FAM3C_MOUSE
ID FAM3C_MOUSE Reviewed; 227 AA.
AC Q91VU0; Q53YY7; Q7TML1; Q9CTB4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein FAM3C;
DE AltName: Full=Interleukin-like EMT inducer;
DE Flags: Precursor;
GN Name=Fam3c; Synonyms=D6Wsu176e, Ilei;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Inner ear;
RX PubMed=15194199; DOI=10.1016/j.gene.2004.03.026;
RA Pilipenko V.V., Reece A., Choo D.I., Greinwald J.H. Jr.;
RT "Genomic organization and expression analysis of the murine Fam3c gene.";
RL Gene 335:159-168(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 73-84, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16959614; DOI=10.1016/j.ccr.2006.07.020;
RA Waerner T., Alacakaptan M., Tamir I., Oberauer R., Gal A., Brabletz T.,
RA Schreiber M., Jechlinger M., Beug H.;
RT "ILEI: a cytokine essential for EMT, tumor formation, and late events in
RT metastasis in epithelial cells.";
RL Cancer Cell 10:227-239(2006).
RN [7]
RP FUNCTION.
RX PubMed=19015638; DOI=10.1038/onc.2008.418;
RA Lahsnig C., Mikula M., Petz M., Zulehner G., Schneller D., van Zijl F.,
RA Huber H., Csiszar A., Beug H., Mikulits W.;
RT "ILEI requires oncogenic Ras for the epithelial to mesenchymal transition
RT of hepatocytes and liver carcinoma progression.";
RL Oncogene 28:638-650(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=20059962; DOI=10.1016/j.bbrc.2009.12.180;
RA Katahira T., Nakagiri S., Terada K., Furukawa T.;
RT "Secreted factor FAM3C (ILEI) is involved in retinal laminar formation.";
RL Biochem. Biophys. Res. Commun. 392:301-306(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INDUCTION BY TGFB.
RX PubMed=20154680; DOI=10.1038/ncb2029;
RA Chaudhury A., Hussey G.S., Ray P.S., Jin G., Fox P.L., Howe P.H.;
RT "TGF-beta-mediated phosphorylation of hnRNP E1 induces EMT via transcript-
RT selective translational induction of Dab2 and ILEI.";
RL Nat. Cell Biol. 12:286-293(2010).
CC -!- FUNCTION: May be involved in retinal laminar formation. Promotes
CC epithelial to mesenchymal transition. {ECO:0000269|PubMed:16959614,
CC ECO:0000269|PubMed:19015638, ECO:0000269|PubMed:20059962}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20059962}.
CC Cytoplasmic vesicle {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in the
CC retina. Up-regulated in mammary epithelial cells and hepatocytes
CC undergoing epithelial to mesenchymal transition (at protein level).
CC {ECO:0000269|PubMed:15194199, ECO:0000269|PubMed:16959614,
CC ECO:0000269|PubMed:20059962}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 15.5 dpc in the nonsensory epithelium
CC of the inner ear and at lower levels in the vestibule of the inner ear,
CC the brain and hair follicles. Expressed in the ganglion cell layer of
CC the retina and in the ciliary body at 15.5 dpc. At later stages,
CC retinal expression becomes restricted to the ganglion cell layer.
CC {ECO:0000269|PubMed:15194199, ECO:0000269|PubMed:20059962}.
CC -!- INDUCTION: By TGF-beta in epithelial cells.
CC {ECO:0000269|PubMed:20154680}.
CC -!- SIMILARITY: Belongs to the FAM3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY424275; AAR84605.1; -; mRNA.
DR EMBL; AK004059; BAB23146.1; -; mRNA.
DR EMBL; AK154498; BAE32629.1; -; mRNA.
DR EMBL; AK170887; BAE42094.1; -; mRNA.
DR EMBL; CH466533; EDL13845.1; -; Genomic_DNA.
DR EMBL; BC009086; AAH09086.1; -; mRNA.
DR EMBL; BC055853; AAH55853.1; -; mRNA.
DR CCDS; CCDS39436.1; -.
DR RefSeq; NP_613053.3; NM_138587.4.
DR RefSeq; XP_006505165.1; XM_006505102.3.
DR RefSeq; XP_006505166.1; XM_006505103.3.
DR PDB; 5LC3; X-ray; 2.00 A; A/B=55-227.
DR PDB; 5LC4; X-ray; 1.84 A; A/B/C/D=55-227.
DR PDBsum; 5LC3; -.
DR PDBsum; 5LC4; -.
DR AlphaFoldDB; Q91VU0; -.
DR SMR; Q91VU0; -.
DR BioGRID; 205708; 2.
DR STRING; 10090.ENSMUSP00000127709; -.
DR PhosphoSitePlus; Q91VU0; -.
DR CPTAC; non-CPTAC-3980; -.
DR EPD; Q91VU0; -.
DR MaxQB; Q91VU0; -.
DR PaxDb; Q91VU0; -.
DR PRIDE; Q91VU0; -.
DR ProteomicsDB; 275587; -.
DR TopDownProteomics; Q91VU0; -.
DR Antibodypedia; 31703; 284 antibodies from 34 providers.
DR DNASU; 27999; -.
DR Ensembl; ENSMUST00000165576; ENSMUSP00000127709; ENSMUSG00000029672.
DR GeneID; 27999; -.
DR KEGG; mmu:27999; -.
DR UCSC; uc009bay.1; mouse.
DR CTD; 10447; -.
DR MGI; MGI:107892; Fam3c.
DR VEuPathDB; HostDB:ENSMUSG00000029672; -.
DR eggNOG; ENOG502QQR8; Eukaryota.
DR GeneTree; ENSGT00950000183004; -.
DR InParanoid; Q91VU0; -.
DR OrthoDB; 1295040at2759; -.
DR PhylomeDB; Q91VU0; -.
DR TreeFam; TF353414; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 27999; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Fam3c; mouse.
DR PRO; PR:Q91VU0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91VU0; protein.
DR Bgee; ENSMUSG00000029672; Expressed in retinal neural layer and 255 other tissues.
DR ExpressionAtlas; Q91VU0; baseline and differential.
DR Genevisible; Q91VU0; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:InterPro.
DR CDD; cd13940; ILEI_FAM3C; 1.
DR InterPro; IPR039220; FAM3.
DR InterPro; IPR039219; FAM3C.
DR InterPro; IPR039477; ILEI/PANDER_dom.
DR InterPro; IPR039475; ILEI_FAM3C.
DR PANTHER; PTHR14592; PTHR14592; 1.
DR PANTHER; PTHR14592:SF10; PTHR14592:SF10; 1.
DR Pfam; PF15711; ILEI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Developmental protein;
KW Direct protein sequencing; Disulfide bond; Oncogene; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..227
FT /note="Protein FAM3C"
FT /id="PRO_0000008753"
FT DISULFID 58..86
FT /evidence="ECO:0000250"
FT DISULFID 64..221
FT /evidence="ECO:0000250"
FT CONFLICT 43
FT /note="A -> T (in Ref. 4; AAH55853)"
FT /evidence="ECO:0000305"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:5LC4"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:5LC4"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:5LC4"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:5LC4"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5LC4"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:5LC4"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:5LC4"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:5LC4"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:5LC4"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:5LC4"
SQ SEQUENCE 227 AA; 24753 MW; 9195280B92838CF4 CRC64;
MRVAGAAKLV VAVAVFLLTF YVISQVFEIK MDASLGNLFA RSALDSAIRS TKPPRYKCGI
SKACPEKHFA FKMASGAANV VGPKICLEDN VLMSGVKNNV GRGINIALVN GKTGEVIDTK
FFDMWGGDVA PFIEFLKTIQ DGTVVLMATY DDGATKLTDE ARRLIAELGS TSITSLGFRD
NWVFCGGKGI KTKSPFEQHI KNNKETNKYE GWPEVVEMEG CIPQKQD
