Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fukutin-related protein

Gene

Fkrp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transferase involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity.By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.By similarity
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • glycoprotein biosynthetic process Source: MGI
  • protein O-linked mannosylation Source: UniProtKB
  • protein processing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Fukutin-related protein (EC:2.-.-.-)
Gene namesi
Name:Fkrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2447586. Fkrp.

Subcellular locationi

  • Golgi apparatus membrane By similarity; Single-pass type II membrane protein By similarity
  • Secreted
  • Cell membranesarcolemma
  • Rough endoplasmic reticulum By similarity

  • Note: According to PubMed:19900540 the N-terminal hydrophobic domain is cleaved after translocation to the Golgi apparatus and the protein is secreted. Localization at the cell membrane may require the presence of dystroglycan. At the Golgi apparatus localizes to the middle-to-trans-cisternae. Detected in rough endoplasmic reticulum in myocytes.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2923HelicalSequence analysisAdd
BLAST
Topological domaini30 – 494465LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • rough endoplasmic reticulum Source: MGI
  • sarcolemma Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality before E12.5.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 54RLTR → ELTE: Localized to the perinuclear region but not retained in or targeted to the medial part of the Golgi apparatus. 1 Publication
Mutagenesisi276 – 2761L → I: Reduced secretion to the medium; localizes mainly to the Golgi apparatus. Mild dystrophy with reduced alpha-dystroglycan glycosylation and no apparent brain defects. 3 Publications
Mutagenesisi318 – 3181C → Y: Reduced secretion to the medium. 1 Publication
Mutagenesisi362 – 3643DVD → NNN: Does not alter dystroglycan processing in vitro. 1 Publication
Mutagenesisi405 – 4051V → L: Localizes mainly to the ER compartment. 1 Publication
Mutagenesisi448 – 4481P → L: Not properly targeted to the Golgi apparatus; strongly reduced secretion to the medium; localizes mainly to the ER compartment. Strongly impaired glycosylation of alpha-dystroglycan in muscles and brain. 5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Fukutin-related proteinPRO_0000204724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 – 6Interchain
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8CG64.
PaxDbiQ8CG64.
PRIDEiQ8CG64.

PTM databases

PhosphoSiteiQ8CG64.

Expressioni

Tissue specificityi

Expressed at highest levels in brain, lung, heart, kidney and liver.

Gene expression databases

BgeeiQ8CG64.
CleanExiMM_FKRP.
GenevisibleiQ8CG64. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Exists also as large multimeric protein complexes (By similarity). May interact with the dystrophin-glycoprotein complex (DGC).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059091.

Structurei

3D structure databases

ProteinModelPortaliQ8CG64.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LicD transferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFID. Eukaryota.
ENOG410XP2R. LUCA.
GeneTreeiENSGT00390000017583.
HOGENOMiHOG000007172.
HOVERGENiHBG048950.
InParanoidiQ8CG64.
KOiK19873.
OMAiTAHARWK.
OrthoDBiEOG7WT40X.
PhylomeDBiQ8CG64.
TreeFamiTF324064.

Family and domain databases

InterProiIPR007074. LicD_fam.
[Graphical view]
PfamiPF04991. LicD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CG64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLTRCWAAL AAAIILNLLV FFYVSWLQHQ PRNSRARGPR RTSAIGPRVT
60 70 80 90 100
VLIREFEAFD NAVPELVDSF LQQDPAQPVV VAADTLPYPP LALPRIPNVR
110 120 130 140 150
LALLQPALDR PAAASRPETY VATEFVALVP DGARAESPGH LERMVEALRG
160 170 180 190 200
SSARLVAAPV ATANPARCLA LNVSLREWTA RYDPAPSAPR CDALDGDAVL
210 220 230 240 250
LMRSRDLFNL SVPLARPLAT SLFLQTALRG WAVQLLDLTF AAARQPPLAT
260 270 280 290 300
AHARWKAERE GRSRRAALLR SLGIRLVSWE GGRLEWFGCS KESARCFGTV
310 320 330 340 350
AGDTPAYLYE GRWTPPCCLR ALRETARYVV GVLEAAGVRY WLEGGSLLGA
360 370 380 390 400
ARHGDIIPWD YDVDLGIYLE DVGNCEQLRG AEAGSVVDER GFVWEKAVEG
410 420 430 440 450
DFFRVQYSEN NHLHVDLWPF YPRNGVMTKD TWLDHRQDVE FPEHFLQPLV
460 470 480 490
PLPFAGFMAQ APNNYRRFLE LKFGPGVIEN PEYPNPALLS LTGG
Length:494
Mass (Da):54,852
Last modified:March 1, 2003 - v1
Checksum:i470499DDEA7CB73F
GO

