NELL1_MOUSE
ID NELL1_MOUSE Reviewed; 810 AA.
AC Q2VWQ2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein kinase C-binding protein NELL1;
DE AltName: Full=NEL-like protein 1;
DE Flags: Precursor;
GN Name=Nell1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=BJR; TISSUE=Head;
RX PubMed=16537572; DOI=10.1093/hmg/ddl053;
RA Desai J., Shannon M.E., Johnson M.D., Ruff D.W., Hughes L.A., Kerley M.K.,
RA Carpenter D.A., Johnson D.K., Rinchik E.M., Culiat C.T.;
RT "Nell1-deficient mice have reduced expression of extracellular matrix
RT proteins causing cranial and vertebral defects.";
RL Hum. Mol. Genet. 15:1329-1341(2006).
CC -!- FUNCTION: Plays a role in the control of cell growth and
CC differentiation. Promotes osteoblast cell differentiation and terminal
CC mineralization. {ECO:0000269|PubMed:16537572}.
CC -!- SUBUNIT: Homotrimer. Binds to PKC beta-1. Interacts with ATRAID; the
CC interaction promotes osteoblast cell differentiation and mineralization
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope
CC {ECO:0000250}. Secreted {ECO:0000250}. Note=Colocalizes with ATRAID on
CC the nuclear envelope and the perinuclear region. {ECO:0000250}.
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DR EMBL; AY622226; AAV41488.1; -; mRNA.
DR CCDS; CCDS21309.1; -.
DR RefSeq; NP_001032995.1; NM_001037906.2.
DR AlphaFoldDB; Q2VWQ2; -.
DR SMR; Q2VWQ2; -.
DR BioGRID; 237208; 7.
DR STRING; 10090.ENSMUSP00000080550; -.
DR GlyConnect; 2633; 1 N-Linked glycan (1 site).
DR GlyGen; Q2VWQ2; 10 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q2VWQ2; -.
DR PhosphoSitePlus; Q2VWQ2; -.
DR PaxDb; Q2VWQ2; -.
DR PRIDE; Q2VWQ2; -.
DR ProteomicsDB; 252821; -.
DR Antibodypedia; 25294; 160 antibodies from 25 providers.
DR DNASU; 338352; -.
DR Ensembl; ENSMUST00000081872; ENSMUSP00000080550; ENSMUSG00000055409.
DR GeneID; 338352; -.
DR KEGG; mmu:338352; -.
DR UCSC; uc009hbx.1; mouse.
DR CTD; 4745; -.
DR MGI; MGI:2443902; Nell1.
DR VEuPathDB; HostDB:ENSMUSG00000055409; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00810000125439; -.
DR HOGENOM; CLU_006887_0_0_1; -.
DR InParanoid; Q2VWQ2; -.
DR OMA; XGGVLVK; -.
DR OrthoDB; 767046at2759; -.
DR PhylomeDB; Q2VWQ2; -.
DR TreeFam; TF323325; -.
DR BioGRID-ORCS; 338352; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Nell1; mouse.
DR PRO; PR:Q2VWQ2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q2VWQ2; protein.
DR Bgee; ENSMUSG00000055409; Expressed in medial geniculate body and 118 other tissues.
DR ExpressionAtlas; Q2VWQ2; baseline and differential.
DR Genevisible; Q2VWQ2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0045778; P:positive regulation of ossification; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:MGI.
DR CDD; cd00110; LamG; 1.
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; IPR001007; VWF_dom.
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; 4.
DR SMART; SM00215; VWC_out; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
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; Cytoplasm; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Nucleus; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..810
FT /note="Protein kinase C-binding protein NELL1"
FT /id="PRO_0000322642"
FT DOMAIN 57..227
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 271..332
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 434..475
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 476..516
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 517..547
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 549..587
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 596..631
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 632..687
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 692..750
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 395..407
FT /evidence="ECO:0000250"
FT DISULFID 401..416
FT /evidence="ECO:0000250"
FT DISULFID 418..432
FT /evidence="ECO:0000250"
FT DISULFID 438..451
FT /evidence="ECO:0000250"
FT DISULFID 445..460
FT /evidence="ECO:0000250"
FT DISULFID 462..474
FT /evidence="ECO:0000250"
FT DISULFID 480..493
FT /evidence="ECO:0000250"
FT DISULFID 487..502
FT /evidence="ECO:0000250"
FT DISULFID 504..515
FT /evidence="ECO:0000250"
FT DISULFID 519..529
FT /evidence="ECO:0000250"
FT DISULFID 523..535
FT /evidence="ECO:0000250"
FT DISULFID 537..546
FT /evidence="ECO:0000250"
FT DISULFID 553..566
FT /evidence="ECO:0000250"
FT DISULFID 560..575
FT /evidence="ECO:0000250"
FT DISULFID 577..594
FT /evidence="ECO:0000250"
FT DISULFID 600..613
FT /evidence="ECO:0000250"
FT DISULFID 607..622
FT /evidence="ECO:0000250"
FT DISULFID 624..630
FT /evidence="ECO:0000250"
SQ SEQUENCE 810 AA; 89415 MW; 3AD132E97FB83590 CRC64;
MPMDVILVLW FCVCTARTVL GFGMDPDLQM DIITELDLVN TTLGVTQVAG LHNASKAFLF
QDVQREIHSA PHVSEKLIQL FRNKSEFTFL ATVQQKPSTS GVILSIRELE HSYFELESSG
PREEIRYHYI HGGKPRTEAL PYRMADGQWH KVALSVSASH LLLHVDCNRI YERVIDPPET
NLPPGSNLWL GQRNQKHGFF KGIIQDGKII FMPNGFITQC PNLNRTCPTC SDFLSLVQGI
MDLQELLAKM TAKLNYAETR LGQLENCHCE KTCQVSGLLY RDQDSWVDGD NCRNCTCKSG
AVECRRMSCP PLNCSPDSLP VHISGQCCKV CRPKCIYGGK VLAEGQRILT KTCRECRGGV
LVKITEACPP LNCSEKDHIL PENQCCRVCR GHNFCAEAPK CGENSECKNW NTKATCECKN
GYISVQGNSA YCEDIDECAA KMHYCHANTV CVNLPGLYRC DCIPGYIRVD DFSCTEHDDC
GSGQHNCDKN AICTNTVQGH SCTCQPGYVG NGTVCKAFCE EGCRYGGTCV APNKCVCPSG
FTGSHCEKDI DECAEGFVEC HNHSRCVNLP GWYHCECRSG FHDDGTYSLS GESCIDIDEC
ALRTHTCWND SACINLAGGF DCLCPSGPSC SGDCPHEGGL KHNGQVWILR EDRCSVCSCK
DGKIFCRRTA CDCQNPNVDL FCCPECDTRV TSQCLDQSGQ KLYRSGDNWT HSCQQCRCLE
GEADCWPLAC PSLSCEYTAI FEGECCPRCV SDPCLADNIA YDIRKTCLDS SGISRLSGAV
WTMAGSPCTT CQCKNGRVCC SVDLVCLENN
