P08473 (NEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neprilysin
EC=3.4.24.11

Alternative name(s):
Atriopeptidase
Common acute lymphocytic leukemia antigen
Short name=CALLA
Enkephalinase
Neutral endopeptidase 24.11
Short name=NEP
Short name=Neutral endopeptidase
Skin fibroblast elastase
Short name=SFE
CD_antigen=CD10

Gene names

Name:	MME
Synonyms:	EPN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	750 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	Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers. Ref.9 Ref.12 Ref.14
Catalytic activity	Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
Cofactor	Binds 1 zinc ion per subunit. Ref.17 Ref.18
Enzyme regulation	Inhibited in a dose dependent manner by opiorphin.
Subcellular location	Cell membrane; Single-pass type II membrane protein.
Post-translational modification	Myristoylation is a determinant of membrane targeting.
Miscellaneous	Important cell surface marker in the diagnostic of human acute lymphocytic leukemia.
Sequence similarities	Belongs to the peptidase M13 family.
Biophysicochemical properties	Kinetic parameters: KM=55.1 µM for angiotensin-1 Ref.12 KM=179 µM for angiotensin-2 KM=111.4 µM for angiotensin 1-9
Sequence caution	The sequence CAA30157.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Lipoprotein Myristate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell-cell signaling Traceable author statement. Source: ProtInc proteolysis Traceable author statement. Source: ProtInc
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSPA1A	P08107	3	EBI-353759,EBI-629985
HSPB1	P04792	4	EBI-353759,EBI-352682

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 750

749

Neprilysin

PRO_0000078213

Regions

Topological domain

2 – 28

27

Cytoplasmic Potential

Transmembrane

29 – 51

23

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

52 – 750

699

Extracellular Potential

Motif

16 – 23

8

Stop-transfer sequence Potential

Sites

Active site

591

1

Active site

651

1

Proton donor Ref.10

Metal binding

584

1

Zinc; catalytic

Metal binding

588

1

Zinc; catalytic

Metal binding

647

1

Zinc; catalytic

Binding site

103

1

Substrate carboxyl By similarity

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine Ref.15

Glycosylation

145

1

N-linked (GlcNAc...) Ref.11 Ref.16 Ref.17 Ref.18

Glycosylation

285

1

N-linked (GlcNAc...) Ref.11

Glycosylation

325

1

N-linked (GlcNAc...) Ref.16 Ref.17 Ref.18

Glycosylation

628

1

N-linked (GlcNAc...) Ref.16 Ref.17 Ref.18

Disulfide bond

57 ↔ 62

Ref.17 Ref.18

Disulfide bond

80 ↔ 735

Ref.17 Ref.18

Disulfide bond

88 ↔ 695

Ref.17 Ref.18

Disulfide bond

143 ↔ 411

Ref.17 Ref.18

Disulfide bond

234 ↔ 242

Ref.17 Ref.18

Disulfide bond

621 ↔ 747

Ref.17 Ref.18

Experimental info

Sequence conflict

26

1

P → R in AAA51915. Ref.4

Sequence conflict

44

1

T → R in AAA51915. Ref.4

Sequence conflict

81

1

T → R in AAA51915. Ref.4

Sequence conflict

304

1

T → R in AAA51915. Ref.4

Secondary structure

1

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750

Helix Strand Turn

Details...

