EGFLA_MOUSE
ID EGFLA_MOUSE Reviewed; 1017 AA.
AC Q4VBE4; B2RWU6; B6JU28; Q80WX4; Q8BGP3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Pikachurin;
DE AltName: Full=EGF-like, fibronectin type-III and laminin G-like domain-containing protein;
DE AltName: Full=Nectican;
DE Flags: Precursor;
GN Name=Egflam;
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), FUNCTION, INTERACTION WITH DAG1
RP ALPHA-DYSTROGLYCAN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=18641643; DOI=10.1038/nn.2160;
RA Sato S., Omori Y., Katoh K., Kondo M., Kanagawa M., Miyata K., Funabiki K.,
RA Koyasu T., Kajimura N., Miyoshi T., Sawai H., Kobayashi K., Tani A.,
RA Toda T., Usukura J., Tano Y., Fujikado T., Furukawa T.;
RT "Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon
RT synapse formation.";
RL Nat. Neurosci. 11:923-931(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Forelimb, Skin, Testis, and Thymus;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Eye, and Olfactory epithelium;
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 FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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).
CC -!- FUNCTION: Involved in both the retinal photoreceptor ribbon synapse
CC formation and physiological functions of visual perception. Necessary
CC for proper bipolar dendritic tip apposition to the photoreceptor ribbon
CC synapse. Promotes matrix assembly and cell adhesiveness.
CC {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:18757743}.
CC -!- SUBUNIT: Interacts with DAG1 alpha-dystroglycan.
CC {ECO:0000269|PubMed:18641643}.
CC -!- INTERACTION:
CC Q4VBE4; PRO_0000021067 [Q62165]: Dag1; NbExp=2; IntAct=EBI-2025048, EBI-2025154;
CC Q4VBE4; Q6PRD1: GPR179; Xeno; NbExp=3; IntAct=EBI-2025048, EBI-20895185;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18757743}. Synaptic cleft
CC {ECO:0000269|PubMed:18641643}. Presynaptic active zone
CC {ECO:0000269|PubMed:18641643}. Note=Detected in the synaptic cleft of
CC the ribbon synapse around the postsynaptic terminals of bipolar cells
CC (PubMed:18641643). Colocalizes with BSN, CTBP2 and DAG1 in
CC photoreceptor synaptic terminals (PubMed:18641643).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4VBE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4VBE4-2; Sequence=VSP_028482;
CC -!- TISSUE SPECIFICITY: Expressed in the outer plexiform layer (first
CC synaptic region) but not in the inner plexiform layer (second synaptic
CC region) of the retina (at protein level). Strongly expressed in the
CC photoreceptor layer of the retina. Moderately expressed in pineal gland
CC and brain. Weakly expressed in lung and ovary.
CC {ECO:0000269|PubMed:18641643}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the apical side of the neuroblastic
CC layer (NBL) of the retina at 14.5 dpc and 17.5 dpc. At 16.5 dpc,
CC present in rib cartilage and hair follicle (at protein level).
CC {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:18757743}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate.
CC {ECO:0000269|PubMed:18757743}.
CC -!- DISRUPTION PHENOTYPE: No morphological abnormalities. Knockout mice are
CC viable and fertile. However, the terminal of bipolar cells do not
CC appose to the synapse terminals in the rod photoreceptor ribbon
CC synapses. The signal transmission from the rod photoreceptor to the rod
CC bipolar cells is less sensitive and is delayed compared to the wild
CC type mouse. The signal transmission from cone photoreceptors to the
CC cone bipolar cells is also impaired. These mice show reduced visual
CC function. {ECO:0000269|PubMed:18641643}.
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DR EMBL; DQ223720; ABB48431.1; -; mRNA.
DR EMBL; AK031136; BAC27271.1; -; mRNA.
DR EMBL; AK033332; BAC28235.1; -; mRNA.
DR EMBL; AK037223; BAC29762.1; -; mRNA.
DR EMBL; AK041546; BAC30982.1; -; mRNA.
DR EMBL; AC105969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051455; AAH51455.1; -; mRNA.
DR EMBL; BC095994; AAH95994.1; -; mRNA.
DR EMBL; BC150710; AAI50711.1; -; mRNA.
DR CCDS; CCDS27370.1; -. [Q4VBE4-2]
DR CCDS; CCDS79359.1; -. [Q4VBE4-1]
DR RefSeq; NP_001276425.1; NM_001289496.1. [Q4VBE4-1]
DR RefSeq; NP_848863.1; NM_178748.6. [Q4VBE4-2]
DR RefSeq; XP_017172117.1; XM_017316628.1. [Q4VBE4-2]
DR AlphaFoldDB; Q4VBE4; -.
DR SMR; Q4VBE4; -.
DR BioGRID; 234554; 1.
DR IntAct; Q4VBE4; 6.
DR STRING; 10090.ENSMUSP00000055599; -.
DR GlyGen; Q4VBE4; 1 site.
DR PhosphoSitePlus; Q4VBE4; -.
DR MaxQB; Q4VBE4; -.
DR PaxDb; Q4VBE4; -.
DR PRIDE; Q4VBE4; -.
DR ProteomicsDB; 277561; -. [Q4VBE4-1]
DR ProteomicsDB; 277562; -. [Q4VBE4-2]
DR Antibodypedia; 23033; 117 antibodies from 20 providers.
