NELL1_RAT
ID NELL1_RAT Reviewed; 810 AA.
AC Q62919;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein kinase C-binding protein NELL1;
DE AltName: Full=NEL-like protein 1;
DE Flags: Precursor;
GN Name=Nell1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10548494; DOI=10.1006/bbrc.1999.1638;
RA Kuroda S., Oyasu M., Kawakami M., Kanayama N., Tanizawa K., Saito N.,
RA Abe T., Matsuhashi S., Ting K.;
RT "Biochemical characterization and expression analysis of neural
RT thrombospondin-1-like proteins NELL1 and NELL2.";
RL Biochem. Biophys. Res. Commun. 265:79-86(1999).
CC -!- FUNCTION: Plays a role in the control of cell growth and
CC differentiation. Promotes osteoblast cell differentiation and terminal
CC mineralization (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ATRAID; the interaction promotes osteoblast
CC cell differentiation and mineralization (By similarity). Homotrimer.
CC Binds to PKC beta-1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope
CC {ECO:0000250}. Secreted. Note=Colocalizes with ATRAID on the nuclear
CC envelope and the perinuclear region. {ECO:0000250}.
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; U48246; AAC72252.1; -; mRNA.
DR PIR; T10756; T10756.
DR RefSeq; NP_112331.1; NM_031069.1.
DR AlphaFoldDB; Q62919; -.
DR SMR; Q62919; -.
DR STRING; 10116.ENSRNOP00000052883; -.
DR GlyGen; Q62919; 10 sites.
DR iPTMnet; Q62919; -.
DR PhosphoSitePlus; Q62919; -.
DR PaxDb; Q62919; -.
DR PRIDE; Q62919; -.
DR GeneID; 81733; -.
DR KEGG; rno:81733; -.
DR UCSC; RGD:620998; rat.
DR CTD; 4745; -.
DR RGD; 620998; Nell1.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q62919; -.
DR OrthoDB; 767046at2759; -.
DR PhylomeDB; Q62919; -.
DR PRO; PR:Q62919; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0045778; P:positive regulation of ossification; IMP:RGD.
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; IMP:RGD.
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; 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_0000007665"
FT DOMAIN 57..227
FT /note="Laminin G-like"
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:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 401..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 418..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 438..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 445..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 462..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 480..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 487..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 504..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 519..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 523..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 537..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 553..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 560..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 577..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 600..613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 607..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 624..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 810 AA; 89212 MW; 46F09C466AF9AB0B CRC64;
MPMDVILVLW FCVCTARTVL GFGMDPDLQL DIISELDLVN TTLGVTQVAG LHNASKAFLF
QDVQREIHSA PHVSEKLIQL FRNKSEFTFL ATVQQKPSTS GVILSIRELE HSYFELESSG
PREEIRYHYI HGGKPRTEAL PYRMADGQWH KVALSVSASH LLLHIDCNRI YERVIDPPET
NLPPGSNLWL GQRNQKHGFF KGIIQDGKII FMPNGFITQC PNLNRTCPTC SDFLSLVQGI
MDLQELLAKM TAKLNYAETR LGQLENCHCE KTCQVSGLLY RDQDSWVDGD NCGNCTCKSG
AVECRRMSCP PLNCSPDSLP VHISGQCCKV CRPKCIYGGK VLAEGQRILT KTCRECRGGV
LVKITEACPP LNCSAKDHIL PENQCCRVCP GHNFCAEAPK CGENSECKNW NTKATCECKN
GYISVQGNSA YCEDIDECAA KMHYCHANTV CVNLPGLYRC DCVPGYIRVD DFSCTEHDDC
GSGQHNCDKN AICTNTVQGH SCTCQPGYVG NGTICKAFCE EGCRYGGTCV APNKCVCPSG
FTGSHCEKDI DECAEGFVEC HNYSRCVNLP GWYHCECRSG FHDDGTYSLS GESCIDIDEC
ALRTHTCWND SACINLAGGF DCLCPSGPSC SGDCPHEGGL KHNGQVWILR EDRCSVCSCK
DGKIFCRRTA CDCQNPNVDL FCCPECDTRV TSQCLDQSGQ KLYRSGDNWT HSCQQCRCLE
GEADCWPLAC PSLGCEYTAM FEGECCPRCV SDPCLAGNIA YDIRKTCLDS FGVSRLSGAV
WTMAGSPCTT CKCKNGRVCC SVDLECIENN
