Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96CW9 (NTNG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Netrin-G2
Alternative name(s):
Laminet-2
Gene names
Name:NTNG2
Synonyms:KIAA1857, LMNT2
ORF Names:UNQ9381/PRO34206
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites. Ref.6

Subunit structure

Interacts with LRRC4 By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor; Extracellular side Ref.6.

Domain

The laminin N-terminal domain mediates 1:1 binding to NGL ligand with sub-micromolar affinity. Three NGL-binding loops mediate discrimination for LRRC4C/NGL1 among other NGLs by binding specifically to its LRR repeats. This specificity drives the sorting of a mixed population of molecules into discrete cell surface subdomains.

Post-translational modification

N-glycosylated By similarity. Ref.7 UniProtKB Q8R4F1

Sequence similarities

Contains 3 laminin EGF-like domains.

Contains 1 laminin N-terminal domain.

Sequence caution

The sequence BAB47486.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRC4Q9HBW14EBI-750795,EBI-7444327
LRRC4CQ9HCJ22EBI-750795,EBI-3925442

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96CW9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96CW9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     352-422: NCECYGHSNR...QIGSVHDRCN → TLQTPPPGRS...DPGGPWLGSQ
     423-530: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 507490Netrin-G2
PRO_0000017095
Propeptide508 – 53023Removed in mature form Potential
PRO_0000017096

Regions

Domain35 – 286252Laminin N-terminal
Domain287 – 34660Laminin EGF-like 1
Domain353 – 40856Laminin EGF-like 2
Domain409 – 45345Laminin EGF-like 3
Region69 – 8820NGL discriminant loop I
Region201 – 2033NGL discriminant loop II
Region264 – 2674NGL discriminant loop III

Amino acid modifications

Lipidation5071GPI-anchor amidated glycine Potential
Glycosylation1221N-linked (GlcNAc...) Ref.7
Glycosylation1281N-linked (GlcNAc...) Ref.7
Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential
Disulfide bond22 ↔ 39 Ref.7
Disulfide bond61 ↔ 81 Ref.7
Disulfide bond69 ↔ 77 Ref.7
Disulfide bond171 ↔ 195 Ref.7
Disulfide bond287 ↔ 296 Ref.7
Disulfide bond289 ↔ 305 Ref.7
Disulfide bond307 ↔ 316 Ref.7
Disulfide bond319 ↔ 344 Ref.7
Disulfide bond353 ↔ 362 Potential
Disulfide bond355 ↔ 373 Potential
Disulfide bond376 ↔ 385 Potential
Disulfide bond388 ↔ 406 Potential
Disulfide bond409 ↔ 421 Potential
Disulfide bond411 ↔ 427 Potential
Disulfide bond429 ↔ 438 Potential
Disulfide bond441 ↔ 451 Potential
Disulfide bond456 ↔ 469 By similarity
Disulfide bond463 ↔ 475 By similarity
Disulfide bond477 ↔ 486 By similarity

Natural variations

Alternative sequence352 – 42271NCECY…HDRCN → TLQTPPPGRSPSALRGSRRG LANVKEPAGSRPQISEMLLG CTVTLHQGSVGPHIPPKLSL PDPGGPWLGSQ in isoform 2.
VSP_013147
Alternative sequence423 – 530108Missing in isoform 2.
VSP_013148
Natural variant3461T → A. Ref.1 Ref.3 Ref.5
Corresponds to variant rs4962173 [ dbSNP | Ensembl ].
VAR_047847

Secondary structure

.................................................................... 530
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: B93A8A7E0E5A8CA3

FASTA53059,799
        10         20         30         40         50         60 
MLHLLALFLH CLPLASGDYD ICKSWVTTDE GPTWEFYACQ PKVMRLKDYV KVKVEPSGIT 

        70         80         90        100        110        120 
CGDPPERFCS HENPYLCSNE CDASNPDLAH PPRLMFDKEE EGLATYWQSI TWSRYPSPLE 

       130        140        150        160        170        180 
ANITLSWNKT VELTDDVVMT FEYGRPTVMV LEKSLDNGRT WQPYQFYAED CMEAFGMSAR 

       190        200        210        220        230        240 
RARDMSSSSA HRVLCTEEYS RWAGSKKEKH VRFEVRDRFA IFAGPDLRNM DNLYTRLESA 

