ID EGFLA_BOVIN Reviewed; 1018 AA.
AC A3KN33;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC133537; AAI33538.1; -; mRNA.
DR RefSeq; NP_001076947.1; NM_001083478.1.
DR AlphaFoldDB; A3KN33; -.
DR SMR; A3KN33; -.
DR STRING; 9913.ENSBTAP00000026111; -.
DR GlyCosmos; A3KN33; 1 site, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000026111; -.
DR GeneID; 534427; -.
DR KEGG; bta:534427; -.
DR CTD; 133584; -.
DR eggNOG; KOG0613; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR InParanoid; A3KN33; -.
DR OrthoDB; 2878505at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1018
FT /note="Pikachurin"
FT /id="PRO_0000306802"
FT DOMAIN 37..145
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 153..248
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 352..390
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 395..573
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 574..611
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 618..797
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 793..829
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 836..1015
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 228..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
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 356..367
FT /evidence="ECO:0000250"
FT DISULFID 361..378
FT /evidence="ECO:0000250"
FT DISULFID 380..389
FT /evidence="ECO:0000250"
FT DISULFID 543..573
FT /evidence="ECO:0000250"
FT DISULFID 578..589
FT /evidence="ECO:0000250"
FT DISULFID 583..599
FT /evidence="ECO:0000250"
FT DISULFID 601..610
FT /evidence="ECO:0000250"
FT DISULFID 797..808
FT /evidence="ECO:0000250"
FT DISULFID 802..817
FT /evidence="ECO:0000250"
FT DISULFID 819..828
FT /evidence="ECO:0000250"
FT DISULFID 988..1015
FT /evidence="ECO:0000250"
SQ SEQUENCE 1018 AA; 111405 MW; 440577855A45D92A CRC64;
MDLIRGVLLR LLLLASSLGP GAAPLRSALR KQGKVGPPLD IILDALNCSA FSIQWKMPRH
PPSPIMGYTV FYSEVGIDKS LQERSYGVPP GLDTPTSGRL DHQMIFEEVI GDLKPGTEYR
VSMAAYSQTG KGRLSSPQHV TTLPQDSCLP PTAPQQPHVI VVSDSEVALS WKPGESEGSS
PIQYYSVEFT RPDFDKSWTS IREQIQMDSM VIKGLDPDTN YQFAVRAVNP HGSSPRSQPS
STIRTARPEE SGSGRYGPHY ATDTEAGEDD DTFEDDLDLD ISFEEVKPLP AIKEGNKKFF
VESKMAPRPN PMTVSRLVPP TPASLPTTAV APQPTPVDRK GKHGVAVMPR LFDTSCDETV
CSADSFCVSD YTWGGSRCHC NLGKGGESCS EDIVIQYPQF FGHSYVTFEP LKNSYQAFQI
TLEFRAEAED GLLLYCGENE HGRGDFMSLA VIRRSLQFRF NCGTGVAIIV SETKIKLGGW
HTVTLYRDGL NGLLQLNNGT PVTGQSQGQY SKITFRTPLY LGGAPSAYWL VRATGTNRGF
QGCVQALTVN GKRLDLRPWP LGKALSGADV GECSSGICDE ASCINGGTCM ASKADSYICL
CPLGFRGRHC EDAFTLTIPQ FKESLRSYAA TPWPLEPRHY LSFMEFEVTF RPDSEDGVLL
YSYDTGSKDF LSINMAGGHV EFRFDCGSGT GVLRSEEPLT LGHWHELCVS RTAKNGILQV
DKQKAVEGMA EGGFTQIKCN SDIFIGGVPN YDDVKKNSGI LKPFSGSIQK IILNDRTIHV
KHDFTWGVNV ENAAHPCVGS PCAHGGSCRP RKEGYECDCP LGFEGLHCQK AITEAIEIPQ
FIGRSYLTYD NPDILKRVSG SRSNAFMRFK TTAKDGLLLW RGDSPMRPNS DFISLGLRDG
ALVFSYNLGS GVASIMVNGS FNDGRWHRVK AVRDGQSGKI TVDDYGARTG KSPGMMRQLN
INGALYVGGM KEIALHTNRQ YMRGLVGCIS HFTLSTDYHI SLVEDAVDGK NINTCGAK
//
