Q8R507 (FKTN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fukutin
EC=2.-.-.-

Gene names

Name:	Fktn
Synonyms:	Fcmd

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May be a glycosyltransferase which participates in glycosylation of alpha-dystroglycan/DAG1. May interact with and reinforce a large complex encompassing the outside and inside of muscle membranes. Could be involved in brain development. Ref.1 Ref.6
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein Potential Ref.1.
Tissue specificity	According to Ref.1: predominantly detected in brain, liver and kidney. According to Ref.2: detected in all adult tissues examined.
Developmental stage	Wide distribution of expression throughout embryonic development, most predominantly in the central and peripheral nervous systems. High expression in the ventricular zone of proliferating neurons at 13.5 dpc. Broadly expressed in late embryonic and early postnatal cerebellar neurons, including premigratory granule neurons of the external granule cell layer. Expression is maintained in neurons of the internal granule cell layer after migration is complete. Intense expression in Purkinje cells throughout development. A unique pattern of intense expression in irregularly spaced cell bodies that do not appear to correlate with known parasagittal stripes. Expressed in Bergmann glial scaffolds used by granule cells during early posnatal radial migration. Ref.5
Disruption phenotype	Results in embryonic lethality. However, when human FCMD disease-causing retrotransposon is introduced into the mouse fukutin gene, alpha-dystroglycan/DAG1 is hypoglycosylated in muscles as is seen in FCMD (congenital muscular dystrophy Fukuyama) patients. Transfer of normal fukutin gene into these knock-in mice restores glycosylation of alpha-dystroglycan. Ref.6
Sequence similarities	Belongs to the LicD transferase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of JNK cascade Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL neuron migration Non-traceable author statement PubMed 15614444. Source: BHF-UCL regulation of protein glycosylation Non-traceable author statement PubMed 15351499. Source: BHF-UCL
Cellular_component	Golgi apparatus Inferred from direct assay Ref.1. Source: MGI Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cis-Golgi network Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	Fukutin		PRO_0000204722
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 28	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	29 – 461	433	Lumenal Potential
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	38	1	P → L in AAH17538. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8R507 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 1E1E0C5F187FCC39	FASTA	461	53,579
	10 20 30 40 50 60 MSRINKNVVL ALLTLTSSAF LLFQLYYYKH YLSARNGPGS SKSKGNRVGF DSTQWRAVKK 70 80 90 100 110 120 FIMLTSSQNV PVFLIDPWIL ESINKNFEQV KNASQGPASE CRFFCVPRDF TAFALQYHLW 130 140 150 160 170 180 KNEDGWFRIA ENMGFQCLKT ESKDPRLDGI DSLSGTEIPL HYVCKLTTHA IHLVVFHERS 190 200 210 220 230 240 GNYLWHGHLR LKGHMDRKFV PFRKLQFGRY PGAFDRPELQ QVTVDGLDML IPKDPGRFLE 250 260 270 280 290 300 EVPHSRFIEC RYKEARAFLQ QYIDDNTVDA MVFRKRAKEL LQLAAKTLKD LGVPFWLSSG 310 320 330 340 350 360 TCLGWYRQCG IIPYSKDVDL GIFIQDYKPD IILAFQEAGL PLKHKFGKVE DSLELSFQGK 370 380 390 400 410 420 NDVKLDIFFF YEEADHLWNG GTQARTGKKF KYLFPKFTLC WTEFVDIKVH VPCETVDYIE 430 440 450 460 ANYGKTWKIP IKTWDWKSSP PNVQPNGIWP ISEWDEVIQL Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional requirements for fukutin-related protein in the Golgi apparatus." Esapa C.T., Benson M.A., Schroeder J.E., Martin-Rendon E., Brockington M., Brown S.C., Muntoni F., Kroeger S., Blake D.J. Hum. Mol. Genet. 11:3319-3331(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, POSSIBLE FUNCTION. Strain: C57BL/6. Tissue: Brain.
[2]	"Isolation and characterization of the mouse ortholog of the Fukuyama-type congenital muscular dystrophy gene." Horie M., Kobayashi K., Takeda S., Nakamura Y., Lyons G.E., Toda T. Genomics 80:482-486(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[3]	"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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Retina.
[5]	"Expression of dystroglycan, fukutin and POMGnT1 during mouse cerebellar development." Henion T.R., Qu Q., Smith F.I. Brain Res. Mol. Brain Res. 112:177-181(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[6]	"Residual laminin-binding activity and enhanced dystroglycan glycosylation by LARGE in novel model mice to dystroglycanopathy." Kanagawa M., Nishimoto A., Chiyonobu T., Takeda S., Miyagoe-Suzuki Y., Wang F., Fujikake N., Taniguchi M., Lu Z., Tachikawa M., Nagai Y., Tashiro F., Miyazaki J., Tajima Y., Takeda S., Endo T., Kobayashi K., Campbell K.P., Toda T. Hum. Mol. Genet. 18:621-631(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ511807 mRNA. Translation: CAD54302.1. AB077383 mRNA. Translation: BAB87769.1. AK085931 mRNA. Translation: BAC39572.1. BC017538 mRNA. Translation: AAH17538.1.
IPI	IPI00153914.
RefSeq	NP_647470.1. NM_139309.4.
UniGene	Mm.247210.
3D structure databases
ProteinModelPortal	Q8R507.
ModBase	Search...
PTM databases
PhosphoSite	Q8R507.
Proteomic databases
PRIDE	Q8R507.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000061771; ENSMUSP00000061489; ENSMUSG00000028414. ENSMUST00000128667; ENSMUSP00000114699; ENSMUSG00000028414.
GeneID	246179.
KEGG	mmu:246179.
Organism-specific databases
CTD	2218.
MGI	MGI:2179507. Fktn.
Phylogenomic databases
eggNOG	NOG83383.
GeneTree	ENSGT00390000014471.
HOGENOM	HOG000231657.
HOVERGEN	HBG005068.
InParanoid	Q8R507.
OMA	FQLYYYK.
OrthoDB	EOG4X97H4.
Gene expression databases
ArrayExpress	Q8R507.
Bgee	Q8R507.
CleanEx	MM_FKTN.
Genevestigator	Q8R507.
GermOnline	ENSMUSG00000028414. Mus musculus.
Family and domain databases
InterPro	IPR009644. Fukutin-related. IPR007074. LicD. [Graphical view]
PANTHER	PTHR15407. PTHR15407. 1 hit.
Pfam	PF04991. LicD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FKTN. mouse.
NextBio	387143.
SOURCE	Search...

Entry information

Entry name

FKTN_MOUSE

Accession

Primary (citable) accession number: Q8R507
Secondary accession number(s): Q8VD64

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2002
Last modified:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program