ID EGFLA_RAT Reviewed; 1005 AA.
AC B4F785;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Pikachurin;
DE AltName: Full=EGF-like, fibronectin type-III and laminin G-like domain-containing protein;
DE Flags: Precursor;
GN Name=Egflam;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
CC -!- FUNCTION: Involved in both the retinal photoreceptor ribbon synapse
CC formation and physiological functions of visual perception. Plays a key
CC role in the synaptic organization of photoreceptors by mediating
CC transsynaptic interaction between alpha-dystroglycan and GPR179 on the
CC postsynaptic membrane. Necessary for proper bipolar dendritic tip
CC apposition to the photoreceptor ribbon synapse. Promotes matrix
CC assembly and cell adhesiveness. {ECO:0000250|UniProtKB:Q4VBE4}.
CC -!- SUBUNIT: Interacts with DAG1 alpha-dystroglycan. Interacts with GPR158
CC and GPR179; transsynaptic interaction is required for synaptic
CC organization of photoreceptor cells. {ECO:0000250|UniProtKB:Q4VBE4}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q4VBE4}. Synaptic cleft
CC {ECO:0000250|UniProtKB:Q4VBE4}. Presynaptic active zone
CC {ECO:0000250|UniProtKB:Q4VBE4}. Note=Detected in the synaptic cleft of
CC the ribbon synapse around the postsynaptic terminals of bipolar cells.
CC Colocalizes with BSN, CTBP2 and DAG1 in photoreceptor synaptic
CC terminals. {ECO:0000250|UniProtKB:Q4VBE4}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate.
CC {ECO:0000250|UniProtKB:Q4VBE4}.
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DR EMBL; AABR03012233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03016535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC168173; AAI68173.1; -; mRNA.
DR RefSeq; NP_001102408.2; NM_001108938.2.
DR AlphaFoldDB; B4F785; -.
DR SMR; B4F785; -.
DR STRING; 10116.ENSRNOP00000016722; -.
DR GlyCosmos; B4F785; 1 site, No reported glycans.
DR GlyGen; B4F785; 1 site.
DR PhosphoSitePlus; B4F785; -.
DR PaxDb; 10116-ENSRNOP00000016722; -.
DR GeneID; 365691; -.
DR KEGG; rno:365691; -.
DR UCSC; RGD:1306592; rat.
DR AGR; RGD:1306592; -.
DR CTD; 133584; -.
DR RGD; 1306592; Egflam.
DR eggNOG; KOG0613; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR InParanoid; B4F785; -.
DR OrthoDB; 2878505at2759; -.
DR PRO; PR:B4F785; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005614; C:interstitial matrix; ISO:RGD.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.10.25.10; Laminin; 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 PANTHER; PTHR15036:SF88; PIKACHURIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
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; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
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 2: Evidence at transcript level;
KW Cell projection; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Heparan sulfate; Proteoglycan; Reference proteome; Repeat;
KW Secreted; Signal; Synapse.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1005
FT /note="Pikachurin"
FT /id="PRO_0000361571"
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 339..377
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 382..560
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 561..598
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 605..784
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 780..816
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 823..1002
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 281..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 343..354
FT /evidence="ECO:0000250"
FT DISULFID 348..365
FT /evidence="ECO:0000250"
FT DISULFID 367..376
FT /evidence="ECO:0000250"
FT DISULFID 530..560
FT /evidence="ECO:0000250"
FT DISULFID 565..576
FT /evidence="ECO:0000250"
FT DISULFID 570..586
FT /evidence="ECO:0000250"
FT DISULFID 588..597
FT /evidence="ECO:0000250"
FT DISULFID 784..795
FT /evidence="ECO:0000250"
FT DISULFID 789..804
FT /evidence="ECO:0000250"
FT DISULFID 806..815
FT /evidence="ECO:0000250"
FT DISULFID 975..1002
FT /evidence="ECO:0000250"
SQ SEQUENCE 1005 AA; 109670 MW; 915F4DCDF275331F CRC64;
MDLISTFLLH FLLLACSLPP GAVSLRTALR KSGKVGPPLD IKLGALNCTA FSIQWKTPKR
SGSSIVGYTV FYSELGSDKS LREQSHNVPV GQDTLITEEV IGDLKPGTEY RVSIAAYSQT
GKGRLSFPRH VTTLSQDSCL PPEAPHQPHV LVVSDSEVAL SWRPGENEGS APIQSYSVEF
IRPDFDKSWT IIQERLQMDS MVIKGLDPDT NYQFAVRAMN AYGFSLRSQP SNTIRTLGPG
EAGSGRYGPG YITDTGVSED DDASEDELDL DVSFEEVKPL PATKVGNKKS KKTSVSNSEM
DSRLAQPTSA SLPETTVAVP PTPAQRKGKN SVAVMSRLFD MSCDETLCSA DSFCVNDYAW
GGSRCHCNLG KGGEACSEDI FIQYPQFFGH SYVTFEPLKN SYQAFQITLE FRAEAEDGLL
LYCGESEHGR GDFMSLALIR RSLHFRFNCG TGMAIIISET KIKLGAWHSV TLYRDGLNGL
LQLNNGTPVT GQSQGQYSKI TFRTPLYLGG APSAYWLVRA TGTNRGFQGC VQSLAVNGKK
IDMRPWPLGK ALNGADVGEC SSGICDEASC INGGTCAAIK ADSYICLCPL GFRGRHCEDA
FTLTIPQFRE SLRSYAATPW PLEPQHYLSF TEFEITFRPD SGDGVLLYSY DTSSKDFLSI
IMAAGHVEFR FDCGSGTGVL RSEDTLTLGQ WHDLRVSRTA KNGILQVDKQ KVVEGMAEGG
FTQIKCNTDI FIGGVPNYDD VKKNSGILHP FSGSIQKIIL NDRTIHVRHD FTSGVNVENA
AHPCVGAPCA HGGSCRPRKE GYECDCPLGF EGLNCQKAIT EAIEIPQFIG RSYLTYDNPN
ILKRVSGSRS NAFMRFKTTA KDGLLLWRGD SPMRPNSDFI SLGLRDGALV FSYNLGSGVA
SIMVNGSFSD GRWHRVKAVR DGQSGKITVD DYGARTGKSP GMMRQLNING ALYVGGMKEI
ALRTNRQYMR GLVGCISHFT LSTDYHISLV EDAVDGKNIN TCGAK
//
