ID NELL2_DANRE Reviewed; 811 AA. AC A1A5Y0; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=Protein kinase C-binding protein NELL2a; DE AltName: Full=NEL-like protein 2; DE Flags: Precursor; GN Name=nell2a; ORFNames=zgc:158375; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May regulate neuronal differentiation, polarization and axon CC guidance. {ECO:0000250|UniProtKB:Q61220, ECO:0000250|UniProtKB:Q62918}. CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q62918}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q62918}. 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; BC128854; AAI28855.1; -; mRNA. DR RefSeq; NP_001073544.1; NM_001080075.1. DR AlphaFoldDB; A1A5Y0; -. DR SMR; A1A5Y0; -. DR STRING; 7955.ENSDARP00000111598; -. DR GlyCosmos; A1A5Y0; 6 sites, No reported glycans. DR PaxDb; 7955-ENSDARP00000107571; -. DR GeneID; 790930; -. DR KEGG; dre:790930; -. DR AGR; ZFIN:ZDB-GENE-030131-7972; -. DR CTD; 790930; -. DR ZFIN; ZDB-GENE-030131-7972; nell2a. DR eggNOG; KOG1217; Eukaryota. DR InParanoid; A1A5Y0; -. DR OrthoDB; 5487at2759; -. DR PhylomeDB; A1A5Y0; -. DR PRO; PR:A1A5Y0; -. DR Proteomes; UP000000437; Chromosome 25. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0008201; F:heparin binding; IBA:GO_Central. DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central. DR GO; GO:0048513; P:animal organ development; IEA:UniProt. DR GO; GO:0009566; P:fertilization; ISS:UniProtKB. DR CDD; cd00054; EGF_CA; 4. DR CDD; cd00110; LamG; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 6.20.200.20; -; 2. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR Gene3D; 2.10.25.10; Laminin; 6. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR024731; EGF_dom. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR048287; TSPN-like_N. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR24042; NEL HOMOLOG; 1. DR PANTHER; PTHR24042:SF0; PROTEIN KINASE C-BINDING PROTEIN NELL2; 1. DR Pfam; PF12947; EGF_3; 1. DR Pfam; PF07645; EGF_CA; 3. DR Pfam; PF02210; Laminin_G_2; 1. DR Pfam; PF00093; VWC; 2. DR SMART; SM00181; EGF; 6. DR SMART; SM00179; EGF_CA; 5. DR SMART; SM00282; LamG; 1. DR SMART; SM00210; TSPN; 1. DR SMART; SM00214; VWC; 3. DR SMART; SM00215; VWC_out; 2. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF57603; FnI-like domain; 2. DR SUPFAM; SSF57184; Growth factor receptor domain; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 3. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS50026; EGF_3; 6. DR PROSITE; PS01187; EGF_CA; 3. DR PROSITE; PS50025; LAM_G_DOMAIN; 1. DR PROSITE; PS01208; VWFC_1; 2. DR PROSITE; PS50184; VWFC_2; 2. PE 2: Evidence at transcript level; KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Metal-binding; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT CHAIN 19..811 FT /note="Protein kinase C-binding protein NELL2a" FT /id="PRO_0000354683" FT DOMAIN 54..225 FT /note="Laminin G-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 269..328 FT /note="VWFC 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 395..437 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 438..479 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 480..520 FT /note="EGF-like 3; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 521..551 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 553..592 FT /note="EGF-like 5; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 600..635 FT /note="EGF-like 6; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 636..691 FT /note="VWFC 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 696..754 FT /note="VWFC 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT BINDING 438 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 439 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 441 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 457 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 458 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 461 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 553 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 554 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 556 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 572 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 573 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 576 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 600 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 601 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 603 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 619 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 620 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 623 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT CARBOHYD 222 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 290 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 295 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 515 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 613 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 633 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 399..411 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 405..420 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 422..436 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 442..455 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 449..464 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 466..478 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 484..497 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 491..506 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 508..519 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 523..533 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 527..539 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 541..550 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 557..570 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 564..579 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 581..598 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 604..617 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 611..626 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 628..634 FT /evidence="ECO:0000250|UniProtKB:Q99435" SQ SEQUENCE 811 AA; 89142 MW; 9D588B3B1574CEC7 CRC64; MAFLQLFVGL LCGAAVSAFG VDPAVRIGVF QEFSPGQGFS GVTQVKGFRD DTRAFMFQGS SRSVRVPDAA AGHMLQKLRG KTEFSIALTL KQDKLNSGVI LSIHHGEHRL LELESSGQKS EVRLHFRTGL QQTHTEIFPF TLADEQWHRV SVSISAAHLT LYVDCNRIYE RVVPVPLMEI PEDSSFWVGQ RNSAHGLFKG IMQDLQILVM PQGFITQCPD LNRTCPTCND FHGLVQKIME LQDILAKTSS KLSLAEEKMS GLDSCYCERT CRVKDQIYRE EQSWTDGCKN CTCSNGTVRC EKILCPPLDC PDGTTPAYVT GTCCKECQPM CLFSEQTLVE GQSCAVHHPS GLCQLFQCRD RTMHRVPGAE DCPALSCAES DQITLTDRCC RVCRGHDFCA EENICSENSD CVNLDAGASC GCKNGFRPLR LDSAYCEDID ECAEGRHYCR ENTECVNTAG SFMCVCHTGF IRIDDYSCTE HDECASGQHD CDENALCFNT VGGHSCSCKP GYSGNGTVCR ALCDGRCLNG GSCASPNVCV CVQGFSGQNC ETDIDECSEG LVQCAAHATC VNLPGWYHCE CRDGYHDNEV FSANGESCRD IDECRTGRST CANDTVCFNL DGGFDCRCPH GHNCSGDCIH NSRVRHNAQI WVLDTDHCSV CSCQEGQVKC RRMVCDCENP TVDVLCCPEC DPRLTSQCLH QNGLLTYSSG DTWIDSCQRC QCLQGEVDCW PLSCPPVDCD FTLVPEGECC PRCVSDPCQA HAVRSDISKT CIDEHGITRF SGSAWVKHGT HCTLCQCKNG HVCCSVDPMC L //