P19801 (ABP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amiloride-sensitive amine oxidase [copper-containing]
Short name=DAO
Short name=Diamine oxidase
EC=1.4.3.22

Alternative name(s):
Amiloride-binding protein
Short name=ABP
Histaminase
Kidney amine oxidase
Short name=KAO

Gene names

Name:	ABP1
Synonyms:	AOC1, DAO1

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	751 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	Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function.
Catalytic activity	Histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2.
Cofactor	Binds 1 copper ion per subunit. Ref.8 Binds 2 calcium ions per subunit. Ref.8 Contains 1 topaquinone per subunit. Ref.8
Subunit structure	Homodimer; disulfide-linked. Ref.8
Subcellular location	Secreted › extracellular space.
Tissue specificity	Placenta and kidney.
Post-translational modification	Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Miscellaneous	Inhibited by amiloride in a competitive manner By similarity.
Sequence similarities	Belongs to the copper/topaquinone oxidase family.
Sequence caution	The sequence AAA58358.1 differs from that shown. Reason: Frameshift at positions 266, 284, 328, 494, 497, 514, 707 and 729.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	Calcium Copper Heparin-binding Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein TPQ
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	amine metabolic process Inferred from electronic annotation. Source: InterPro cellular response to azide Inferred from direct assay PubMed 16846222. Source: UniProtKB cellular response to copper ion Inferred from direct assay PubMed 9399025. Source: UniProtKB cellular response to copper ion starvation Inferred from direct assay PubMed 9399025. Source: UniProtKB cellular response to heparin Traceable author statement Ref.8. Source: UniProtKB cellular response to histamine Inferred from direct assay PubMed 12072962. Source: UniProtKB response to antibiotic Inferred from direct assay Ref.8PubMed 7626074. Source: UniProtKB response to drug Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	extracellular space Inferred from direct assay PubMed 12072962PubMed 9399025. Source: UniProtKB peroxisome Non-traceable author statement PubMed 1356107. Source: UniProtKB plasma membrane Inferred from direct assay Ref.1Ref.7. Source: UniProtKB tight junction Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from direct assay PubMed 12072962Ref.8. Source: UniProtKB copper ion binding Inferred from direct assay PubMed 12072962Ref.8. Source: UniProtKB diamine oxidase activity Inferred from direct assay PubMed 12072962PubMed 16846222Ref.7PubMed 9399025. Source: UniProtKB drug binding Inferred from direct assay Ref.1Ref.7. Source: UniProtKB heparin binding Inferred from direct assay PubMed 12072962Ref.8. Source: UniProtKB histamine oxidase activity Inferred from electronic annotation. Source: EC methylputrescine oxidase activity Inferred from electronic annotation. Source: EC primary amine oxidase activity Inferred from direct assay Ref.8. Source: UniProtKB propane-1,3-diamine oxidase activity Inferred from electronic annotation. Source: EC protein complex binding Inferred from direct assay Ref.8. Source: UniProtKB quinone binding Inferred from direct assay PubMed 12072962Ref.8. Source: UniProtKB receptor activity Inferred from direct assay Ref.1. Source: UniProtKB sodium channel activity Traceable author statement Ref.1. Source: UniProtKB zinc ion binding Inferred from direct assay PubMed 12072962. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P19801-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P19801-2)

Also known as: DAO2;

The sequence of this isoform differs from the canonical sequence as follows:
     619-619: R → RTEGGQPRALSQARSPVPGR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.7

Chain

20 – 751

732

Amiloride-sensitive amine oxidase [copper-containing]

PRO_0000035666

Regions

Region

568 – 575

8

Heparin-binding By similarity

Sites

Active site

373

1

Proton acceptor Ref.8

Active site

461

1

Schiff-base intermediate with substrate; via topaquinone Ref.8

Metal binding

510

1

Copper

Metal binding

512

1

Copper

Metal binding

519

1

Calcium 1

Metal binding

520

1

Calcium 1; via carbonyl oxygen

Metal binding

521

1

Calcium 1

Metal binding

562

1

Calcium 2

Metal binding

653

1

Calcium 2; via carbonyl oxygen

Metal binding

656

1

Calcium 2

Metal binding

658

1

Calcium 2

Metal binding

664

1

Calcium 1

Metal binding

665

1

Calcium 1; via carbonyl oxygen

Metal binding

675

1

Copper

Amino acid modifications

Modified residue

461

1

2',4',5'-topaquinone

Glycosylation

110

1

N-linked (GlcNAc...) Ref.8

Glycosylation

168

1

N-linked (GlcNAc...) Potential

Glycosylation

538

1

N-linked (GlcNAc...) Ref.8

Glycosylation

745

1

N-linked (GlcNAc...) Ref.8

Disulfide bond

177 ↔ 181

Ref.8

Disulfide bond

391 ↔ 417

Ref.8

Disulfide bond

736

Interchain Ref.8

Natural variations

Alternative sequence

619

1

R → RTEGGQPRALSQARSPVPGR in isoform 2.

VSP_006548

Natural variant

16

1

T → M. Ref.4
Corresponds to variant rs10156191 [ dbSNP | Ensembl ].

VAR_025078

Natural variant

332

1

S → F. Ref.3 Ref.4
Corresponds to variant rs1049742 [ dbSNP | Ensembl ].

VAR_025079

Natural variant

479

1

M → I. Ref.4
Corresponds to variant rs45558339 [ dbSNP | Ensembl ].

VAR_025080

Natural variant

645

1

H → D. Ref.1 Ref.3 Ref.4 Ref.6
Corresponds to variant rs1049793 [ dbSNP | Ensembl ].

VAR_007542

Natural variant

659

1

N → H. Ref.4
Corresponds to variant rs35070995 [ dbSNP | Ensembl ].

VAR_025081

Experimental info

Sequence conflict

28

1

R → A AA sequence Ref.7

Sequence conflict

280

1

P → A in AAA58358. Ref.1

Sequence conflict

290

1

D → T in AAA58358. Ref.1

Sequence conflict

572

1

K → R in AAA58358. Ref.1

Sequence conflict

592

1

T → S in AAA58358. Ref.1

Sequence conflict

592

1

T → S in CAA55046. Ref.2

Sequence conflict

592

1

T → S in AAC50270. Ref.3

Sequence conflict

592

1

T → S in AAB60381. Ref.3

Sequence conflict

592

1

T → S in AAH14093. Ref.6

Secondary structure

1

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751

Helix Strand Turn

Details...