DR DNASU; 268780; -.
DR Ensembl; ENSMUST00000058593; ENSMUSP00000055599; ENSMUSG00000042961. [Q4VBE4-2]
DR Ensembl; ENSMUST00000096494; ENSMUSP00000094238; ENSMUSG00000042961. [Q4VBE4-1]
DR GeneID; 268780; -.
DR KEGG; mmu:268780; -.
DR UCSC; uc007vea.2; mouse. [Q4VBE4-2]
DR UCSC; uc007veb.2; mouse. [Q4VBE4-1]
DR CTD; 133584; -.
DR MGI; MGI:2146149; Egflam.
DR VEuPathDB; HostDB:ENSMUSG00000042961; -.
DR eggNOG; KOG0613; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000158504; -.
DR HOGENOM; CLU_013380_0_0_1; -.
DR InParanoid; Q4VBE4; -.
DR OMA; ISIQYPQ; -.
DR OrthoDB; 414294at2759; -.
DR PhylomeDB; Q4VBE4; -.
DR TreeFam; TF326548; -.
DR BioGRID-ORCS; 268780; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Egflam; mouse.
DR PRO; PR:Q4VBE4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q4VBE4; protein.
DR Bgee; ENSMUSG00000042961; Expressed in retinal neural layer and 154 other tissues.
DR ExpressionAtlas; Q4VBE4; baseline and differential.
DR Genevisible; Q4VBE4; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IEA:UniProtKB-SubCell.
DR GO; GO:0043083; C:synaptic cleft; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 3.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Synapse.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1017
FT /note="Pikachurin"
FT /id="PRO_0000306804"
FT DOMAIN 37..136
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 144..239
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 343..381
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 386..564
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 565..602
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 609..788
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 784..820
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 835..1014
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 347..358
FT /evidence="ECO:0000250"
FT DISULFID 352..369
FT /evidence="ECO:0000250"
FT DISULFID 371..380
FT /evidence="ECO:0000250"
FT DISULFID 534..564
FT /evidence="ECO:0000250"
FT DISULFID 569..580
FT /evidence="ECO:0000250"
FT DISULFID 574..590
FT /evidence="ECO:0000250"
FT DISULFID 592..601
FT /evidence="ECO:0000250"
FT DISULFID 788..799
FT /evidence="ECO:0000250"
FT DISULFID 793..808
FT /evidence="ECO:0000250"
FT DISULFID 810..819
FT /evidence="ECO:0000250"
FT DISULFID 987..1014
FT /evidence="ECO:0000250"
FT VAR_SEQ 822..830
FT /note="ECGNHCLNT -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028482"
FT CONFLICT 45
FT /note="A -> T (in Ref. 4; AAI50711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1017 AA; 110735 MW; F8A21D89B251D455 CRC64;
MDLISTFSLH FLLLACSLPP GAVSLRTALR KSGKVGPPLD IKLGALNCTA FSIQWKTPKR
SGSSIIGYTV FYSEVGSDKS LRERSHNVPV GQDTLITEEV IGDLKPGTEY QVSVAAYSQT
GKGRLSFPRH VTTLSQDSCL PPAAPQQPHV LVVSDSEVAL SWRPGENEGS APIQSYSVEF
IRPDFDKSWT IIQERLQMDS MVIKGLDPDT NYQFAVKAMN AHGFSPRSWP SNTVRTLGPG
EAGSGHYGPG YITNPGVSED DDGSEDELDL DVSFEEVKPL PATKVGNKKF SVESKKTSVS
NSVMGSRLAQ PTSASLHETT VAIPPTPAQR KGKNSVAMMS RLFDMSCDET LCSADSFCVN
DYAWGGSRCH CNLGKGGEAC SEDIFIQYPQ FFGHSYVTFE PLKNSYQAFQ VTLEFRAEAE
DGLLLYCGES EHGRGDFMSL ALIRRSLHFR FNCGTGIAII ISETKIKLGA WHTVTLYRDG
LNGMLQLNNG TPVTGQSQGQ YSKITFRTPL YLGGAPSAYW LVRATGTNRG FQGCVQSLSV
NGKKIDMRPW PLGKALNGAD VGECSSGICD EASCIHGGTC AAIKADSYIC LCPLGFRGRH
CEDAFALTIP QFRESLRSYA ATPWPLEPQH YLSFTEFEIT FRPDSGDGVL LYSYDTGSKD
FLSINMAAGH VEFRFDCGSG TGVLRSEAPL TLGQWHDLRV SRTAKNGILQ VDKQKVVEGM
AEGGFTQIKC NTDIFIGGVP NYDDVKKNSG ILHPFSGSIQ KIILNDRTIH VKHDFTSGVN
VENAAHPCVG APCAHGGSCR PRKEGYECDC PLGFEGLNCQ KECGNHCLNT IIEAIEIPQF
IGRSYLTYDN PNILKRVSGS RSNAFMRFKT TAKDGLLLWR GDSPMRPNSD FISLGLRDGA
LIFSYNLGSG VASIMVNGSF SDGRWHRVKA VRDGQSGKIT VDDYGARTGK SPGLMRQLNI
NGALYVGGMK EIALHTNRQY LRGLVGCISH FTLSTDYHIS LVEDAVDGKN INTCGAK
