Wnt inhibitory factor 1 precursor - Homo sapiens (Human)

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Q9Y5W5 (WIF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Wnt inhibitory factor 1
Short name=WIF-1

Gene names

Name:	WIF1
ORF Names:	UNQ191/PRO217

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	379 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

Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation.

Subcellular location

Secreted.

Sequence similarities

Contains 5 EGF-like domains.

Contains 1 WIF domain.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Cellular component	Secreted
Domain	EGF-like domain Repeat Signal
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of fat cell differentiation Inferred from electronic annotation. Source: Compara signal transduction Non-traceable author statement Ref.1. Source: ProtInc
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

Potential

Chain

29 – 379

351

Wnt inhibitory factor 1

PRO_0000007775

Regions

Domain

38 – 177

140

WIF

Domain

178 – 210

EGF-like 1

Domain

211 – 242

EGF-like 2

Domain

243 – 271

EGF-like 3

Domain

274 – 306

EGF-like 4

Domain

307 – 338

EGF-like 5

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

245

N-linked (GlcNAc...) Potential

Disulfide bond

140 ↔ 177

Ref.4

Disulfide bond

182 ↔ 192

By similarity

Disulfide bond

186 ↔ 198

By similarity

Disulfide bond

200 ↔ 209

By similarity

Disulfide bond

214 ↔ 224

By similarity

Disulfide bond

218 ↔ 230

By similarity

Disulfide bond

232 ↔ 241

By similarity

Disulfide bond

246 ↔ 256

By similarity

Disulfide bond

250 ↔ 262

By similarity

Disulfide bond

278 ↔ 288

By similarity

Disulfide bond

282 ↔ 294

By similarity

Disulfide bond

296 ↔ 305

By similarity

Disulfide bond

310 ↔ 320

By similarity

Disulfide bond

314 ↔ 326

By similarity

Disulfide bond

328 ↔ 337

By similarity

Experimental info

Sequence conflict

166

Q → K in AAH18037. Ref.3

Sequence conflict

178

Q → L in AAD25402. Ref.1

Secondary structure

379

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Y5W5 [UniParc].

Last modified March 15, 2005. Version 3.
Checksum: 32ADFA6644833E9D
Show »

FASTA

379

41,528

        10         20         30         40         50         60 
MARRSAFPAA ALWLWSILLC LLALRAEAGP PQEESLYLWI DAHQARVLIG FEEDILIVSE 

        70         80         90        100        110        120 
GKMAPFTHDF RKAQQRMPAI PVNIHSMNFT WQAAGQAEYF YEFLSLRSLD KGIMADPTVN 

       130        140        150        160        170        180 
VPLLGTVPHK ASVVQVGFPC LGKQDGVAAF EVDVIVMNSE GNTILQTPQN AIFFKTCQQA 

       190        200        210        220        230        240 
ECPGGCRNGG FCNERRICEC PDGFHGPHCE KALCTPRCMN GGLCVTPGFC ICPPGFYGVN 

       250        260        270        280        290        300 
CDKANCSTTC FNGGTCFYPG KCICPPGLEG EQCEISKCPQ PCRNGGKCIG KSKCKCSKGY 

       310        320        330        340        350        360 
QGDLCSKPVC EPGCGAHGTC HEPNKCQCQE GWHGRHCNKR YEASLIHALR PAGAQLRQHT 

       370 
PSLKKAEERR DPPESNYIW

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new secreted protein that binds to Wnt proteins and inhibits their activities." Hsieh J.-C., Kodjabachian L., Rebbert M.L., Rattner A., Smallwood P.M., Samos C.H., Nusse R., Dawid I.B., Nathans J. Nature 398:431-436(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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]. Tissue: Brain.
[4]	"NMR structure of the WIF domain of the human Wnt-inhibitory factor-1." Liepinsh E., Banyai L., Patthy L., Otting G. J. Mol. Biol. 357:942-950(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 32-181, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF122922 mRNA. Translation: AAD25402.1.
AY358344 mRNA. Translation: AAQ88710.1.
BC018037 mRNA. Translation: AAH18037.1.

IPI

IPI00001863.

PIR

A59180.

RefSeq

NP_009122.2. NM_007191.4.

UniGene

Hs.284122.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D3J	NMR	-	A	32-181	[»]
2YGN	X-ray	1.85	A	35-178	[»]
2YGO	X-ray	1.85	A	35-210	[»]
2YGP	X-ray	2.22	A	35-210	[»]
2YGQ	X-ray	3.95	A	35-346	[»]

ProteinModelPortal

Q9Y5W5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59097N.

IntAct

Q9Y5W5. 2 interactions.

STRING

9606.ENSP00000286574.

Polymorphism databases

DMDM

61252765.

Proteomic databases

PaxDb

Q9Y5W5.

PRIDE

Q9Y5W5.

Protocols and materials databases

DNASU

11197.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000286574; ENSP00000286574; ENSG00000156076.

GeneID

11197.

KEGG

hsa:11197.

UCSC

uc001ssk.3. human.

Organism-specific databases

CTD

11197.

GeneCards

GC12M065444.

HGNC

HGNC:18081. WIF1.

HPA

HPA039104.

MIM

605186. gene.

neXtProt

NX_Q9Y5W5.

PharmGKB

PA38291.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG328460.

HOVERGEN

HBG017335.

InParanoid

Q9Y5W5.

K01691.

OMA

DKGIMAD.

OrthoDB

EOG4P5K97.

PhylomeDB

Q9Y5W5.

Enzyme and pathway databases

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.
ps1pathway. Presenilin action in Notch and Wnt signaling.

Gene expression databases

ArrayExpress

Q9Y5W5.

Bgee

Q9Y5W5.

CleanEx

HS_WIF1.

Genevestigator

Q9Y5W5.

GermOnline

ENSG00000156076. Homo sapiens.

Family and domain databases

InterPro

IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR003306. WIF.
IPR013309. Wnt-inh.
[Graphical view]

Pfam

PF12661. hEGF. 4 hits.
PF02019. WIF. 1 hit.
[Graphical view]

PRINTS

PR01901. WIFPROTEIN.

ProDom

PD013948. WIF. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00181. EGF. 5 hits.
SM00469. WIF. 1 hit.
[Graphical view]

PROSITE

PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 5 hits.
PS50814. WIF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9Y5W5.

GenomeRNAi

11197.

NextBio

42617.

SOURCE

Search...

Entry information

Entry name

WIF1_HUMAN

Accession

Primary (citable) accession number: Q9Y5W5
Secondary accession number(s): Q6UXI1, Q8WVG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 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.

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents