P49748 (ACADV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Short name=VLCAD
EC=1.3.99.-

Gene names

Name:	ACADVL
Synonyms:	VLCAD

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	655 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	Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accomodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons. Ref.9
Catalytic activity	Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
Cofactor	FAD. Ref.9
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homodimer. Ref.9
Subcellular location	Mitochondrion inner membrane.
Involvement in disease	Defects in ACADVL are the cause of acyl-CoA dehydrogenase very long chain deficiency (ACADVLD) [MIM:201475]. ACADVLD is an autosomal recessive disease which leads to impaired long-chain fatty acid beta-oxidation. It is clinically heterogeneous, with three major phenotypes: a severe childhood form, with early onset, high mortality, and high incidence of cardiomyopathy; a milder childhood form, with later onset, usually with hypoketotic hypoglycemia as the main presenting feature, low mortality, and rare cardiomyopathy; and an adult form, with isolated skeletal muscle involvement, rhabdomyolysis, and myoglobinuria, usually triggered by exercise or fasting. Ref.10 Ref.11 Ref.12
Miscellaneous	A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cardiomyopathy Disease mutation
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	energy derivation by oxidation of organic compounds Traceable author statement. Source: ProtInc fatty acid beta-oxidation using acyl-CoA dehydrogenase Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of fatty acid biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of fatty acid oxidation Inferred from sequence or structural similarity. Source: BHF-UCL regulation of cholesterol metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL temperature homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial nucleoid Inferred from direct assay. Source: BHF-UCL
Molecular function	long-chain-acyl-CoA dehydrogenase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: P49748-1)

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: P49748-2)

The sequence of this isoform differs from the canonical sequence as follows:
     47-68: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 40

40

Mitochondrion By similarity

Chain

41 – 655

615

Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

PRO_0000000515

Regions

Nucleotide binding

214 – 223

10

FAD

Nucleotide binding

249 – 251

3

FAD

Nucleotide binding

435 – 439

5

FAD By similarity

Nucleotide binding

464 – 466

3

FAD

Region

41 – 482

442

Catalytic

Region

338 – 341

4

Substrate binging By similarity

Region

462 – 463

2

Substrate binding

Region

483 – 516

34

Membrane-anchoring Probable

Sites

Active site

462

1

Proton acceptor Ref.9

Binding site

223

1

Substrate; via carbonyl oxygen By similarity

Binding site

366

1

FAD By similarity

Binding site

463

1

Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue

239

1

N6-acetyllysine Ref.7

Modified residue

276

1

N6-acetyllysine By similarity

Modified residue

331

1

N6-acetyllysine Ref.7

Cross-link

331

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence

47 – 68

22

Missing in isoform 2.

VSP_007734

Natural variant

17

1

L → F.
Corresponds to variant rs2230179 [ dbSNP | Ensembl ].

VAR_029286

Natural variant

43

1

G → D in ACADVLD; could be a polymorphism.
Corresponds to variant rs2230178 [ dbSNP | Ensembl ].

VAR_000330

Natural variant

65

1

P → L.
Corresponds to variant rs28934585 [ dbSNP | Ensembl ].

VAR_048176

Natural variant

130

1

Missing in ACADVLD.

VAR_000331

Natural variant

158

1

T → N in ACADVLD.

VAR_000332

Natural variant

159

1

Q → R in ACADVLD.

VAR_000333

Natural variant

174

1

V → M in ACADVLD.

VAR_000334

Natural variant

185

1

G → S in ACADVLD.

VAR_000335

Natural variant

213

1

A → P in ACADVLD.

VAR_010101

Natural variant

218

1

E → K in ACADVLD.

VAR_000336

Natural variant

243

1

L → R in ACADVLD.

VAR_000337

Natural variant

247

1

K → E in ACADVLD.

VAR_010102

Natural variant

247

1

K → T in ACADVLD.

VAR_000338

Natural variant

260

1

T → M in ACADVLD.

VAR_000339

Natural variant

278

1

Missing in ACADVLD.

VAR_000340

Natural variant

281

1

A → D in ACADVLD.

VAR_000341

Natural variant

283

1

V → A in ACADVLD.

VAR_000342

Natural variant

290

1

G → D in ACADVLD.

VAR_000343

Natural variant

294

1

G → E in ACADVLD.

VAR_000344

Natural variant

299

1

K → N in ACADVLD.

VAR_000345

Natural variant

299

1

Missing in ACADVLD.

VAR_000346

Natural variant

317

1

V → A in ACADVLD.

VAR_000347

Natural variant

352

1

M → V in ACADVLD.

VAR_000348

Natural variant

359

1

A → S.
Corresponds to variant rs1051701 [ dbSNP | Ensembl ].

VAR_011990

Natural variant

366

1

R → C in ACADVLD.

VAR_000349

Natural variant

366

1

R → H in ACADVLD.

VAR_000350

Natural variant

381

1

Missing in ACADVLD.

VAR_000351

Natural variant

382

1

K → Q in ACADVLD. Ref.10

VAR_000352

Natural variant

405

1

D → H in ACADVLD.

VAR_000353

Natural variant

441

1

G → D in ACADVLD.
Corresponds to variant rs2309689 [ dbSNP | Ensembl ].

VAR_000354

Natural variant

450

1

R → H in ACADVLD. Ref.11

VAR_000355

Natural variant

453

1

R → Q in ACADVLD.

VAR_000356

Natural variant

454

1

D → N in ACADVLD.

VAR_000357

Natural variant

456

1

R → H in ACADVLD.

VAR_000358

Natural variant

458

1

F → L in ACADVLD.

VAR_010103

Natural variant

459

1

R → W in ACADVLD.

VAR_000359

Natural variant

463

1

G → E in ACADVLD.

VAR_000360

Natural variant

469

1

R → Q in ACADVLD.

VAR_000361

Natural variant

469

1

R → W in ACADVLD.

VAR_000362

Natural variant

490

1

A → P in ACADVLD.

VAR_010104

Natural variant

502

1

L → P in ACADVLD.

VAR_000363

Natural variant

534

1

E → K in ACADVLD.
Corresponds to variant rs2230180 [ dbSNP | Ensembl ].

VAR_010105

Natural variant

602

1

L → I in ACADVLD.

VAR_000364

Natural variant

613

1

R → W in ACADVLD. Ref.10

VAR_000365

Natural variant

615

1

R → Q in ACADVLD.

VAR_010106

Natural variant

623

1

S → F.
Corresponds to variant rs13383 [ dbSNP | Ensembl ].

VAR_011991

Experimental info

Sequence conflict

193

1

G → C in BAA29057. Ref.3

Secondary structure

1

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655

Helix Strand Turn

Details...

Helix

73 – 77

5

Turn

78 – 80

3

Turn

85 – 87

3

Helix

96 – 115

20

Helix

119 – 125

7

Helix

130 – 138

9

Turn

139 – 142

4

Helix

148 – 150

3

Helix

157 – 170

14

Helix

172 – 182

11

Turn

183 – 186

4

Helix

187 – 192

6

Helix

195 – 206

12

Beta strand

212 – 215

4

Beta strand

221 – 223

3

Helix

225 – 227

3

Beta strand

231 – 234

4

Beta strand

238 – 251

14

Turn

252 – 255

4

Beta strand

257 – 268

12

Turn

270 – 272

3

Beta strand

275 – 285

11

Helix

286 – 288

3

Beta strand

289 – 293

5

Beta strand

299 – 301

3

Beta strand

307 – 318

12

Helix

319 – 321

3

Beta strand

322 – 325

4

Helix

329 – 365

37

Helix

373 – 375

3

Helix

377 – 405

29

Helix

412 – 437

26

Helix

439 – 442

4

Helix

448 – 455

8

Helix

456 – 459

4

Beta strand

461 – 463

3

Helix

465 – 485

21

Helix

486 – 488

3

Helix

527 – 529

3

Helix

530 – 554

25

Helix

555 – 560

6

Helix

562 – 591

30

Helix

596 – 622

27

Helix

627 – 644

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: A5594D1EA7911D19	FASTA	655	70,390
	10 20 30 40 50 60 MQAARMAASL GRQLLRLGGG SSRLTALLGQ PRPGPARRPY AGGAAQLALD KSDSHPSDAL 70 80 90 100 110 120 TRKKPAKAES KSFAVGMFKG QLTTDQVFPY PSVLNEEQTQ FLKELVEPVS RFFEEVNDPA 130 140 150 160 170 180 KNDALEMVEE TTWQGLKELG AFGLQVPSEL GGVGLCNTQY ARLVEIVGMH DLGVGITLGA 190 200 210 220 230 240 HQSIGFKGIL LFGTKAQKEK YLPKLASGET VAAFCLTEPS SGSDAASIRT SAVPSPCGKY 250 260 270 280 290 300 YTLNGSKLWI SNGGLADIFT VFAKTPVTDP ATGAVKEKIT AFVVERGFGG ITHGPPEKKM 310 320 330 340 350 360 GIKASNTAEV FFDGVRVPSE NVLGEVGSGF KVAMHILNNG RFGMAAALAG TMRGIIAKAV 370 380 390 400 410 420 DHATNRTQFG EKIHNFGLIQ EKLARMVMLQ YVTESMAYMV SANMDQGATD FQIEAAISKI 430 440 450 460 470 480 FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDLRIFRI FEGTNDILRL FVALQGCMDK 490 500 510 520 530 540 GKELSGLGSA LKNPFGNAGL LLGEAGKQLR RRAGLGSGLS LSGLVHPELS RSGELAVRAL 550 560 570 580 590 600 EQFATVVEAK LIKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGHPTAQHEK 610 620 630 640 650 MLCDTWCIEA AARIREGMAA LQSDPWQQEL YRNFKSISKA LVERGGVVTS NPLGF
	Isoform 2 [UniParc]. Checksum: D84E8F01DF1E8958	FASTA	633	68,058
	10 20 30 40 50 60 MQAARMAASL GRQLLRLGGG SSRLTALLGQ PRPGPARRPY AGGAAQESKS FAVGMFKGQL 70 80 90 100 110 120 TTDQVFPYPS VLNEEQTQFL KELVEPVSRF FEEVNDPAKN DALEMVEETT WQGLKELGAF 130 140 150 160 170 180 GLQVPSELGG VGLCNTQYAR LVEIVGMHDL GVGITLGAHQ SIGFKGILLF GTKAQKEKYL 190 200 210 220 230 240 PKLASGETVA AFCLTEPSSG SDAASIRTSA VPSPCGKYYT LNGSKLWISN GGLADIFTVF 250 260 270 280 290 300 AKTPVTDPAT GAVKEKITAF VVERGFGGIT HGPPEKKMGI KASNTAEVFF DGVRVPSENV 310 320 330 340 350 360 LGEVGSGFKV AMHILNNGRF GMAAALAGTM RGIIAKAVDH ATNRTQFGEK IHNFGLIQEK 370 380 390 400 410 420 LARMVMLQYV TESMAYMVSA NMDQGATDFQ IEAAISKIFG SEAAWKVTDE CIQIMGGMGF 430 440 450 460 470 480 MKEPGVERVL RDLRIFRIFE GTNDILRLFV ALQGCMDKGK ELSGLGSALK NPFGNAGLLL 490 500 510 520 530 540 GEAGKQLRRR AGLGSGLSLS GLVHPELSRS GELAVRALEQ FATVVEAKLI KHKKGIVNEQ 550 560 570 580 590 600 FLLQRLADGA IDLYAMVVVL SRASRSLSEG HPTAQHEKML CDTWCIEAAA RIREGMAALQ 610 620 630 SDPWQQELYR NFKSISKALV ERGGVVTSNP LGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and molecular characterization of its deficiency in two patients." Aoyama T., Souri M., Ueno I., Kamijo T., Yamaguchi S., Rhead W.J., Tanaka K., Hashimoto T. Am. J. Hum. Genet. 57:273-283(1995) [PubMed: 7668252] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene." Andresen B.S., Bross P., Vianey-Saban C., Divry P., Zabot M.-T., Roe C.R., Nada M.A., Byskov A., Kruse T.A., Neve S., Kristiansen K., Knudsen I., Corydon M.J., Gregersen N. Hum. Mol. Genet. 5:461-472(1996) [PubMed: 8845838] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS. Tissue: Placenta.
[3]	"Genomic DNA organization of human mitochondrial very-long-chain acyl-CoA dehydrogenase and mutation analysis." Orii K.O., Aoyama T., Souri M., Orii K.E., Kondo N., Orii T., Hashimoto T. Biochem. Biophys. Res. Commun. 217:987-992(1995) [PubMed: 8554625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Tissue: Peripheral blood.
[4]	"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] (ISOFORMS 1 AND 2). Tissue: Liver, Lung and Pancreas.
[5]	"Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients." Aoyama T., Souri M., Ushikubo S., Kamijo T., Yamaguchi S., Kelley R.I., Rhead W.J., Uetake K., Tanaka K., Hashimoto T. J. Clin. Invest. 95:2465-2473(1995) [PubMed: 7769092] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency." Andresen B.S., Olpin S., Poorthuis B.J.H.M., Scholte H.R., Vianey-Saban C., Wanders R., Ijlst L., Morris A., Pourfarzam M., Bartlett K., Baumgartner E.R., de Klerk J.B.C., Schroeder L.D., Corydon T.J., Lund H., Winter V., Bross P., Bolund L., Gregersen N. Am. J. Hum. Genet. 64:479-494(1999) [PubMed: 9973285] [Abstract] Cited for: REVIEW ON VARIANTS.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-331, MASS SPECTROMETRY.
[8]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase." McAndrew R.P., Wang Y., Mohsen A.W., He M., Vockley J., Kim J.J. J. Biol. Chem. 283:9435-9443(2008) [PubMed: 18227065] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 69-655 IN COMPLEX WITH MYRISTOYL-COA, FUNCTION, SUBUNIT, COFACTOR, ACTIVE SITE.
[10]	"Mutation analysis of very-long-chain acyl-coenzyme A dehydrogenase (VLCAD) deficiency: identification and characterization of mutant VLCAD cDNAs from four patients." Souri M., Aoyama T., Orii K., Yamaguchi S., Hashimoto T. Am. J. Hum. Genet. 58:97-106(1996) [PubMed: 8554073] [Abstract] Cited for: VARIANTS ACADVLD GLU-130 DEL; LYS-299 DEL; GLN-382 AND TRP-613.
[11]	"Very long chain acyl-coenzyme A dehydrogenase deficiency with adult onset." Smelt A.H., Poorthuis B.J.H.M., Onkenhout W., Scholte H.R., Andresen B.S., van Duinen S.G., Gregersen N., Wintzen A.R. Ann. Neurol. 43:540-544(1998) [PubMed: 9546340] [Abstract] Cited for: VARIANT ACADVLD HIS-450.
[12]	"Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase deficiency causing pediatric cardiomyopathy and sudden death." Mathur A., Sims H.F., Gopalakrishnan D., Gibson B., Rinaldo P., Vockley J., Hug G., Strauss A.W. Circulation 99:1337-1343(1999) [PubMed: 10077518] [Abstract] Cited for: VARIANTS ACADVLD.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D43682 mRNA. Translation: BAA07781.1.
L46590 Genomic DNA. Translation: AAA79002.1.
X86556 mRNA. Translation: CAA60253.1.
D78298 Genomic DNA. Translation: BAA29057.1.
BC000399 mRNA. Translation: AAH00399.1.
BC012912 mRNA. Translation: AAH12912.1.
BC020218 mRNA. Translation: AAH20218.1.

