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Database: UniProt
Entry: B4F785
LinkDB: B4F785
Original site: B4F785 
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   16-JAN-2019, entry version 61.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   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.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   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.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in both the normal retinal photoreceptor ribbon
CC       synapse formation and physiological functions of visual
CC       perception. Necessary for proper bipolar dendritic tip apposition
CC       to the photoreceptor ribbon synapse. Promotes matrix assembly and
CC       cell adhesiveness (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DAG1 alpha-dystroglycan. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q4VBE4}. Cell junction, synapse
CC       {ECO:0000250|UniProtKB:Q4VBE4}. Note=Detected in the synaptic
CC       cleft of the ribbon synapse around the postsynaptic terminals of
CC       bipolar cells. Colocalizes with BSN, CTBP2 and DAG1 in
CC       photoreceptor synaptic terminals. {ECO:0000250|UniProtKB:Q4VBE4}.
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan
CC       sulfate. {ECO:0000250}.
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   UniGene; Rn.27713; -.
DR   ProteinModelPortal; B4F785; -.
DR   SMR; B4F785; -.
DR   STRING; 10116.ENSRNOP00000016722; -.
DR   PaxDb; B4F785; -.
DR   PRIDE; B4F785; -.
DR   GeneID; 365691; -.
DR   KEGG; rno:365691; -.
DR   UCSC; RGD:1306592; rat.
DR   CTD; 133584; -.
DR   RGD; 1306592; Egflam.
DR   eggNOG; KOG0613; Eukaryota.
DR   eggNOG; KOG3509; Eukaryota.
DR   eggNOG; ENOG410XTD2; LUCA.
DR   HOGENOM; HOG000112344; -.
DR   HOVERGEN; HBG107839; -.
DR   InParanoid; B4F785; -.
DR   OrthoDB; 414294at2759; -.
DR   PRO; PR:B4F785; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; 2.
DR   Pfam; PF02210; Laminin_G_2; 1.
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   2: Evidence at transcript level;
KW   Cell junction; Complete proteome; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW   Secreted; Signal; Synapse.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25   1005       Pikachurin.
FT                                /FTId=PRO_0000361571.
FT   DOMAIN       37    136       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      144    239       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      339    377       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      382    560       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      561    598       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      605    784       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      780    816       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      823   1002       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   CARBOHYD     47     47       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    343    354       {ECO:0000250}.
FT   DISULFID    348    365       {ECO:0000250}.
FT   DISULFID    367    376       {ECO:0000250}.
FT   DISULFID    530    560       {ECO:0000250}.
FT   DISULFID    565    576       {ECO:0000250}.
FT   DISULFID    570    586       {ECO:0000250}.
FT   DISULFID    588    597       {ECO:0000250}.
FT   DISULFID    784    795       {ECO:0000250}.
FT   DISULFID    789    804       {ECO:0000250}.
FT   DISULFID    806    815       {ECO:0000250}.
FT   DISULFID    975   1002       {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
//
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