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Q91VU0 (FAM3C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein FAM3C
Alternative name(s):
Interleukin-like EMT inducer
Gene names
Name:Fam3c
Synonyms:D6Wsu176e, Ilei
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in retinal laminar formation. Promotes epithelial to mesenchymal transition. Ref.6 Ref.7 Ref.8

Subcellular location

Secreted. Cytoplasmic vesicle By similarity Ref.8.

Tissue specificity

Ubiquitously expressed, with highest levels in the retina. Up-regulated in mammary epithelial cells and hepatocytes undergoing epithelial to mesenchymal transition (at protein level). Ref.1 Ref.6 Ref.8

Developmental stage

Expressed at E15.5 in the nonsensory epithelium of the inner ear and at lower levels in the vestibule of the inner ear, the brain and hair follicles. Expressed in the ganglion cell layer of the retina and in the ciliary body at E15.5. At later stages, retinal expression becomes restricted to the ganglion cell layer. Ref.1 Ref.8

Induction

By TGF-beta in epithelial cells. Ref.9

Sequence similarities

Belongs to the FAM3 family.

Ontologies

Keywords
   Cellular componentCytoplasmic vesicle
Secreted
   DiseaseOncogene
   DomainSignal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processmulticellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 227203Protein FAM3C
PRO_0000008753

Amino acid modifications

Disulfide bond58 ↔ 221 Potential
Disulfide bond64 ↔ 86 Potential

Experimental info

Sequence conflict431A → T in AAH55853. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q91VU0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 9195280B92838CF4

FASTA22724,753
        10         20         30         40         50         60 
MRVAGAAKLV VAVAVFLLTF YVISQVFEIK MDASLGNLFA RSALDSAIRS TKPPRYKCGI 

        70         80         90        100        110        120 
SKACPEKHFA FKMASGAANV VGPKICLEDN VLMSGVKNNV GRGINIALVN GKTGEVIDTK 

       130        140        150        160        170        180 
FFDMWGGDVA PFIEFLKTIQ DGTVVLMATY DDGATKLTDE ARRLIAELGS TSITSLGFRD 

       190        200        210        220 
NWVFCGGKGI KTKSPFEQHI KNNKETNKYE GWPEVVEMEG CIPQKQD 

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization and expression analysis of the murine Fam3c gene."
Pilipenko V.V., Reece A., Choo D.I., Greinwald J.H. Jr.
Gene 335:159-168(2004) [PubMed: 15194199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Strain: CD-1.
Tissue: Inner ear.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Embryo.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Strain: Czech II.
Tissue: Mammary tumor.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 73-84, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"ILEI: a cytokine essential for EMT, tumor formation, and late events in metastasis in epithelial cells."
Waerner T., Alacakaptan M., Tamir I., Oberauer R., Gal A., Brabletz T., Schreiber M., Jechlinger M., Beug H.
Cancer Cell 10:227-239(2006) [PubMed: 16959614] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[7]"ILEI requires oncogenic Ras for the epithelial to mesenchymal transition of hepatocytes and liver carcinoma progression."
Lahsnig C., Mikula M., Petz M., Zulehner G., Schneller D., van Zijl F., Huber H., Csiszar A., Beug H., Mikulits W.
Oncogene 28:638-650(2009) [PubMed: 19015638] [Abstract]
Cited for: FUNCTION.
[8]"Secreted factor FAM3C (ILEI) is involved in retinal laminar formation."
Katahira T., Nakagiri S., Terada K., Furukawa T.
Biochem. Biophys. Res. Commun. 392:301-306(2010) [PubMed: 20059962] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[9]"TGF-beta-mediated phosphorylation of hnRNP E1 induces EMT via transcript-selective translational induction of Dab2 and ILEI."
Chaudhury A., Hussey G.S., Ray P.S., Jin G., Fox P.L., Howe P.H.
Nat. Cell Biol. 12:286-293(2010) [PubMed: 20154680] [Abstract]
Cited for: INDUCTION BY TGFB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY424275 mRNA. Translation: AAR84605.1.
AK004059 mRNA. Translation: BAB23146.1.
AK154498 mRNA. Translation: BAE32629.1.
AK170887 mRNA. Translation: BAE42094.1.
CH466533 Genomic DNA. Translation: EDL13845.1.
BC009086 mRNA. Translation: AAH09086.1.
BC055853 mRNA. Translation: AAH55853.1.
IPIIPI00454042.
RefSeqNP_613053.3. NM_138587.4.
UniGeneMm.400193.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ91VU0.

Proteomic databases

PRIDEQ91VU0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000165576; ENSMUSP00000127709; ENSMUSG00000029672.
ENSMUST00000169936; ENSMUSP00000132681; ENSMUSG00000029672.
GeneID27999.
KEGGmmu:27999.
NMPDRfig|10090.3.peg.12994.
UCSCuc009bay.1. mouse.

Organism-specific databases

CTD10447.
MGIMGI:107892. Fam3c.

Phylogenomic databases

GeneTreeENSGT00530000063020.
HOVERGENHBG051544.
InParanoidQ91VU0.
OMAVGPKICV.
OrthoDBEOG43R3NW.

Gene expression databases

ArrayExpressQ91VU0.
BgeeQ91VU0.
GenevestigatorQ91VU0.
GermOnlineENSMUSG00000029672. Mus musculus.

Family and domain databases

ProtoNetSearch...

Other

NextBio306500.
SOURCESearch...

Entry information

Entry nameFAM3C_MOUSE
AccessionPrimary (citable) accession number: Q91VU0
Secondary accession number(s): Q53YY7, Q7TML1, Q9CTB4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: September 21, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families