; 4311; -.
DR MGI; MGI:97004; Mme.
DR VEuPathDB; HostDB:ENSMUSG00000027820; -.
DR eggNOG; KOG3624; Eukaryota.
DR GeneTree; ENSGT00940000156745; -.
DR HOGENOM; CLU_006187_8_0_1; -.
DR InParanoid; Q61391; -.
DR OMA; GYPDEIM; -.
DR OrthoDB; 282463at2759; -.
DR PhylomeDB; Q61391; -.
DR TreeFam; TF315192; -.
DR BRENDA; 3.4.24.11; 3474.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 17380; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Mme; mouse.
DR EvolutionaryTrace; Q61391; -.
DR PRO; PR:Q61391; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61391; protein.
DR Bgee; ENSMUSG00000027820; Expressed in epithelium of lens and 214 other tissues.
DR ExpressionAtlas; Q61391; baseline and differential.
DR Genevisible; Q61391; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:1901612; F:cardiolipin binding; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0008238; F:exopeptidase activity; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0070012; F:oligopeptidase activity; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0042277; F:peptide binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0097242; P:amyloid-beta clearance; IGI:ARUK-UCL.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; ISO:MGI.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IDA:MGI.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
DR GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR GO; GO:0046449; P:creatinine metabolic process; ISS:UniProtKB.
DR GO; GO:0042447; P:hormone catabolic process; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0061837; P:neuropeptide processing; ISO:MGI.
DR GO; GO:0006518; P:peptide metabolic process; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0090399; P:replicative senescence; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0010814; P:substance P catabolic process; ISS:UniProtKB.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR IDEAL; IID50229; -.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR029727; MME/CD10/NEP.
DR InterPro; IPR000718; Peptidase_M13.
DR InterPro; IPR018497; Peptidase_M13_C.
DR InterPro; IPR042089; Peptidase_M13_dom_2.
DR InterPro; IPR008753; Peptidase_M13_N.
DR PANTHER; PTHR11733; PTHR11733; 1.
DR PANTHER; PTHR11733:SF114; PTHR11733:SF114; 1.
DR Pfam; PF01431; Peptidase_M13; 1.
DR Pfam; PF05649; Peptidase_M13_N; 1.
DR PRINTS; PR00786; NEPRILYSIN.
DR PROSITE; PS51885; NEPRILYSIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Metalloprotease; Myristate; Phosphoprotein; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT CHAIN 2..750
FT /note="Neprilysin"
FT /id="PRO_0000078214"
FT TOPO_DOM 2..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..750
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 56..750
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT MOTIF 16..23
FT /note="Stop-transfer sequence"
FT /evidence="ECO:0000255"
FT ACT_SITE 585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 651
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 103
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /ligand_note="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07861"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 588
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT DISULFID 57..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 80..735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 88..695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 143..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 234..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 621..747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CONFLICT 230
FT /note="D -> G (in Ref. 1; AAA37386)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2YVC"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2YVC"
SQ SEQUENCE 750 AA; 85702 MW; 1FC39A971D98F6FE CRC64;
MGRSESQMDI TDINAPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS
DCIKSAARLI QNMDASVEPC TDFFKYACGG WLKRNVIPET SSRYSNFDIL RDELEVILKD
VLQEPKTEDI VAVQKAKTLY RSCINESAID SRGGQPLLKL LPDIYGWPVA SDNWDQTYGT
SWTAEKSIAQ LNSKYGKKVL INFFVGTDDK NSTQHIIHFD QPRLGLPSRD YYECTGIYKE
ACTAYVDFMI SVARLIRQEQ SLPIDENQLS LEMNKVMELE KEIANATTKP EDRNDPMLLY
NKMTLAKLQN NFSLEVNGKS FSWSNFTNEI MSTVNINIQN EEEVVVYAPE YLTKLKPILT
KYSPRDLQNL MSWRFIMDLV SSLSRNYKES RNAFRKALYG TTSETATWRR CANYVNGNME
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKKAE EKALAIKERI
GYPDDIISNE NKLNNEYLEL NYREDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA
VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
GDLVDWWTQQ SANNFKDQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGIGQAYR
AYQNYVKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
GTLQNSAEFA DAFHCRKNSY MNPERKCRVW