Helix

29 – 33

5

Helix

38 – 49

12

Helix

52 – 54

3

Beta strand

64 – 75

12

Helix

79 – 88

10

Beta strand

96 – 103

8

Beta strand

105 – 108

4

Beta strand

110 – 117

8

Beta strand

119 – 121

3

Beta strand

124 – 129

6

Helix

137 – 140

4

Helix

145 – 158

14

Helix

160 – 162

3

Helix

163 – 170

8

Beta strand

173 – 176

4

Beta strand

178 – 186

9

Beta strand

191 – 193

3

Beta strand

198 – 205

8

Helix

210 – 212

3

Beta strand

214 – 222

9

Beta strand

225 – 227

3

Helix

228 – 230

3

Beta strand

232 – 238

7

Helix

246 – 254

9

Beta strand

301 – 303

3

Beta strand

309 – 313

5

Beta strand

316 – 320

5

Beta strand

322 – 329

8

Turn

330 – 332

3

Beta strand

333 – 341

9

Beta strand

344 – 359

16

Helix

364 – 368

5

Beta strand

370 – 372

3

Helix

373 – 376

4

Helix

378 – 380

3

Turn

387 – 389

3

Beta strand

395 – 405

11

Beta strand

410 – 422

13

Beta strand

427 – 433

7

Beta strand

435 – 445

11

Beta strand

448 – 456

9

Beta strand

458 – 469

12

Beta strand

475 – 483

9

Beta strand

487 – 489

3

Helix

492 – 496

5

Beta strand

497 – 502

6

Beta strand

505 – 508

4

Beta strand

510 – 520

11

Beta strand

524 – 540

17

Beta strand

547 – 559

13

Helix

562 – 565

4

Beta strand

569 – 571

3

Beta strand

575 – 584

10

Beta strand

590 – 598

9

Helix

610 – 619

10

Beta strand

621 – 626

6

Helix

629 – 631

3

Turn

637 – 641

5

Beta strand

643 – 645

3

Helix

652 – 655

4

Beta strand

661 – 675

15

Helix

679 – 681

3

Beta strand

691 – 704

14

Helix

706 – 709

4

Beta strand

714 – 717

4

Beta strand

720 – 723

4

Beta strand

725 – 727

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 7, 2009. Version 4. Checksum: 37114CD0D446639C	FASTA	751	85,378
	10 20 30 40 50 60 MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS KKELRLQPSS 70 80 90 100 110 120 TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV IFFGDQEHPN VTEFAVGPLP 130 140 150 160 170 180 GPCYMRALSP RPGYQSSWAS RPISTAEYAL LYHTLQEATK PLHQFFLNTT GFSFQDCHDR 190 200 210 220 230 240 CLAFTDVAPR GVASGQRRSW LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG 250 260 270 280 290 300 KFYGSPEELA RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP 310 320 330 340 350 360 RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV SVQEAVALYG 370 380 390 400 410 420 GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT FHYYDADDPV HYPRALCLFE 430 440 450 460 470 480 MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH 490 500 510 520 530 540 ATGYVHATFY TPEGLRHGTR LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT 550 560 570 580 590 600 NPWSPRHRVV QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM 610 620 630 640 650 660 ADQVLPPGWQ EEQAITWARY PLAVTKYRES ELCSSSIYHQ NDPWHPPVVF EQFLHNNENI 670 680 690 700 710 720 ENEDLVAWVT VGFLHIPHSE DIPNTATPGN SVGFLLRPFN FFPEDPSLAS RDTVIVWPRD 730 740 750 NGPNYVQRWI PEDRDCSMPP PFSYNGTYRP V
	Isoform 2 (DAO2) [UniParc]. Checksum: D592FC97BA29D7CC	FASTA	770	87,324
	10 20 30 40 50 60 MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS KKELRLQPSS 70 80 90 100 110 120 TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV IFFGDQEHPN VTEFAVGPLP 130 140 150 160 170 180 GPCYMRALSP RPGYQSSWAS RPISTAEYAL LYHTLQEATK PLHQFFLNTT GFSFQDCHDR 190 200 210 220 230 240 CLAFTDVAPR GVASGQRRSW LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG 250 260 270 280 290 300 KFYGSPEELA RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP 310 320 330 340 350 360 RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV SVQEAVALYG 370 380 390 400 410 420 GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT FHYYDADDPV HYPRALCLFE 430 440 450 460 470 480 MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH 490 500 510 520 530 540 ATGYVHATFY TPEGLRHGTR LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT 550 560 570 580 590 600 NPWSPRHRVV QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM 610 620 630 640 650 660 ADQVLPPGWQ EEQAITWART EGGQPRALSQ ARSPVPGRYP LAVTKYRESE LCSSSIYHQN 670 680 690 700 710 720 DPWHPPVVFE QFLHNNENIE NEDLVAWVTV GFLHIPHSED IPNTATPGNS VGFLLRPFNF 730 740 750 760 770 FPEDPSLASR DTVIVWPRDN GPNYVQRWIP EDRDCSMPPP FSYNGTYRPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human kidney amiloride-binding protein: cDNA structure and functional expression." Barbry P., Champe M., Chassande O., Munemitsu S., Champigny G., Lingueglia E., Maes P., Frelin C., Tartar A., Ullrich A., Lazdunski M. Proc. Natl. Acad. Sci. U.S.A. 87:7347-7351(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT ASP-645. Tissue: Kidney.
[2]	"The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter." Chassande O., Renard S., Barbry P., Lazdunski M. J. Biol. Chem. 269:14484-14489(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"cDNA sequences of variant forms of human placenta diamine oxidase." Zhang X., Kim J., McIntire W.S. Biochem. Genet. 33:261-268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS PHE-332 AND ASP-645. Tissue: Placenta.
[4]	NIEHS SNPs program Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-16; PHE-332; ILE-479; ASP-645 AND HIS-659.
[5]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-645. Tissue: Colon.
[7]	"Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues." Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P. J. Biol. Chem. 269:9921-9925(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-39, CHARACTERIZATION. Tissue: Placenta.
[8]	"Structure and inhibition of human diamine oxidase." McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M. Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, COFACTOR, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M55602 mRNA. Translation: AAA58358.1. Frameshift.
X78212 Genomic DNA. Translation: CAA55046.1.
U11862 mRNA. Translation: AAC50270.1.
U11863 mRNA. Translation: AAB60381.1.
AY948960 Genomic DNA. Translation: AAX81409.1.
AC006343 Genomic DNA. No translation available.
BC014093 mRNA. Translation: AAH14093.1.

IPI

IPI00020982.
IPI00219832.

PIR

A54053.

RefSeq

NP_001082.2. NM_001091.3.

UniGene

Hs.647097.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HI7	X-ray	1.80	A/B	22-751	[»]
3HIG	X-ray	2.09	A/B	22-751	[»]
3HII	X-ray	2.15	A/B	22-751	[»]
3K5T	X-ray	2.11	A	22-751	[»]
3MPH	X-ray	2.05	A/B	22-751	[»]

ProteinModelPortal

P19801.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000354193.

PTM databases

PhosphoSite

P19801.

Polymorphism databases

DMDM

251757489.

Proteomic databases

PaxDb

P19801.

PRIDE

P19801.

Protocols and materials databases

DNASU

26.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360937; ENSP00000354193; ENSG00000002726.
ENST00000467291; ENSP00000418328; ENSG00000002726.
ENST00000493429; ENSP00000418614; ENSG00000002726.

GeneID

26.

KEGG

hsa:26.

UCSC

uc003why.1. human.

Organism-specific databases

CTD

26.

GeneCards

GC07P150521.

H-InvDB

HIX0007216.

HGNC

HGNC:80. ABP1.

HPA

HPA031032.
HPA031033.

MIM

104610. gene.

neXtProt

NX_P19801.

PharmGKB

PA24416.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3733.

HOGENOM

HOG000233919.

HOVERGEN

HBG004164.

InParanoid

P19801.

KO

K11182.

OrthoDB

EOG4RV2QQ.

PhylomeDB

P19801.

Gene expression databases

ArrayExpress

P19801.

Bgee

P19801.

CleanEx

HS_ABP1.

Genevestigator

P19801.

GermOnline

ENSG00000002726. Homo sapiens.

Family and domain databases

Gene3D

2.70.98.20. 1 hit.
3.10.450.40. 1 hit.

InterPro

IPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]

PANTHER

PTHR10638. PTHR10638. 1 hit.

Pfam

PF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]

PRINTS

PR00766. CUDAOXIDASE.

SUPFAM

SSF54416. Cu_amine_oxidase_N-reg. 2 hits.
SSF49998. CuNH_oxidase. 1 hit.

PROSITE

PS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P19801.

ChEMBL

CHEMBL2118.

DrugBank

DB00594. Amiloride.
DB00127. Spermine.

EvolutionaryTrace

P19801.

GenomeRNAi

26.

NextBio

85.

SOURCE

Search...

Entry information

Entry name

ABP1_HUMAN

Accession

Primary (citable) accession number: P19801
Secondary accession number(s): Q16683 , Q16684, Q56II4, Q6GU42

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 7, 2009
Last modified:	May 1, 2013
This is version 139 of the entry and version 4 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.