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Q96CW9

- NTNG2_HUMAN

UniProt

Q96CW9 - NTNG2_HUMAN

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Protein

Netrin-G2

Gene

NTNG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites.1 Publication

GO - Biological processi

  1. axonogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Netrin-G2
Alternative name(s):
Laminet-2
Gene namesi
Name:NTNG2
Synonyms:KIAA1857, LMNT2
ORF Names:UNQ9381/PRO34206
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:14288. NTNG2.

Subcellular locationi

Cell membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication; Extracellular side 1 Publication

GO - Cellular componenti

  1. anchored component of plasma membrane Source: UniProtKB
  2. axon Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134962540.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 507490Netrin-G2PRO_0000017095Add
BLAST
Propeptidei508 – 53023Removed in mature formSequence AnalysisPRO_0000017096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 391 Publication
Disulfide bondi61 ↔ 811 Publication
Disulfide bondi69 ↔ 771 Publication
Glycosylationi122 – 1221N-linked (GlcNAc...)1 Publication
Glycosylationi128 – 1281N-linked (GlcNAc...)1 Publication
Disulfide bondi171 ↔ 1951 Publication
Disulfide bondi287 ↔ 2961 Publication
Disulfide bondi289 ↔ 3051 Publication
Disulfide bondi307 ↔ 3161 Publication
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi319 ↔ 3441 Publication
Disulfide bondi353 ↔ 362Sequence Analysis
Disulfide bondi355 ↔ 373Sequence Analysis
Disulfide bondi376 ↔ 385Sequence Analysis
Disulfide bondi388 ↔ 406Sequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi409 ↔ 421Sequence Analysis
Disulfide bondi411 ↔ 427Sequence Analysis
Glycosylationi422 – 4221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi429 ↔ 438Sequence Analysis
Disulfide bondi441 ↔ 451Sequence Analysis
Disulfide bondi456 ↔ 469By similarity
Disulfide bondi463 ↔ 475By similarity
Disulfide bondi477 ↔ 486By similarity
Lipidationi507 – 5071GPI-anchor amidated glycineSequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ96CW9.
PRIDEiQ96CW9.

PTM databases

PhosphoSiteiQ96CW9.

Expressioni

Gene expression databases

BgeeiQ96CW9.
CleanExiHS_NTNG2.
GenevestigatoriQ96CW9.

Interactioni

Subunit structurei

Interacts with LRRC4.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRC4Q9HBW14EBI-750795,EBI-7444327
LRRC4CQ9HCJ22EBI-750795,EBI-3925442

Protein-protein interaction databases

BioGridi124157. 2 interactions.
IntActiQ96CW9. 4 interactions.
MINTiMINT-7969778.
STRINGi9606.ENSP00000376921.

Structurei

Secondary structure

1
530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 287Combined sources
Beta strandi31 – 366Combined sources
Helixi46 – 494Combined sources
Beta strandi51 – 566Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 733Combined sources
Turni74 – 763Combined sources
Beta strandi79 – 813Combined sources
Beta strandi83 – 853Combined sources
Turni86 – 883Combined sources
Helixi92 – 954Combined sources
Beta strandi107 – 1093Combined sources
Turni113 – 1164Combined sources
Beta strandi121 – 13313Combined sources
Beta strandi137 – 1437Combined sources
Beta strandi147 – 15610Combined sources
Beta strandi162 – 1709Combined sources
Helixi171 – 1755Combined sources
Helixi182 – 1843Combined sources
Helixi187 – 1893Combined sources
Turni198 – 2047Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi210 – 2134Combined sources
Helixi216 – 2238Combined sources
Turni224 – 2274Combined sources
Helixi230 – 23910Combined sources
Helixi243 – 2464Combined sources
Beta strandi248 – 25811Combined sources
Helixi271 – 2733Combined sources
Beta strandi277 – 2826Combined sources
Beta strandi284 – 2874Combined sources
Beta strandi296 – 2994Combined sources
Beta strandi302 – 3054Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi324 – 3263Combined sources
Turni336 – 3383Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TBDX-ray1.80A18-349[»]
3ZYGX-ray2.20A/B1-345[»]
3ZYIX-ray2.60B1-345[»]
ProteinModelPortaliQ96CW9.
SMRiQ96CW9. Positions 18-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 286252Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini287 – 34660Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini353 – 40856Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini409 – 45345Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 8820NGL discriminant loop IAdd
BLAST
Regioni201 – 2033NGL discriminant loop II
Regioni264 – 2674NGL discriminant loop III

Domaini

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.

Sequence similaritiesi

Contains 3 laminin EGF-like domains.CuratedPROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG286598.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000231614.
HOVERGENiHBG052676.
InParanoidiQ96CW9.
KOiK16359.
OrthoDBiEOG7HQN7W.
PhylomeDBiQ96CW9.
TreeFamiTF333945.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 3 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
SM00180. EGF_Lam. 3 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96CW9-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MLHLLALFLH CLPLASGDYD ICKSWVTTDE GPTWEFYACQ PKVMRLKDYV
60 70 80 90 100
KVKVEPSGIT CGDPPERFCS HENPYLCSNE CDASNPDLAH PPRLMFDKEE
110 120 130 140 150
EGLATYWQSI TWSRYPSPLE ANITLSWNKT VELTDDVVMT FEYGRPTVMV
160 170 180 190 200
LEKSLDNGRT WQPYQFYAED CMEAFGMSAR RARDMSSSSA HRVLCTEEYS
210 220 230 240 250
RWAGSKKEKH VRFEVRDRFA IFAGPDLRNM DNLYTRLESA KGLKEFFTLT
260 270 280 290 300
DLRMRLLRPA LGGTYVQREN LYKYFYAISN IEVIGRCKCN LHANLCSMRE
310 320 330 340 350
GSLQCECEHN TTGPDCGKCK KNFRTRSWRA GSYLPLPHGS PNACATAGSF
360 370 380 390 400
GNCECYGHSN RCSYIDFLNV VTCVSCKHNT RGQHCQHCRL GYYRNGSAEL
410 420 430 440 450
DDENVCIECN CNQIGSVHDR CNETGFCECR EGAAGPKCDD CLPTHYWRQG
460 470 480 490 500
CYPNVCDDDQ LLCQNGGTCL QNQRCACPRG YTGVRCEQPR CDPADDDGGL
510 520 530
DCDRAPGAAP RPATLLGCLL LLGLAARLGR
Length:530
Mass (Da):59,799
Last modified:January 11, 2011 - v2
Checksum:iB93A8A7E0E5A8CA3
GO
Isoform 2 (identifier: Q96CW9-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:422
Mass (Da):47,491
Checksum:i9A4B38913B097AF9
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti346 – 3461T → A.3 Publications
Corresponds to variant rs4962173 [ dbSNP | Ensembl ].
VAR_047847

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei352 – 42271NCECY…HDRCN → TLQTPPPGRSPSALRGSRRG LANVKEPAGSRPQISEMLLG CTVTLHQGSVGPHIPPKLSL PDPGGPWLGSQ in isoform 2. 1 PublicationVSP_013147Add
BLAST
Alternative sequencei423 – 530108Missing in isoform 2. 1 PublicationVSP_013148Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6946.1. [Q96CW9-1]
RefSeqiNP_115925.2. NM_032536.2. [Q96CW9-1]
UniGeneiHs.163642.

Genome annotation databases

GeneIDi84628.
KEGGihsa:84628.
UCSCiuc004cbh.2. human. [Q96CW9-1]

Polymorphism databases

DMDMi317373402.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS6946.1. [Q96CW9-1 ]
RefSeqi NP_115925.2. NM_032536.2. [Q96CW9-1 ]
UniGenei Hs.163642.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TBD X-ray 1.80 A 18-349 [» ]
3ZYG X-ray 2.20 A/B 1-345 [» ]
3ZYI X-ray 2.60 B 1-345 [» ]
ProteinModelPortali Q96CW9.
SMRi Q96CW9. Positions 18-499.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124157. 2 interactions.
IntActi Q96CW9. 4 interactions.
MINTi MINT-7969778.
STRINGi 9606.ENSP00000376921.

PTM databases

PhosphoSitei Q96CW9.

Polymorphism databases

DMDMi 317373402.

Proteomic databases

PaxDbi Q96CW9.
PRIDEi Q96CW9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 84628.
KEGGi hsa:84628.
UCSCi uc004cbh.2. human. [Q96CW9-1 ]

Organism-specific databases

CTDi 84628.
GeneCardsi GC09P135037.
H-InvDB HIX0008489.
HGNCi HGNC:14288. NTNG2.
neXtProti NX_Q96CW9.
PharmGKBi PA134962540.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG286598.
GeneTreei ENSGT00760000118860.
HOGENOMi HOG000231614.
HOVERGENi HBG052676.
InParanoidi Q96CW9.
KOi K16359.
OrthoDBi EOG7HQN7W.
PhylomeDBi Q96CW9.
TreeFami TF333945.

Miscellaneous databases

GeneWikii NTNG2.
GenomeRNAii 84628.
NextBioi 74534.
PROi Q96CW9.

Gene expression databases

Bgeei Q96CW9.
CleanExi HS_NTNG2.
Genevestigatori Q96CW9.

Family and domain databases

InterProi IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00053. Laminin_EGF. 3 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00181. EGF. 1 hit.
SM00180. EGF_Lam. 3 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi PS00022. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: BrainImported.
  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. 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.
    , 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 glandImported.
  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.

Entry informationi

Entry nameiNTNG2_HUMAN
AccessioniPrimary (citable) accession number: Q96CW9
Secondary accession number(s): Q5JUJ2, Q6UXY0, Q96JH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: January 11, 2011
Last modified: November 26, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3