Helix

60 – 72

13

Turn

79 – 81

3

Helix

83 – 94

12

Beta strand

102 – 105

4

Helix

106 – 122

17

Helix

131 – 144

14

Helix

146 – 151

6

Turn

152 – 154

3

Helix

155 – 160

6

Helix

161 – 164

4

Helix

168 – 170

3

Helix

174 – 177

4

Turn

178 – 181

4

Helix

184 – 195

12

Beta strand

200 – 208

9

Beta strand

211 – 220

10

Beta strand

225 – 228

4

Helix

229 – 233

5

Helix

236 – 238

3

Helix

239 – 259

21

Helix

266 – 286

21

Helix

290 – 292

3

Helix

296 – 299

4

Beta strand

302 – 304

3

Helix

305 – 311

7

Helix

323 – 331

9

Helix

332 – 334

3

Beta strand

343 – 347

5

Helix

349 – 359

11

Helix

364 – 379

16

Helix

380 – 382

3

Helix

385 – 389

5

Helix

392 – 399

8

Helix

407 – 418

12

Helix

420 – 431

12

Helix

436 – 457

22

Helix

463 – 475

13

Beta strand

477 – 482

6

Helix

485 – 488

4

Helix

490 – 496

7

Turn

497 – 499

3

Helix

507 – 523

17

Turn

524 – 527

4

Beta strand

545 – 547

3

Turn

548 – 551

4

Beta strand

552 – 556

5

Helix

557 – 559

3

Turn

562 – 564

3

Helix

571 – 576

6

Helix

578 – 587

10

Helix

588 – 590

3

Helix

594 – 596

3

Helix

609 – 627

19

Helix

632 – 634

3

Turn

641 – 644

4

Helix

645 – 669

25

Helix

682 – 693

12

Beta strand

696 – 698

3

Helix

700 – 709

10

Helix

715 – 724

10

Helix

727 – 732

6

Sequences

	Sequence		Length	Mass (Da)
	P08473 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: BCF3827C39898630	FASTA	750	85,514
	10 20 30 40 50 60 MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS 70 80 90 100 110 120 DCIKSAARLI QNMDATTEPC TDFFKYACGG WLKRNVIPET SSRYGNFDIL RDELEVVLKD 130 140 150 160 170 180 VLQEPKTEDI VAVQKAKALY RSCINESAID SRGGEPLLKL LPDIYGWPVA TENWEQKYGA 190 200 210 220 230 240 SWTAEKAIAQ LNSKYGKKVL INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE 250 260 270 280 290 300 ACTAYVDFMI SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY 310 320 330 340 350 360 NKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE YLTKLKPILT 370 380 390 400 410 420 KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG TTSETATWRR CANYVNGNME 430 440 450 460 470 480 NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKRAE EKALAIKERI 490 500 510 520 530 540 GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA 550 560 570 580 590 600 VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD 610 620 630 640 650 660 GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGLGQAYR 670 680 690 700 710 720 AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII 730 740 750 GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase." Letarte M., Vera S., Tran R., Addis J.B.L., Onizuka R.J., Quackenbush E.J., Jongeneel C.V., McInnes R.R. J. Exp. Med. 168:1247-1253(1988) [PubMed: 2971756] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Molecular cloning of the common acute lymphoblastic leukemia antigen (CALLA) identifies a type II integral membrane protein." Shipp M.A., Richardson N.E., Sayre P.H., Brown N.R., Masteller E.L., Clayton L.K., Ritz J., Reinherz E.L. Proc. Natl. Acad. Sci. U.S.A. 85:4819-4823(1988) [PubMed: 2968607] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Organization of the gene encoding common acute lymphoblastic leukemia antigen (neutral endopeptidase 24.11): multiple miniexons and separate 5' untranslated regions." D'Adamio L., Shipp M.A., Masteller E.L., Reinherz E.L. Proc. Natl. Acad. Sci. U.S.A. 86:7103-7107(1989) [PubMed: 2528730] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[8]	"Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)." Malfroy B., Kuang W.-J., Seeburg P.H., Mason A.J., Schofield P.R. FEBS Lett. 229:206-210(1988) [PubMed: 3162217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-750. Tissue: Placenta.
[9]	"Endopeptidase-24.11 in human plasma degrades atrial natriuretic factor (ANF) to ANF(99-105/106-126)." Yandle T.G., Brennan S.O., Espiner E.A., Nicholls M.G., Richards A.M. Peptides 10:891-894(1989) [PubMed: 2531377] [Abstract] Cited for: FUNCTION IN THE DEGRADATION OF ANF.
[10]	"Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11." Le Moual H., Dion N., Roques B.P., Crine P., Boileau G. Eur. J. Biochem. 221:475-480(1994) [PubMed: 8168535] [Abstract] Cited for: ACTIVE SITE ASP-651.
[11]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-145 AND ASN-285.
[12]	"Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism." Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M. Biochem. J. 383:45-51(2004) [PubMed: 15283675] [Abstract] Cited for: FUNCTION IN ANGIOTENSIN PEPTIDE METABOLISM, BIOPHYSICOCHEMICAL PROPERTIES.
[13]	"Human opiorphin, a natural antinociceptive modulator of opioid-dependent pathways." Wisner A., Dufour E., Messaoudi M., Nejdi A., Marcel A., Ungeheuer M.-N., Rougeot C. Proc. Natl. Acad. Sci. U.S.A. 103:17979-17984(2006) [PubMed: 17101991] [Abstract] Cited for: INHIBITION BY OPIORPHIN.
[14]	"Neprilysin is identical to skin fibroblast elastase: its role in skin aging and UV responses." Morisaki N., Moriwaki S., Sugiyama-Nakagiri Y., Haketa K., Takema Y., Imokawa G. J. Biol. Chem. 285:39819-39827(2010) [PubMed: 20876573] [Abstract] Cited for: IDENTIFICATION AS SKIN FIBROBLAST ELASTASE, FUNCTION.
[15]	"Neutral endopeptidase is a myristoylated protein." Zheng R., Horiguchi A., Iida K., Lee J., Shen R., Goodman O.B. Jr., Nanus D.M. Mol. Cell. Biochem. 335:173-180(2010) [PubMed: 19756956] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.
[16]	"Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon." Oefner C., D'Arcy A., Hennig M., Winkler F.K., Dale G.E. J. Mol. Biol. 296:341-349(2000) [PubMed: 10669592] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
[17]	"Structural analysis of neprilysin with various specific and potent inhibitors." Oefner C., Roques B.P., Fournie-Zaluski M.-C., Dale G.E. Acta Crystallogr. D 60:392-396(2004) [PubMed: 14747736] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 55-750 IN COMPLEXES WITH ZINC IONS AND SYNTHETIC INHIBITORS, DISULFIDE BONDS, COFACTOR, GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
[18]	"Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV." Oefner C., Pierau S., Schulz H., Dale G.E. Acta Crystallogr. D 63:975-981(2007) [PubMed: 17704566] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 55-750 IN COMPLEX WITH ZINC IONS AND THE SYNTHETIC INHIBITOR MCB3937, DISULFIDE BONDS, COFACTOR, GLYCOSYLATION AT ASN-145; ASN-325 AND ASN-628.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00811 mRNA. Translation: CAA68752.1.
J03779 mRNA. Translation: AAA51915.1.
M26628 , M26607, M26608, M26609, M26610, M26611, M26612, M26613, M26614, M26615, M26616, M26617, M26618, M26619, M26620, M26621, M26622, M26623, M26624, M26625, M26626, M26627 Genomic DNA. Translation: AAA52294.1.
AK291761 mRNA. Translation: BAF84450.1.
EU326307 Genomic DNA. Translation: ACA05913.1.
CH471052 Genomic DNA. Translation: EAW78754.1.
CH471052 Genomic DNA. Translation: EAW78755.1.
CH471052 Genomic DNA. Translation: EAW78756.1.
CH471052 Genomic DNA. Translation: EAW78757.1.
CH471052 Genomic DNA. Translation: EAW78758.1.
BC101632 mRNA. Translation: AAI01633.1.
BC101658 mRNA. Translation: AAI01659.1.
X07166 mRNA. Translation: CAA30157.1. Different initiation.

IPI

IPI00247063.

PIR

HYHUN. A41387.

RefSeq

NP_000893.2. NM_000902.3.
NP_009218.2. NM_007287.2.
NP_009219.2. NM_007288.2.
NP_009220.2. NM_007289.2.

UniGene

Hs.307734.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DL9	model	-	A	508-750	[»]
1DMT	X-ray	2.10	A	55-750	[»]
1QVD	model	-	A	55-750	[»]
1R1H	X-ray	1.95	A	55-749	[»]
1R1I	X-ray	2.60	A	55-749	[»]
1R1J	X-ray	2.35	A	55-749	[»]
1Y8J	X-ray	2.25	A	55-749	[»]
2QPJ	X-ray	2.05	A	55-750	[»]
2YB9	X-ray	2.40	A	55-750	[»]

ProteinModelPortal

P08473.

SMR

P08473. Positions 55-750.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08473. 68 interactions.

STRING

P08473.

Protein family/group databases

MEROPS

M13.001.

PTM databases

PhosphoSite

P08473.

Polymorphism databases

DMDM

128062.

Proteomic databases

PeptideAtlas

P08473.

PRIDE

P08473.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360490; ENSP00000353679; ENSG00000196549.
ENST00000404362; ENSP00000384558; ENSG00000196549.
ENST00000460393; ENSP00000418525; ENSG00000196549.
ENST00000462745; ENSP00000419653; ENSG00000196549.
ENST00000492661; ENSP00000420389; ENSG00000196549.
ENST00000493237; ENSP00000417079; ENSG00000196549.

GeneID

4311.

KEGG

hsa:4311.

UCSC

uc003fab.1. human.

Organism-specific databases

CTD

4311.

GeneCards

GC03P154741.

H-InvDB

HIX0003792.

HGNC

HGNC:7154. MME.

HPA

CAB000013.

MIM

120520. gene.

neXtProt

NX_P08473.

PharmGKB

PA30864.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07698.

GeneTree

ENSGT00550000074200.

HOGENOM

HBG701001.

HOVERGEN

HBG005554.

InParanoid

P08473.

OMA

TYRPEYA.

OrthoDB

EOG4XWFXB.

PhylomeDB

P08473.

Gene expression databases

ArrayExpress

P08473.

Bgee

P08473.

CleanEx

HS_MME.

Genevestigator

P08473.

GermOnline

ENSG00000196549. Homo sapiens.

Family and domain databases

InterPro

IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]

Gene3D

G3DSA:3.40.390.10. G3DSA:3.40.390.10. 2 hits.

KO

K01389.

PANTHER

PTHR11733. Peptidase_M13. 1 hit.

Pfam

PF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]

PRINTS

PR00786. NEPRILYSIN.

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00616. Candoxatril.

NextBio

16959.

SOURCE

Search...

Entry information

Entry name

NEP_HUMAN

Accession

Primary (citable) accession number: P08473
Secondary accession number(s): A8K6U6, D3DNJ9, Q3MIX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 152 of the entry and version 2 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.