Q9BYT8 (NEUL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neurolysin, mitochondrial
EC=3.4.24.16

Alternative name(s):
Angiotensin-binding protein
Microsomal endopeptidase
Short name=MEP
Mitochondrial oligopeptidase M
Neurotensin endopeptidase

Gene names

Name:	NLN
Synonyms:	AGTBP, KIAA1226

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	704 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A By similarity.
Catalytic activity	Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Mitochondrion intermembrane space By similarity. Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase M3 family.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 37	37	Mitochondrion By similarity
	Chain	38 – 704	667	Neurolysin, mitochondrial		PRO_0000028575
Sites
	Active site	498	1	By similarity
	Metal binding	497	1	Zinc; catalytic By similarity
	Metal binding	501	1	Zinc; catalytic By similarity
	Metal binding	504	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	32	1	Phosphoserine Ref.4 Ref.6
	Modified residue	664	1	N6-acetyllysine Ref.5
Natural variations
	Natural variant	79	1	G → S. Corresponds to variant rs34339013 [ dbSNP | Ensembl ].		VAR_062224
	Natural variant	323	1	S → G. Corresponds to variant rs34063558 [ dbSNP | Ensembl ].		VAR_054002
	Natural variant	372	1	K → R. Corresponds to variant rs6863012 [ dbSNP | Ensembl ].		VAR_054003
	Natural variant	417	1	S → G. Corresponds to variant rs2289884 [ dbSNP | Ensembl ].		VAR_054004
	Natural variant	704	1	P → S. Corresponds to variant rs6860508 [ dbSNP | Ensembl ].		VAR_024594

Sequences

	Sequence		Length	Mass (Da)
	Q9BYT8 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 80136688D79BBEDF	FASTA	704	80,652
	10 20 30 40 50 60 MIARCLLAVR SLRRVGGSRI LLRMTLGREV MSPLQAMSSY TVAGRNVLRW DLSPEQIKTR 70 80 90 100 110 120 TEELIVQTKQ VYDAVGMLGI EEVTYENCLQ ALADVEVKYI VERTMLDFPQ HVSSDKEVRA 130 140 150 160 170 180 ASTEADKRLS RFDIEMSMRG DIFERIVHLQ ETCDLGKIKP EARRYLEKSI KMGKRNGLHL 190 200 210 220 230 240 PEQVQNEIKS MKKRMSELCI DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKTDDDKYK 250 260 270 280 290 300 ITLKYPHYFP VMKKCCIPET RRRMEMAFNT RCKEENTIIL QQLLPLRTKV AKLLGYSTHA 310 320 330 340 350 360 DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILNL KKKECKDRGF EYDGKINAWD 370 380 390 400 410 420 LYYYMTQTEE LKYSIDQEFL KEYFPIEVVT EGLLNTYQEL LGLSFEQMTD AHVWNKSVTL 430 440 450 460 470 480 YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMAVA ALVVNFSQPV 490 500 510 520 530 540 AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD 550 560 570 580 590 600 SLRRLSKHYK DGSPIADDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NTSLDAASEY 610 620 630 640 650 660 AKYCSEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC FKKEGIMNPE 670 680 690 700 VGMKYRNLIL KPGGSLDGMD MLHNFLKREP NQKAFLMSRG LHAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of human neurolysin, an oligopeptidase of family M3." Chen J.M., Rawlings N.D., Barrett A.J. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-664, MASS SPECTROMETRY.
[6]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ300837 mRNA. Translation: CAC27329.1. AB033052 mRNA. Translation: BAA86540.2.
IPI	IPI00010346.
RefSeq	NP_065777.1. NM_020726.4.
UniGene	Hs.247460.
3D structure databases
ProteinModelPortal	Q9BYT8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BYT8. 1 interaction.
STRING	9606.ENSP00000370372.
Protein family/group databases
MEROPS	M03.002.
PTM databases
PhosphoSite	Q9BYT8.
Polymorphism databases
DMDM	20139130.
Proteomic databases
PaxDb	Q9BYT8.
PeptideAtlas	Q9BYT8.
PRIDE	Q9BYT8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380985; ENSP00000370372; ENSG00000123213.
GeneID	57486.
KEGG	hsa:57486.
UCSC	uc003juf.3. human.
Organism-specific databases
CTD	57486.
GeneCards	GC05P065018.
HGNC	HGNC:16058. NLN.
HPA	HPA031862.
MIM	611530. gene.
neXtProt	NX_Q9BYT8.
PharmGKB	PA31651.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0339.
HOGENOM	HOG000245985.
HOVERGEN	HBG000238.
InParanoid	Q9BYT8.
KO	K01393.
OMA	IFLRIVH.
OrthoDB	EOG4CG07P.
PhylomeDB	Q9BYT8.
Gene expression databases
ArrayExpress	Q9BYT8.
Bgee	Q9BYT8.
CleanEx	HS_NLN.
Genevestigator	Q9BYT8.
GermOnline	ENSG00000123213. Homo sapiens.
Family and domain databases
Gene3D	1.10.1370.10. 2 hits. 1.20.1050.40. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR024079. MetalloPept_cat_dom. IPR024077. Neurolysin/TOP_dom2. IPR024080. Neurolysin/TOP_N. IPR001567. Pept_M3A_M3B. [Graphical view]
Pfam	PF01432. Peptidase_M3. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	57486.
NextBio	63764.
SOURCE	Search...

Entry information

Entry name

NEUL_HUMAN

Accession

Primary (citable) accession number: Q9BYT8
Secondary accession number(s): Q9ULJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.