Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BY79 (MFRP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Membrane frizzled-related protein
Alternative name(s):
Membrane-type frizzled-related protein
Gene names
Name:MFRP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in eye development. Ref.8

Subcellular location

Membrane; Single-pass type II membrane protein Potential.

Tissue specificity

Specifically expressed in brain. Strongly expressed in medulla oblongata and to a lower extent in hippocampus and corpus callosum. Expressed in keratinocytes. Ref.1 Ref.6

Developmental stage

Expressed in fetal brain. Ref.1

Involvement in disease

Nanophthalmos 2 (NNO2) [MIM:609549]: Rare autosomal recessive disorder of eye development characterized by extreme hyperopia and small functional eyes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Microphthalmia, isolated, 5 (MCOP5) [MIM:611040]: A disorder characterized by posterior microphthalmia, retinitis pigmentosa, foveoschisis and optic disk drusen. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Miscellaneous

This protein is produced by a bicistronic gene which also produces the C1QTNF5 protein from a non-overlapping reading frame.

Sequence similarities

Contains 2 CUB domains.

Contains 1 FZ (frizzled) domain.

Contains 2 LDL-receptor class A domains.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BY79-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BY79-2)

The sequence of this isoform differs from the canonical sequence as follows:
     259-259: S → D

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Membrane frizzled-related protein
PRO_0000228132

Regions

Topological domain1 – 6969Cytoplasmic Potential
Transmembrane70 – 9021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain91 – 579489Extracellular Potential
Domain144 – 253110CUB 1
Domain259 – 29537LDL-receptor class A 1
Domain301 – 414114CUB 2
Domain420 – 45536LDL-receptor class A 2
Domain461 – 579119FZ
Compositional bias111 – 12111Poly-Thr

Amino acid modifications

Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation4151N-linked (GlcNAc...) Potential
Disulfide bond144 ↔ 170 By similarity
Disulfide bond197 ↔ 216 By similarity
Disulfide bond260 ↔ 272 By similarity
Disulfide bond267 ↔ 285 By similarity
Disulfide bond279 ↔ 294 By similarity
Disulfide bond301 ↔ 327 By similarity
Disulfide bond354 ↔ 377 By similarity
Disulfide bond421 ↔ 433 By similarity
Disulfide bond428 ↔ 446 By similarity
Disulfide bond440 ↔ 454 By similarity
Disulfide bond466 ↔ 528 By similarity
Disulfide bond474 ↔ 521 By similarity
Disulfide bond512 ↔ 549 By similarity
Disulfide bond538 ↔ 576 By similarity
Disulfide bond542 ↔ 564 By similarity

Natural variations

Alternative sequence2591S → D in isoform 2.
VSP_046546
Natural variant541R → G. Ref.7
Corresponds to variant rs139436396 [ dbSNP | Ensembl ].
VAR_025691
Natural variant1191I → V. Ref.7
Corresponds to variant rs4639950 [ dbSNP | Ensembl ].
VAR_025692
Natural variant1361V → M. Ref.2 Ref.7
Corresponds to variant rs3814762 [ dbSNP | Ensembl ].
VAR_025693
Natural variant1821I → T in NNO2. Ref.8
VAR_025694
Natural variant4491G → S. Ref.7
VAR_025695
Natural variant5141Q → H. Ref.7
VAR_025696

Experimental info

Sequence conflict401P → Q in CAH93521. Ref.2
Sequence conflict831Missing in CAH93521. Ref.2
Sequence conflict3931A → S in BAB70859. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8E5F8D3A1C4BB074

FASTA57962,212
        10         20         30         40         50         60 
MKDFSDVILC MEATESSKTE FCNPAFEPES GPPCPPPVFP EDASYSVPAP WHGRRPRGLR 

        70         80         90        100        110        120 
PDCRFSWLCV LLLSSLLLLL LGLLVAIILA QLQAAPPSGA SHSPLPAGGL TTTTTTPTIT 

       130        140        150        160        170        180 
TSQAAGTPKG QQESGVSPSP QSTCGGLLSG PRGFFSSPNY PDPYPPNTHC VWHIQVATDH 

       190        200        210        220        230        240 
AIQLKIEALS IESVASCLFD RLELSPEPEG PLLRVCGRVP PPTLNTNASH LLVVFVSDSS 

       250        260        270        280        290        300 
VEGFGFHAWY QAMAPGRGSC AHDEFRCDQL ICLLPDSVCD GFANCADGSD ETNCSAKFSG 

       310        320        330        340        350        360 
CGGNLTGLQG TFSTPSYLQQ YPHQLLCTWH ISVPAGHSIE LQFHNFSLEA QDECKFDYVE 

       370        380        390        400        410        420 
VYETSSSGAF SLLGRFCGAE PPPHLVSSHH ELAVLFRTDH GISSGGFSAT YLAFNATENP 

       430        440        450        460        470        480 
CGPSELSCQA GGCKGVQWMC DMWRDCTDGS DDNCSGPLFP PPELACEPVQ VEMCLGLSYN 

       490        500        510        520        530        540 
TTAFPNIWVG MITQEEVVEV LSGYKSLTSL PCYQHFRRLL CGLLVPRCTP LGSVLPPCRS 

       550        560        570 
VCQEAEHQCQ SGLALLGTPW PFNCNRLPEA ADLEACAQP 

« Hide

Isoform 2 [UniParc].

