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EGFLA_BOVIN
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   03-AUG-2022, entry version 82.
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. Necessary
CC       for proper bipolar dendritic tip apposition to the photoreceptor ribbon
CC       synapse. Promotes matrix assembly and cell adhesiveness (By
CC       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}. 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}.
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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   PaxDb; A3KN33; -.
DR   GeneID; 534427; -.
DR   KEGG; bta:534427; -.
DR   CTD; 133584; -.
DR   eggNOG; KOG0613; Eukaryota.
DR   eggNOG; KOG3509; Eukaryota.
DR   InParanoid; A3KN33; -.
DR   OrthoDB; 414294at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; 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; 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 projection; Disulfide bond; EGF-like domain; Extracellular matrix;
KW   Glycoprotein; Reference proteome; Repeat; 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
 
 
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