       250        260        270        280        290        300 
KGLKEFFTLT DLRMRLLRPA LGGTYVQREN LYKYFYAISN IEVIGRCKCN LHANLCSMRE 

       310        320        330        340        350        360 
GSLQCECEHN TTGPDCGKCK KNFRTRSWRA GSYLPLPHGS PNACATAGSF GNCECYGHSN 

       370        380        390        400        410        420 
RCSYIDFLNV VTCVSCKHNT RGQHCQHCRL GYYRNGSAEL DDENVCIECN CNQIGSVHDR 

       430        440        450        460        470        480 
CNETGFCECR EGAAGPKCDD CLPTHYWRQG CYPNVCDDDQ LLCQNGGTCL QNQRCACPRG 

       490        500        510        520        530 
YTGVRCEQPR CDPADDDGGL DCDRAPGAAP RPATLLGCLL LLGLAARLGR 

« Hide

Isoform 2 [UniParc].

Checksum: 9A4B38913B097AF9
Show »

FASTA42247,491

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-346.
Tissue: Brain.
[2]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ALA-346.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-346.
Tissue: Adrenal gland.
[6]"Structural basis for cell surface patterning through NetrinG-NGL interactions."
Seiradake E., Coles C.H., Perestenko P.V., Harlos K., McIlhinney R.A., Aricescu A.R., Jones E.Y.
EMBO J. 30:4479-4488(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-345 ALONE AND IN COMPLEX WITH LRRC4, FUNCTION, SUBCELLULAR LOCATION.
[7]"Crystal structure of the ligand binding domain of netrin G2."
Brasch J., Harrison O.J., Ahlsen G., Liu Q., Shapiro L.
J. Mol. Biol. 414:723-734(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-349, DISULFIDE BONDS, GLYCOSYLATION AT ASN-122 AND ASN-128.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB058760 mRNA. Translation: BAB47486.2. Different initiation.
AY358165 mRNA. Translation: AAQ88532.1.
AL353631, AL159997 Genomic DNA. Translation: CAI16125.1.
AL159997, AL353631 Genomic DNA. Translation: CAI40856.1.
BC013770 mRNA. Translation: AAH13770.1.
RefSeqNP_115925.2. NM_032536.2.
UniGeneHs.163642.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TBDX-ray1.80A18-349[»]
3ZYGX-ray2.20A/B1-345[»]
3ZYIX-ray2.60B1-345[»]
ProteinModelPortalQ96CW9.
SMRQ96CW9. Positions 18-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124157. 2 interactions.
IntActQ96CW9. 4 interactions.
MINTMINT-7969778.
STRING9606.ENSP00000376921.

PTM databases

PhosphoSiteQ96CW9.

Polymorphism databases

DMDM317373402.

Proteomic databases

PaxDbQ96CW9.
PRIDEQ96CW9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372179; ENSP00000361252; ENSG00000196358. [Q96CW9-2]
ENST00000393229; ENSP00000376921; ENSG00000196358. [Q96CW9-1]
GeneID84628.
KEGGhsa:84628.
UCSCuc004cbh.2. human. [Q96CW9-1]

Organism-specific databases

CTD84628.
GeneCardsGC09P135037.
H-InvDBHIX0008489.
HGNCHGNC:14288. NTNG2.
neXtProtNX_Q96CW9.
PharmGKBPA134962540.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG286598.
HOGENOMHOG000231614.
HOVERGENHBG052676.
KOK16359.
OrthoDBEOG7HQN7W.
PhylomeDBQ96CW9.
TreeFamTF333945.

Gene expression databases

ArrayExpressQ96CW9.
BgeeQ96CW9.
CleanExHS_NTNG2.
GenevestigatorQ96CW9.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00053. Laminin_EGF. 3 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 1 hit.
SM00180. EGF_Lam. 3 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 3 hits.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01248. EGF_LAM_1. 2 hits.
PS50027. EGF_LAM_2. 3 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNTNG2.
GenomeRNAi84628.
NextBio74534.
PROQ96CW9.

Entry information

Entry nameNTNG2_HUMAN
AccessionPrimary (citable) accession number: Q96CW9
Secondary accession number(s): Q5JUJ2, Q6UXY0, Q96JH0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM