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Q62919 (NELL1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein kinase C-binding protein NELL1
Alternative name(s):
NEL-like protein 1
Gene names
Name:Nell1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization By similarity.

Subunit structure

Interacts with ATRAID; the interaction promotes osteoblast cell differentiation and mineralization By similarity. Homotrimer. Binds to PKC beta-1.

Subcellular location

Cytoplasm By similarity. Nucleus envelope By similarity. Secreted. Note: Colocalizes with ATRAID on the nuclear envelope and the perinuclear region By similarity.

Sequence similarities

Contains 5 EGF-like domains.

Contains 1 laminin G-like domain.

Contains 3 VWFC domains.

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentCytoplasm
Nucleus
Secreted
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

induction of apoptosis

Inferred from mutant phenotype PubMed 14672347. Source: RGD

negative regulation of cyclin catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of osteoblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of bone mineralization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

protein homotrimerization

Inferred from direct assay Ref.1. Source: RGD

regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular space

Inferred from direct assay Ref.1. Source: RGD

nuclear envelope

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from direct assay Ref.1. Source: RGD

identical protein binding

Inferred from direct assay Ref.1. Source: RGD

protein kinase C binding

Inferred from direct assay PubMed 10600492. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 810789Protein kinase C-binding protein NELL1
PRO_0000007665

Regions

Domain57 – 227171Laminin G-like
Domain271 – 33262VWFC 1
Domain434 – 47542EGF-like 1; calcium-binding Potential
Domain476 – 51641EGF-like 2; calcium-binding Potential
Domain517 – 54731EGF-like 3
Domain549 – 58739EGF-like 4; calcium-binding Potential
Domain596 – 63136EGF-like 5; calcium-binding Potential
Domain632 – 68756VWFC 2
Domain692 – 75059VWFC 3

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation2241N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential
Glycosylation5111N-linked (GlcNAc...) Potential
Glycosylation5621N-linked (GlcNAc...) Potential
Glycosylation6091N-linked (GlcNAc...) Potential
Glycosylation7081N-linked (GlcNAc...) Potential
Disulfide bond395 ↔ 407 By similarity
Disulfide bond401 ↔ 416 By similarity
Disulfide bond418 ↔ 432 By similarity
Disulfide bond438 ↔ 451 By similarity
Disulfide bond445 ↔ 460 By similarity
Disulfide bond462 ↔ 474 By similarity
Disulfide bond480 ↔ 493 By similarity
Disulfide bond487 ↔ 502 By similarity
Disulfide bond504 ↔ 515 By similarity
Disulfide bond519 ↔ 529 By similarity
Disulfide bond523 ↔ 535 By similarity
Disulfide bond537 ↔ 546 By similarity
Disulfide bond553 ↔ 566 By similarity
Disulfide bond560 ↔ 575 By similarity
Disulfide bond577 ↔ 594 By similarity
Disulfide bond600 ↔ 613 By similarity
Disulfide bond607 ↔ 622 By similarity
Disulfide bond624 ↔ 630 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62919 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 46F09C466AF9AB0B

FASTA81089,212
        10         20         30         40         50         60 
MPMDVILVLW FCVCTARTVL GFGMDPDLQL DIISELDLVN TTLGVTQVAG LHNASKAFLF 

        70         80         90        100        110        120 
QDVQREIHSA PHVSEKLIQL FRNKSEFTFL ATVQQKPSTS GVILSIRELE HSYFELESSG 

       130        140        150        160        170        180 
PREEIRYHYI HGGKPRTEAL PYRMADGQWH KVALSVSASH LLLHIDCNRI YERVIDPPET 

       190        200        210        220        230        240 
NLPPGSNLWL GQRNQKHGFF KGIIQDGKII FMPNGFITQC PNLNRTCPTC SDFLSLVQGI 

       250        260        270        280        290        300 
MDLQELLAKM TAKLNYAETR LGQLENCHCE KTCQVSGLLY RDQDSWVDGD NCGNCTCKSG 

       310        320        330        340        350        360 
AVECRRMSCP PLNCSPDSLP VHISGQCCKV CRPKCIYGGK VLAEGQRILT KTCRECRGGV 

       370        380        390        400        410        420 
LVKITEACPP LNCSAKDHIL PENQCCRVCP GHNFCAEAPK CGENSECKNW NTKATCECKN 

       430        440        450        460        470        480 
GYISVQGNSA YCEDIDECAA KMHYCHANTV CVNLPGLYRC DCVPGYIRVD DFSCTEHDDC 

       490        500        510        520        530        540 
GSGQHNCDKN AICTNTVQGH SCTCQPGYVG NGTICKAFCE EGCRYGGTCV APNKCVCPSG 

       550        560        570        580        590        600 
FTGSHCEKDI DECAEGFVEC HNYSRCVNLP GWYHCECRSG FHDDGTYSLS GESCIDIDEC 

       610        620        630        640        650        660 
ALRTHTCWND SACINLAGGF DCLCPSGPSC SGDCPHEGGL KHNGQVWILR EDRCSVCSCK 

       670        680        690        700        710        720 
DGKIFCRRTA CDCQNPNVDL FCCPECDTRV TSQCLDQSGQ KLYRSGDNWT HSCQQCRCLE 

       730        740        750        760        770        780 
GEADCWPLAC PSLGCEYTAM FEGECCPRCV SDPCLAGNIA YDIRKTCLDS FGVSRLSGAV 

       790        800        810 
WTMAGSPCTT CKCKNGRVCC SVDLECIENN

« Hide

References

[1]"Biochemical characterization and expression analysis of neural thrombospondin-1-like proteins NELL1 and NELL2."
Kuroda S., Oyasu M., Kawakami M., Kanayama N., Tanizawa K., Saito N., Abe T., Matsuhashi S., Ting K.
Biochem. Biophys. Res. Commun. 265:79-86(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U48246 mRNA. Translation: AAC72252.1.
IPIIPI00210166.
PIRT10756.
RefSeqNP_112331.1. NM_031069.1.
UniGeneRn.10695.

3D structure databases

ProteinModelPortalQ62919.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021340.

PTM databases

PhosphoSiteQ62919.

Proteomic databases

PaxDbQ62919.
PRIDEQ62919.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81733.
KEGGrno:81733.
UCSCRGD:620998. rat.

Organism-specific databases

CTD4745.
RGD620998. Nell1.

Phylogenomic databases

eggNOGNOG253557.
HOGENOMHOG000217920.
HOVERGENHBG004805.
OrthoDBEOG4M0F11.

Gene expression databases

ArrayExpressQ62919.
GenevestigatorQ62919.
GermOnlineENSRNOG00000015675. Rattus norvegicus.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
IPR001791. Laminin_G.
IPR001007. VWF_C.
[Graphical view]
PfamPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
PF12661. hEGF. 1 hit.
PF02210. Laminin_G_2. 1 hit.
PF00093. VWC. 2 hits.
[Graphical view]
SMARTSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
SM00214. VWC. 4 hits.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 3 hits.
PS50025. LAM_G_DOMAIN. False negative.
PS01208. VWFC_1. 2 hits.
PS50184. VWFC_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio615404.

Entry information

Entry nameNELL1_RAT
AccessionPrimary (citable) accession number: Q62919
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: April 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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