MFRP_MOUSE
ID MFRP_MOUSE Reviewed; 584 AA.
AC Q8K480; Q8BPP4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Membrane frizzled-related protein;
DE AltName: Full=Membrane-type frizzled-related protein;
GN Name=Mfrp;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND INVOLVEMENT
RP IN RD6.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=12140190; DOI=10.1093/hmg/11.16.1879;
RA Kameya S., Hawes N.L., Chang B., Heckenlively J.R., Naggert J.K.,
RA Nishina P.M.;
RT "Mfrp, a gene encoding a frizzled related protein, is mutated in the mouse
RT retinal degeneration 6.";
RL Hum. Mol. Genet. 11:1879-1886(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH C1QTNF5.
RX PubMed=17122143; DOI=10.1167/iovs.06-0449;
RA Mandal M.N., Vasireddy V., Jablonski M.M., Wang X., Heckenlively J.R.,
RA Hughes B.A., Reddy G.B., Ayyagari R.;
RT "Spatial and temporal expression of MFRP and its interaction with CTRP5.";
RL Invest. Ophthalmol. Vis. Sci. 47:5514-5521(2006).
CC -!- FUNCTION: May play a role in eye development.
CC -!- SUBUNIT: Interacts with C1QTNF5. {ECO:0000269|PubMed:17122143}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:17122143}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:17122143}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K480-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K480-2; Sequence=VSP_017664;
CC -!- TISSUE SPECIFICITY: Expressed in retinal pigment epithelium and ciliary
CC epithelium of the eye. {ECO:0000269|PubMed:12140190,
CC ECO:0000269|PubMed:17122143}.
CC -!- DISEASE: Note=Defects in Mfrp are the cause of retinal degeneration 6
CC (RD6). RD6 is an autosomal recessive degeneration of the photoreceptors
CC causing dysfunction of both rods and cones.
CC {ECO:0000269|PubMed:12140190}.
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DR EMBL; AF469650; AAM89216.1; -; mRNA.
DR EMBL; AK053629; BAC35452.1; -; mRNA.
DR CCDS; CCDS40597.1; -. [Q8K480-1]
DR CCDS; CCDS52776.1; -. [Q8K480-2]
DR RefSeq; NP_001177242.1; NM_001190313.1.
DR RefSeq; NP_001177243.1; NM_001190314.1. [Q8K480-2]
DR RefSeq; NP_663588.2; NM_145613.4.
DR RefSeq; NP_667337.1; NM_147126.3. [Q8K480-1]
DR AlphaFoldDB; Q8K480; -.
DR SMR; Q8K480; -.
DR STRING; 10090.ENSMUSP00000034654; -.
DR GlyGen; Q8K480; 3 sites.
DR iPTMnet; Q8K480; -.
DR PhosphoSitePlus; Q8K480; -.
DR PaxDb; Q8K480; -.
DR PeptideAtlas; Q8K480; -.
DR PRIDE; Q8K480; -.
DR ProteomicsDB; 293462; -. [Q8K480-1]
DR ProteomicsDB; 293463; -. [Q8K480-2]
DR Antibodypedia; 32688; 110 antibodies from 19 providers.
DR DNASU; 259172; -.
DR Ensembl; ENSMUST00000034654; ENSMUSP00000034654; ENSMUSG00000034739. [Q8K480-1]
DR Ensembl; ENSMUST00000161381; ENSMUSP00000124456; ENSMUSG00000034739. [Q8K480-2]
DR GeneID; 235312; -.
DR GeneID; 259172; -.
DR KEGG; mmu:259172; -.
DR UCSC; uc009pbr.2; mouse. [Q8K480-1]
DR UCSC; uc012grq.1; mouse. [Q8K480-2]
DR CTD; 114902; -.
DR CTD; 83552; -.
DR MGI; MGI:2385957; Mfrp.
DR VEuPathDB; HostDB:ENSMUSG00000034739; -.
DR eggNOG; KOG3577; Eukaryota.
DR eggNOG; KOG4292; Eukaryota.
DR GeneTree; ENSGT00940000154525; -.
DR HOGENOM; CLU_032137_0_0_1; -.
DR InParanoid; Q8K480; -.
DR OMA; ENPCGPR; -.
DR OrthoDB; 490520at2759; -.
DR PhylomeDB; Q8K480; -.
DR TreeFam; TF316506; -.
DR BioGRID-ORCS; 235312; 1 hit in 39 CRISPR screens.
DR BioGRID-ORCS; 259172; 4 hits in 74 CRISPR screens.
DR ChiTaRS; C1qtnf5; mouse.
DR PRO; PR:Q8K480; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K480; protein.
DR Bgee; ENSMUSG00000034739; Expressed in secondary oocyte and 38 other tissues.
DR ExpressionAtlas; Q8K480; baseline and differential.
DR Genevisible; Q8K480; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF57424; SSF57424; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..584
FT /note="Membrane frizzled-related protein"
FT /id="PRO_0000228133"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 150..259
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 265..301
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 307..420
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 426..460
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 466..584
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 108..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..176
FT /evidence="ECO:0000250"
FT DISULFID 203..222
FT /evidence="ECO:0000250"
FT DISULFID 266..278
FT /evidence="ECO:0000250"
FT DISULFID 273..291
FT /evidence="ECO:0000250"
FT DISULFID 285..300
FT /evidence="ECO:0000250"
FT DISULFID 307..333
FT /evidence="ECO:0000250"
FT DISULFID 360..383
FT /evidence="ECO:0000250"
FT DISULFID 433..451
FT /evidence="ECO:0000250"
FT DISULFID 445..459
FT /evidence="ECO:0000250"
FT DISULFID 471..533
FT /evidence="ECO:0000250"
FT DISULFID 479..526
FT /evidence="ECO:0000250"
FT DISULFID 517..554
FT /evidence="ECO:0000250"
FT DISULFID 543..581
FT /evidence="ECO:0000250"
FT DISULFID 547..569
FT /evidence="ECO:0000250"
FT VAR_SEQ 425..431
FT /note="SGCPWAE -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017664"
FT CONFLICT 98
FT /note="P -> H (in Ref. 2; BAC35452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 584 AA; 63669 MW; 0CF6A6403107E16C CRC64;
MKDYDDVILR PEASELSKTE FCNPAFDPEA GPSCPPPALQ RDVGSRLQAP WHAQRLRGLQ
PDCHFSWFCI LLLSGLLLLL LGLLVAVILA QLQATSLPRT TKNPLLTRGL TPMGVIPSTT
PNTTTTTTTT TPARTGQQEA AMSPTHQTTC GGLLPGPSGF FSSPNYPDLY PPLSHCVWHI
QVAAGQTIQL KIQALSIESM LTCLFDRLEI ISEPTGPLLR VCGKTPPATL NTNTSHLRVS
FVSDNDVEGS GFQAWYQAVA PGHWSCAHNE FHCDLLLCLK RDSVCDGITE CADGSDEANC
SAKTLGCGGN LTGLYGVFST PNYPQHYPHQ QLCTWYIEVP VGYGIRLEFH NFSLEAQAEC
KFDYVEVYEA SNLGTFSFLG RFCGAEPPLN VVSSMHQLAV IFKTDLGISS GGFLATYQAI
NTTESGCPWA EFCQSGGYRD LQWMCDLWKD CANDSNDNCS SHLSPQPDLT CEPVQVEMCL
GLSYNTTAFP NIWVGLATQT EVTDILRGYK SLTSLPCYQT FQRFLCGLLV PRCTSLGTIL
PPCRSVCQAA EQQCQSSLAL LGTPWPFNCN RLPVAASLEA CSQP
