ID NELL2_XENTR Reviewed; 814 AA. AC A2VCU8; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=Protein kinase C-binding protein NELL2; DE AltName: Full=NEL-like protein 2; DE Flags: Precursor; GN Name=nell2; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RG NIH - Xenopus Gene Collection (XGC) 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; BC128627; AAI28628.1; -; mRNA. DR RefSeq; NP_001090754.1; NM_001097285.1. DR AlphaFoldDB; A2VCU8; -. DR SMR; A2VCU8; -. DR STRING; 8364.ENSXETP00000003252; -. DR GlyCosmos; A2VCU8; 6 sites, No reported glycans. DR PaxDb; 8364-ENSXETP00000032027; -. DR Ensembl; ENSXETT00000032027; ENSXETP00000032027; ENSXETG00000014625. DR GeneID; 100037839; -. DR KEGG; xtr:100037839; -. DR AGR; Xenbase:XB-GENE-852641; -. DR CTD; 4753; -. DR Xenbase; XB-GENE-852641; nell2. DR eggNOG; KOG1217; Eukaryota. DR HOGENOM; CLU_006887_0_0_1; -. DR InParanoid; A2VCU8; -. DR OMA; TCGQFLE; -. DR OrthoDB; 5487at2759; -. DR PhylomeDB; A2VCU8; -. DR TreeFam; TF323325; -. DR Proteomes; UP000008143; Chromosome 3. DR Bgee; ENSXETG00000014625; Expressed in brain and 9 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. 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; SSF57196; EGF/Laminin; 2. DR SUPFAM; SSF57603; FnI-like domain; 2. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. 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; PS01208; VWFC_1; 2. DR PROSITE; PS50184; VWFC_2; 3. 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..19 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT CHAIN 20..814 FT /note="Protein kinase C-binding protein NELL2" FT /id="PRO_0000354685" FT DOMAIN 53..226 FT /note="Laminin G-like" FT DOMAIN 270..329 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..599 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 51 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 223 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 296 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 814 AA; 90762 MW; 87EB9F240779A9B7 CRC64; MEFILGIFCV IFCLRAGAGF GVDPSLQIDI FEDFQLGEAT PGVQQVQGFH NRSKAFLFQD TSRSIKASAE TAERIFTKLR NKHEFTILVT LKQAMLNSGV ILSIHHADHR YLELESSGHR NEVRLHYRSG SHRSQTEVFP YILADDKWHR FSIAISASHL VLHIDCNKIY ERIVEKTFMD VPPGTALWVG QRNNVHGYFK GIMQDLQIVV MPQGFISQCP DLNRTCPTCN DFHGLVQKIM ELQDILAKTS AKLSRAEQRM NRLDQCYCER SCTVKGNIYR ELESWMDGCK KCTCTNGTAQ CETLTCSVPN CLSGFAPAYV PGKCCKECQP VCMYQGQMYF EGEQEAVQSS SGACVLFQCK SNTMQRIESP ECLPLNCPQS QHITLRSGCC KVCKGHDFCS EGHNCVEYSI CKNLNDKAVC ICRDGFRALR EDSAYCEDID ECTEGRHYCR ENTVCVNTPG SFMCVCQTGY LKIDDYSCTE HNECATNQHS CDENAVCYNT VGGHNCVCQP GYTGNGTVCK AFCTDGCRNG GTCIAPNICA CPQGFTGPSC EADIDECTEG FVQCDSRANC INLPGWYHCE CRDGYHDNGM FSLSGESCED IDECATGRHS CSNDTVCFNL DGGFDCRCPH GKNCSGDCTH EGKIKHNGQI WVLENDRCSV CSCQVGLVMC RRMVCDCENP TVDLFCCPEC DPRLSSQCLH QSGELTYKSG DTWVQNCQQC RCLQGEVDCW PLPCPEIDCE FSVVPESECC PRCISDPCQA DIIRNDITKT CVDETNVVRF TGSSWIKHGT ECTLCQCKNG HMCCSVDPQC LQEL //