P05000 (IFNW1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interferon omega-1

Alternative name(s):
Interferon alpha-II-1

Gene names

Name:

IFNW1

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	195 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)

Subcellular location	Secreted.
Sequence similarities	Belongs to the alpha/beta interferon family.

Ontologies

Keywords
Biological process	Antiviral defense
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Cytokine
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle arrest Traceable author statement PubMed 10835682. Source: ProtInc defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW response to virus Traceable author statement Ref.2. Source: ProtInc
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytokine receptor binding Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Or 23 in some molecules Ref.8 Ref.9 Ref.10

Chain

22 – 195

174

Interferon omega-1

PRO_0000016408

Amino acid modifications

Glycosylation

101

1

N-linked (GlcNAc...) Ref.10

CAR_000050

Disulfide bond

24 ↔ 122

By similarity

Disulfide bond

52 ↔ 162

Ref.12

Natural variations

Natural variant

95

1

R → S.
Corresponds to variant rs2230055 [ dbSNP | Ensembl ].

VAR_020028

Experimental info

Sequence conflict

22 – 23

2

LG → EF in AAA70091. Ref.7

Sequence conflict

42

1

H → M AA sequence Ref.8

Sequence conflict

79

1

V → A in AAA70091. Ref.7

Sequence conflict

111

1

G → E in AAA52724. Ref.1

Sequence conflict

167

1

V → D in AAA70091. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

195

Helix Strand Turn

Details...

Helix

31 – 43

13

Helix

49 – 52

4

Helix

73 – 91

19

Helix

96 – 98

3

Helix

102 – 119

18

Helix

139 – 157

19

Helix

161 – 178

18

Sequences

	Sequence		Length	Mass (Da)
	P05000 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: 1E4306F3487987FA	FASTA	195	22,319
	10 20 30 40 50 60 MALLFPLLAA LVMTSYSPVG SLGCDLPQNH GLLSRNTLVL LHQMRRISPF LCLKDRRDFR 70 80 90 100 110 120 FPQEMVKGSQ LQKAHVMSVL HEMLQQIFSL FHTERSSAAW NMTLLDQLHT GLHQQLQHLE 130 140 150 160 170 180 TCLLQVVGEG ESAGAISSPA LTLRRYFQGI RVYLKEKKYS DCAWEVVRME IMKSLFLSTN 190 MQERLRSKDR DLGSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two distinct families of human and bovine interferon-alpha genes are coordinately expressed and encode functional polypeptides." Capon D.J., Shepard H.M., Goeddel D.V. Mol. Cell. Biol. 5:768-779(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Human interferon omega 1: isolation of the gene, expression in Chinese hamster ovary cells and characterization of the recombinant protein." Adolf G.R., Fruehbeis B., Hauptmann R., Kalsner I., Maurer-Fogy I., Ostermann E., Patzelt E., Schwendenwein R., Sommergruber W., Zoephel A. Biochim. Biophys. Acta 1089:167-174(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leukocyte.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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].
[6]	"A novel class of human type I interferons." Hauptmann R., Swetly P. Nucleic Acids Res. 13:4739-4749(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-195.
[7]	"Cloning, sequencing and expression in E. coli of interferon-omega 1 gene." Li M.F., Zeng Q., Zhou Y., Guo H.Y., Hou Y.D. Sci. China, Ser. B, Chem. Life Sci. Earth Sci. 36:1361-1366(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-195.
[8]	"Identification of glycosylated subtypes of interferon-alpha produced by human leukocytes." Shirono H., Koga J., Uemura H., Matsuo A. Biosci. Biotechnol. Biochem. 58:1714-1715(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-55.
[9]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-36.
[10]	"Purification and characterization of natural human interferon omega 1. Two alternative cleavage sites for the signal peptidase." Adolf G.R., Maurer-Fogy I., Kalsner I., Cantell K. J. Biol. Chem. 265:9290-9295(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-33, GLYCOSYLATION AT ASN-101.
[11]	"Human IFN-omega 1 gene isolated from embryonic hepar." Yang R.Y., Yang Z.F., Zhu Y.T., Feng L.L., Liu N., Zhao F., Zhang F.X., Fu L.C. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-195. Tissue: Liver.
[12]	"Structural linkage between ligand discrimination and receptor activation by type I interferons." Thomas C., Moraga I., Levin D., Krutzik P.O., Podoplelova Y., Trejo A., Lee C., Yarden G., Vleck S.E., Glenn J.S., Nolan G.P., Piehler J., Schreiber G., Garcia K.C. Cell 146:621-632(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 22-195 IN COMPLEX WITH IFNAR1 AND IFNAR2, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M11003 Genomic DNA. Translation: AAA52724.1.
X58822 Genomic DNA. Translation: CAA41626.1.
AL390882 Genomic DNA. Translation: CAH70158.1.
CH471071 Genomic DNA. Translation: EAW58624.1.
BC069095 mRNA. Translation: AAH69095.1.
BC117290 mRNA. Translation: AAI17291.1.
BC117292 mRNA. Translation: AAI17293.1.
X02669 mRNA. Translation: CAA26501.1.
U25670 Genomic DNA. Translation: AAA70091.1.
AY780805 mRNA. Translation: AAV49320.1.

IPI

IPI00006434.

PIR

IVHUII. A93070.
PC2204.
PC2205.

RefSeq

NP_002168.1. NM_002177.1.

UniGene

Hs.73010.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SE4	X-ray	3.50	B	22-195	[»]

ProteinModelPortal

P05000.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05000. 2 interactions.

STRING

9606.ENSP00000369578.

PTM databases

GlycoSuiteDB

P05000.

PhosphoSite

P05000.

Polymorphism databases

DMDM

400061.

Proteomic databases

PaxDb

P05000.

PRIDE

P05000.

Protocols and materials databases

DNASU

3467.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380229; ENSP00000369578; ENSG00000177047.

GeneID

3467.

KEGG

hsa:3467.

UCSC

uc003zol.1. human.

Organism-specific databases

CTD

3467.

GeneCards

GC09M021103.

HGNC

HGNC:5448. IFNW1.

MIM

147553. gene.

neXtProt

NX_P05000.

PharmGKB

PA29683.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG71630.

HOGENOM

HOG000230500.

HOVERGEN

HBG052086.

InParanoid

P05000.

KO

K05440.

OMA

RISPFLC.

OrthoDB

EOG4KKZ45.

PhylomeDB

P05000.

Gene expression databases

Bgee

P05000.

CleanEx

HS_IFNW1.

Genevestigator

P05000.

GermOnline

ENSG00000177047. Homo sapiens.

Family and domain databases

Gene3D

1.20.1250.10. 1 hit.

InterPro

IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000471. Interferon_alpha/beta/delta.
[Graphical view]

PANTHER

PTHR11691. PTHR11691. 1 hit.

Pfam

PF00143. Interferon. 1 hit.
[Graphical view]

PRINTS

PR00266. INTERFERONAB.

SMART

SM00076. IFabd. 1 hit.
[Graphical view]

SUPFAM

SSF47266. 4_helix_cytokine. 1 hit.

PROSITE

PS00252. INTERFERON_A_B_D. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

3467.

NextBio

13648.

SOURCE

Search...

Entry information

Entry name

IFNW1_HUMAN

Accession

Primary (citable) accession number: P05000
Secondary accession number(s): Q13168 , Q5U802, Q5VWD0, Q7M4P5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 136 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.