Sequence cautioni

The sequence BAC37963.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431A → E in BAC37963 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ511806 mRNA. Translation: CAD54301.1.
BC053072 mRNA. Translation: AAH53072.1.
AK080624 mRNA. Translation: BAC37963.1. Different initiation.
CCDSiCCDS20853.1.
RefSeqiNP_775606.1. NM_173430.2.
XP_006539991.1. XM_006539928.2.
XP_006539992.1. XM_006539929.2.
XP_006539993.1. XM_006539930.2.
XP_011248864.1. XM_011250562.1.
UniGeneiMm.39703.

Genome annotation databases

EnsembliENSMUST00000061390; ENSMUSP00000059091; ENSMUSG00000048920.
GeneIDi243853.
KEGGimmu:243853.
UCSCiuc009fic.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ511806 mRNA. Translation: CAD54301.1.
BC053072 mRNA. Translation: AAH53072.1.
AK080624 mRNA. Translation: BAC37963.1. Different initiation.
CCDSiCCDS20853.1.
RefSeqiNP_775606.1. NM_173430.2.
XP_006539991.1. XM_006539928.2.
XP_006539992.1. XM_006539929.2.
XP_006539993.1. XM_006539930.2.
XP_011248864.1. XM_011250562.1.
UniGeneiMm.39703.

3D structure databases

ProteinModelPortaliQ8CG64.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059091.

PTM databases

PhosphoSiteiQ8CG64.

Proteomic databases

MaxQBiQ8CG64.
PaxDbiQ8CG64.
PRIDEiQ8CG64.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061390; ENSMUSP00000059091; ENSMUSG00000048920.
GeneIDi243853.
KEGGimmu:243853.
UCSCiuc009fic.1. mouse.

Organism-specific databases

CTDi79147.
MGIiMGI:2447586. Fkrp.

Phylogenomic databases

eggNOGiENOG410IFID. Eukaryota.
ENOG410XP2R. LUCA.
GeneTreeiENSGT00390000017583.
HOGENOMiHOG000007172.
HOVERGENiHBG048950.
InParanoidiQ8CG64.
KOiK19873.
OMAiTAHARWK.
OrthoDBiEOG7WT40X.
PhylomeDBiQ8CG64.
TreeFamiTF324064.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

ChiTaRSiFkrp. mouse.
PROiQ8CG64.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CG64.
CleanExiMM_FKRP.
GenevisibleiQ8CG64. MM.

Family and domain databases

InterProiIPR007074. LicD_fam.
[Graphical view]
PfamiPF04991. LicD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, MUTAGENESIS OF 2-ARG--ARG-5; 362-ASP--ASP-364 AND PRO-448, POSSIBLE FUNCTION.
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain cortex.
  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] OF 63-494.
    Strain: C57BL/6J.
    Tissue: Brain cortex.
  4. "Fukutin-related protein associates with the sarcolemmal dystrophin-glycoprotein complex."
    Beedle A.M., Nienaber P.M., Campbell K.P.
    J. Biol. Chem. 282:16713-16717(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DGC COMPLEX.
  5. "Fukutin-related protein localizes to the Golgi apparatus and mutations lead to mislocalization in muscle in vivo."
    Keramaris-Vrantsis E., Lu P.J., Doran T., Zillmer A., Ashar J., Esapa C.T., Benson M.A., Blake D.J., Rosenfeld J., Lu Q.L.
    Muscle Nerve 36:455-465(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-276; VAL-405 AND PRO-448.
  6. Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-276; CYS-318 AND PRO-448.
  7. "Fukutin-related protein is essential for mouse muscle, brain and eye development and mutation recapitulates the wide clinical spectrums of dystroglycanopathies."
    Chan Y.M., Keramaris-Vrantsis E., Lidov H.G., Norton J.H., Zinchenko N., Gruber H.E., Thresher R., Blake D.J., Ashar J., Rosenfeld J., Lu Q.L.
    Hum. Mol. Genet. 19:3995-4006(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-448.
  8. "Mouse models of fukutin-related protein mutations show a wide range of disease phenotypes."
    Blaeser A., Keramaris E., Chan Y.M., Sparks S., Cowley D., Xiao X., Lu Q.L.
    Hum. Genet. 132:923-934(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-276 AND PRO-448.

Entry informationi

Entry nameiFKRP_MOUSE
AccessioniPrimary (citable) accession number: Q8CG64
Secondary accession number(s): Q8BJR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.