IPI

IPI00178744.
IPI01013108.

PIR

S54183.

RefSeq

NP_000009.1. NM_000018.2.
NP_001029031.1. NM_001033859.1.

UniGene

Hs.437178.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2UXW	X-ray	1.45	A	72-655	[»]
3B96	X-ray	1.91	A	69-655	[»]

ProteinModelPortal

P49748.

SMR

P49748. Positions 69-655.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49748. 3 interactions.

MINT

MINT-4824254.

STRING

P49748.

PTM databases

PhosphoSite

P49748.

Polymorphism databases

DMDM

1703068.

Proteomic databases

PRIDE

P49748.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322910; ENSP00000325395; ENSG00000072778.
ENST00000356839; ENSP00000349297; ENSG00000072778.

GeneID

37.

KEGG

hsa:37.

UCSC

uc002gev.1. human.
uc002gew.1. human.

Organism-specific databases

CTD

37.

GeneCards

GC17P007063.

H-InvDB

HIX0013488.

HGNC

HGNC:92. ACADVL.

HPA

HPA019006.
HPA020595.

MIM

201475. phenotype.
609575. gene.

neXtProt

NX_P49748.

Orphanet

26793. Very long chain acyl-CoA dehydrogenase deficiency.

PharmGKB

PA24428.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13137.

HOVERGEN

HBG050448.

InParanoid

P49748.

OrthoDB

EOG4P5K8R.

PhylomeDB

P49748.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.

Reactome

REACT_15380. Diabetes pathways.
REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P49748.

Bgee

P49748.

CleanEx

HS_ACADVL.

Genevestigator

P49748.

GermOnline

ENSG00000072778. Homo sapiens.

Family and domain databases

InterPro

IPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
[Graphical view]

Gene3D

G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.

KO

K09479.

Pfam

PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]

SUPFAM

SSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 1 hit.

PROSITE

PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

143.

SOURCE

Search...

Entry information

Entry name

ACADV_HUMAN

Accession

Primary (citable) accession number: P49748
Secondary accession number(s): O76056, Q8WUL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 122 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.