CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014566
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pikachurin 
Protein Synonyms/Alias
 Agrin-like protein; EGF-like, fibronectin type-III and laminin G-like domain-containing protein 
Gene Name
 EGFLAM 
Gene Synonyms/Alias
 AGRINL; AGRNL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
289ATKGGNKKFLVESKKubiquitination[1, 2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Involved in both the retinal photoreceptor ribbon synapse formation and physiological functions of visual perception. Necessary for proper bipolar dendritic tip apposition to the photoreceptor ribbon synapse. Promotes matrix assembly and cell adhesiveness (By similarity). 
Sequence Annotation
 DOMAIN 34 133 Fibronectin type-III 1.
 DOMAIN 141 237 Fibronectin type-III 2.
 DOMAIN 343 381 EGF-like 1.
 DOMAIN 386 564 Laminin G-like 1.
 DOMAIN 565 602 EGF-like 2.
 DOMAIN 609 788 Laminin G-like 2.
 DOMAIN 784 820 EGF-like 3.
 DOMAIN 835 1014 Laminin G-like 3.
 CARBOHYD 47 47 N-linked (GlcNAc...) (Potential).
 DISULFID 347 358 By similarity.
 DISULFID 352 369 By similarity.
 DISULFID 371 380 By similarity.
 DISULFID 534 564 By similarity.
 DISULFID 569 580 By similarity.
 DISULFID 574 590 By similarity.
 DISULFID 592 601 By similarity.
 DISULFID 788 799 By similarity.
 DISULFID 793 808 By similarity.
 DISULFID 810 819 By similarity.
 DISULFID 987 1014 By similarity.  
Keyword
 Alternative splicing; Cell junction; Complete proteome; Direct protein sequencing; Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1017 AA 
Protein Sequence
MDLIRGVLLR LLLLASSLGP GAVSLRAAIR KPGKVGPPLD IKLGALNCTA FSIQWKMPRH 60
PGSPILGYTV FYSEVGADKS LQEQLHSVPL SRDIPTTEEV IGDLKPGTEY RVSIAAYSQA 120
GKGRLSSPRH VTTLSQDSCL PPAAPQQPHV IVVSDSEVAL SWKPGASEGS APIQYYSVEF 180
IRPDFDKKWT SIHERIQMDS MVIKGLDPDT NYQFAVRAMN SHGPSPRSWP SDIIRTLCPE 240
EAGSGRYGPR YITDMGAGED DEGFEDDLDL DISFEEVKPL PATKGGNKKF LVESKKMSIS 300
NPKTISRLIP PTSASLPVTT VAPQPIPIQR KGKNGVAIMS RLFDMPCDET LCSADSFCVN 360
DYTWGGSRCQ CTLGKGGESC SEDIVIQYPQ FFGHSYVTFE PLKNSYQAFQ ITLEFRAEAE 420
DGLLLYCGEN EHGRGDFMSL AIIRRSLQFR FNCGTGVAII VSETKIKLGG WHTVMLYRDG 480
LNGLLQLNNG TPVTGQSQGQ YSKITFRTPL YLGGAPSAYW LVRATGTNRG FQGCVQSLAV 540
NGRRIDMRPW PLGKALSGAD VGECSSGICD EASCIHGGTC TAIKADSYIC LCPLGFKGRH 600
CEDAFTLTIP QFRESLRSYA ATPWPLEPQH YLSFMEFEIT FRPDSGDGVL LYSYDTGSKD 660
FLSINLAGGH VEFRFDCGSG TGVLRSEDPL TLGNWHELRV SRTAKNGILQ VDKQKIVEGM 720
AEGGFTQIKC NTDIFIGGVP NYDDVKKNSG VLKPFSGSIQ KIILNDRTIH VKHDFTSGVN 780
VENAAHPCVR APCAHGGSCR PRKEGYDCDC PLGFEGLHCQ KECGNYCLNT IIEAIEIPQF 840
IGRSYLTYDN PDILKRVSGS RSNVFMRFKT TAKDGLLLWR GDSPMRPNSD FISLGLRDGA 900
LVFSYNLGSG VASIMVNGSF NDGRWHRVKA VRDGQSGKIT VDDYGARTGK SPGMMRQLNI 960
NGALYVGGMK EIALHTNRQY MRGLVGCISH FTLSTDYHIS LVEDAVDGKN INTCGAK 1017 
Gene Ontology
 GO:0005604; C:basement membrane; IEA:Compara.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005614; C:interstitial matrix; IEA:Compara.
 GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
 GO:0005539; F:glycosaminoglycan binding; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; IEA:Compara.
 GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Compara.
 GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Compara. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR000742; EG-like_dom.
 IPR013032; EGF-like_CS.
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR001791; Laminin_G. 
Pfam
 PF00008; EGF
 PF00041; fn3
 PF00054; Laminin_G_1
 PF02210; Laminin_G_2 
SMART
 SM00181; EGF
 SM00060; FN3
 SM00282; LamG 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS50853; FN3
 PS50025; LAM_G_DOMAIN 
PRINTS