Checksum: 4F932A6DB12A7B79
Show »

FASTA57962,240

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of MFRP, a novel gene encoding a membrane-type frizzled-related protein."
Katoh M.
Biochem. Biophys. Res. Commun. 282:116-123(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"Sequencing arrays for screening multiple genes associated with early-onset human retinal degenerations on a high-throughput platform."
Mandal M.N.A., Heckenlively J.R., Burch T., Chen L., Vasireddy V., Koenekoop R.K., Sieving P.A., Ayyagari R.
Invest. Ophthalmol. Vis. Sci. 46:3355-3362(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-136.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Bone morphogenetic protein-2 modulates Wnt and frizzled expression and enhances the canonical pathway of Wnt signaling in normal keratinocytes."
Yang L., Yamasaki K., Shirakata Y., Dai X., Tokumaru S., Yahata Y., Tohyama M., Hanakawa Y., Sayama K., Hashimoto K.
J. Dermatol. Sci. 42:111-119(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Mutation screen of the membrane-type frizzled-related protein (MFRP) gene in patients with inherited retinal degenerations."
Pauer G.J.T., Xi Q., Zhang K., Traboulsi E.I., Hagstrom S.A.
Ophthalmic Genet. 26:157-161(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLY-54; VAL-119; MET-136; SER-449 AND HIS-514.
[8]"Extreme hyperopia is the result of null mutations in MFRP, which encodes a frizzled-related protein."
Sundin O.H., Leppert G.S., Silva E.D., Yang J.-M., Dharmaraj S., Maumenee I.H., Santos L.C., Parsa C.F., Traboulsi E.I., Broman K.W., Dibernardo C., Sunness J.S., Toy J., Weinberg E.M.
Proc. Natl. Acad. Sci. U.S.A. 102:9553-9558(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NNO2 THR-182, FUNCTION.
[9]"A new autosomal recessive syndrome consisting of posterior microphthalmos, retinitis pigmentosa, foveoschisis, and optic disc drusen is caused by a MFRP gene mutation."
Ayala-Ramirez R., Graue-Wiechers F., Robredo V., Amato-Almanza M., Horta-Diez I., Zenteno J.C.
Mol. Vis. 12:1483-1489(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MCOP5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB055505 mRNA. Translation: BAB39771.1.
AJ862823 mRNA. Translation: CAH93521.1.
AK055132 mRNA. Translation: BAB70859.1.
EF444994 Genomic DNA. Translation: ACA06013.1.
EF444994 Genomic DNA. Translation: ACA06015.1.
CH471065 Genomic DNA. Translation: EAW67483.1.
PIRJC7629.
RefSeqNP_113621.1. NM_031433.3.
UniGeneHs.632102.

3D structure databases

ProteinModelPortalQ9BY79.
SMRQ9BY79. Positions 127-455, 463-572.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123684. 1 interaction.
125392. 1 interaction.
STRING9606.ENSP00000391664.

Polymorphism databases

DMDM74717666.

Proteomic databases

PaxDbQ9BY79.
PRIDEQ9BY79.

Protocols and materials databases

DNASU83552.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000449574; ENSP00000391664; ENSG00000235718. [Q9BY79-1]
ENST00000555262; ENSP00000450509; ENSG00000235718. [Q9BY79-1]
GeneID83552.
KEGGhsa:83552.
UCSCuc001pwj.2. human. [Q9BY79-1]

Organism-specific databases

CTD83552.
GeneCardsGC11M119244.
HGNCHGNC:18121. MFRP.
HPAHPA042946.
MIM606227. gene.
609549. phenotype.
611040. phenotype.
neXtProtNX_Q9BY79.
Orphanet251279. Microphthalmia - retinitis pigmentosa - foveoschisis - optic disc drusen.
35612. Nanophthalmia.
PharmGKBPA30776.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG261421.
HOGENOMHOG000048709.
HOVERGENHBG081968.
InParanoidQ9BY79.
OMAGLEACAQ.
OrthoDBEOG7S4X5R.
PhylomeDBQ9BY79.
TreeFamTF316506.

Gene expression databases

CleanExHS_MFRP.
GenevestigatorQ9BY79.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
2.60.120.290. 2 hits.
4.10.400.10. 2 hits.
InterProIPR000859. CUB_dom.
IPR020067. Frizzled_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamPF00431. CUB. 2 hits.
PF01392. Fz. 1 hit.
PF00057. Ldl_recept_a. 1 hit.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00042. CUB. 2 hits.
SM00192. LDLa. 2 hits.
[Graphical view]
SUPFAMSSF49854. SSF49854. 2 hits.
SSF57424. SSF57424. 2 hits.
SSF63501. SSF63501. 1 hit.
PROSITEPS01180. CUB. 2 hits.
PS50038. FZ. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi83552.
NextBio35466294.
PROQ9BY79.
SOURCESearch...

Entry information

Entry nameMFRP_HUMAN
AccessionPrimary (citable) accession number: Q9BY79
Secondary accession number(s): B0YJ36 expand/collapse secondary AC list , B0YJ37, Q335M3, Q96DQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM