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Protein

Neuroplastin

Gene

Nptn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroplastin
Alternative name(s):
Stromal cell-derived receptor 1
Short name:
SDR-1
Gene namesi
Name:Nptn
Synonyms:Sdfr1, Sdr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:108077. Nptn.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 338310ExtracellularSequence analysisAdd
BLAST
Transmembranei339 – 35921HelicalSequence analysisAdd
BLAST
Topological domaini360 – 39738CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828By similarityAdd
BLAST
Chaini29 – 397369NeuroplastinPRO_0000394471Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 116PROSITE-ProRule annotation
Disulfide bondi169 ↔ 217PROSITE-ProRule annotation
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence analysis
Glycosylationi186 – 1861N-linked (GlcNAc...); atypical1 Publication
Glycosylationi196 – 1961N-linked (GlcNAc...)1 Publication
Glycosylationi199 – 1991N-linked (GlcNAc...); atypical1 Publication
Glycosylationi228 – 2281N-linked (GlcNAc...)2 Publications
Disulfide bondi258 ↔ 315PROSITE-ProRule annotation
Glycosylationi275 – 2751N-linked (GlcNAc...); atypical2 Publications
Glycosylationi283 – 2831N-linked (GlcNAc...)3 Publications
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP97300.
MaxQBiP97300.
PaxDbiP97300.
PRIDEiP97300.

PTM databases

PhosphoSiteiP97300.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are widely expressed with variable levels in brain. Isoform 1 is expressed in cerebellum and midbrain. Isoform 1 and isoform 2 are expressed in cerebral cortex, hipoccampus and striatum. Isoform 2 is more abundant in the cerebral cortex than isoform 1.2 Publications

Gene expression databases

BgeeiP97300.
CleanExiMM_NPTN.
ExpressionAtlasiP97300. baseline and differential.
GenevisibleiP97300. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiP97300. 4 interactions.
MINTiMINT-4106313.
STRINGi10090.ENSMUSP00000082793.

Structurei

3D structure databases

ProteinModelPortaliP97300.
SMRiP97300. Positions 31-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 134106Ig-like 1Add
BLAST
Domaini148 – 23487Ig-like 2Add
BLAST
Domaini237 – 32791Ig-like 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 16113Narpin; mediates binding with FGFR1 and has antidepressant-like activityBy similarityAdd
BLAST

Domaini

Some isoforms lack the first Ig-like domain which may confer homophilic adhesion activity. However, they can bind and activate FGFR1 (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJET. Eukaryota.
ENOG4111V1Q. LUCA.
GeneTreeiENSGT00390000010516.
HOGENOMiHOG000263411.
HOVERGENiHBG008120.
InParanoidiP97300.
OMAiTINTAYG.
OrthoDBiEOG7V1FQN.
PhylomeDBiP97300.
TreeFamiTF326759.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR027112. Neuroplastin.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
[Graphical view]
PANTHERiPTHR10075:SF5. PTHR10075:SF5. 1 hit.
PIRSFiPIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P97300-2) [UniParc]FASTAAdd to basket

Also known as: SDR-1beta

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
MSGSSLPGAL ALSLLLVSGS LLPGPGAAQN AGFVKSPMSE TKLTGDAFEL
60 70 80 90 100
YCDVVGSPTP EIQWWYAEVN RAESFRQLWD GARKRRVTVN TAYGSNGVSV
110 120 130 140 150
LRITRLTLED SGTYECRASN DPKRNDLRQN PSITWIRAQA TISVLQKPRI
160 170 180 190 200
VTSEEVIIRE SLLPVTLQCN LTSSSHTLMY SYWTRNGVEL TATRKNASNM
210 220 230 240 250
EYRINKPRAE DSGEYHCVYH FVSAPKANAT IEVKAAPDIT GHKRSENKNE
260 270 280 290 300
GQDAMMYCKS VGYPHPEWIW RKKENGVFEE ISNSSGRFFI TNKENYTELS
310 320 330 340 350
IVNLQITEDP GEYECNATNS IGSASVSTVL RVRSHLAPLW PFLGILAEII
360 370 380 390
ILVVIIVVYE KRKRPDEVPD DDEPAGPMKT NSTNNHKDKN LRQRNTN
Length:397
Mass (Da):44,373
Last modified:June 15, 2010 - v3
Checksum:iE9C19EE0BD3A324A
GO
Isoform 1 (identifier: P97300-1) [UniParc]FASTAAdd to basket

Also known as: SDR-1alpha

The sequence of this isoform differs from the canonical sequence as follows:
     31-147: AGFVKSPMSE...AQATISVLQK → E

Show »
Length:281
Mass (Da):31,277
Checksum:iEA6ABF19E5A916EF
GO
Isoform 3 (identifier: P97300-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-147: AGFVKSPMSE...AQATISVLQK → E
     371-374: Missing.

Show »
Length:277
Mass (Da):30,821
Checksum:i386D78C9AADDF437
GO
Isoform 4 (identifier: P97300-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-226: Missing.
     227-235: ANATIEVKA → MSVVDLPNS

Note: No experimental confirmation available.
Show »
Length:171
Mass (Da):19,359
Checksum:iDDE5FE3CA8C948A5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451S → C in BAE32261 (PubMed:16141072).Curated
Sequence conflicti246 – 2461E → R in BAC35855 (PubMed:16141072).Curated
Sequence conflicti386 – 3861H → P in BAA09054 (PubMed:8938438).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 226226Missing in isoform 4. 1 PublicationVSP_039254Add
BLAST
Alternative sequencei31 – 147117AGFVK…SVLQK → E in isoform 1 and isoform 3. 2 PublicationsVSP_039255Add
BLAST
Alternative sequencei227 – 2359ANATIEVKA → MSVVDLPNS in isoform 4. 1 PublicationVSP_039256
Alternative sequencei371 – 3744Missing in isoform 3. 1 PublicationVSP_039257

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50463 mRNA. Translation: BAA09054.1.
AK075610 mRNA. Translation: BAC35855.1.
AK076624 mRNA. Translation: BAC36420.1.
AK153930 mRNA. Translation: BAE32261.1.
CT030640 Genomic DNA. No translation available.
CCDSiCCDS23245.1. [P97300-1]
CCDS81009.1. [P97300-3]
RefSeqiNP_001280602.1. NM_001293673.1. [P97300-3]
NP_033171.2. NM_009145.2. [P97300-1]
XP_006510945.1. XM_006510882.1. [P97300-2]
XP_006510946.1. XM_006510883.1. [P97300-2]
UniGeneiMm.15125.

Genome annotation databases

EnsembliENSMUST00000085651; ENSMUSP00000082793; ENSMUSG00000032336. [P97300-1]
ENSMUST00000176250; ENSMUSP00000135250; ENSMUSG00000032336. [P97300-4]
ENSMUST00000176557; ENSMUSP00000135541; ENSMUSG00000032336. [P97300-3]
ENSMUST00000176916; ENSMUSP00000134977; ENSMUSG00000032336. [P97300-4]
ENSMUST00000177292; ENSMUSP00000135199; ENSMUSG00000032336. [P97300-2]
GeneIDi20320.
KEGGimmu:20320.
UCSCiuc009pxd.1. mouse. [P97300-1]
uc009pxe.1. mouse. [P97300-3]
uc009pxf.1. mouse. [P97300-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50463 mRNA. Translation: BAA09054.1.
AK075610 mRNA. Translation: BAC35855.1.
AK076624 mRNA. Translation: BAC36420.1.
AK153930 mRNA. Translation: BAE32261.1.
CT030640 Genomic DNA. No translation available.
CCDSiCCDS23245.1. [P97300-1]
CCDS81009.1. [P97300-3]
RefSeqiNP_001280602.1. NM_001293673.1. [P97300-3]
NP_033171.2. NM_009145.2. [P97300-1]
XP_006510945.1. XM_006510882.1. [P97300-2]
XP_006510946.1. XM_006510883.1. [P97300-2]
UniGeneiMm.15125.

3D structure databases

ProteinModelPortaliP97300.
SMRiP97300. Positions 31-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97300. 4 interactions.
MINTiMINT-4106313.
STRINGi10090.ENSMUSP00000082793.

PTM databases

PhosphoSiteiP97300.

Proteomic databases

EPDiP97300.
MaxQBiP97300.
PaxDbiP97300.
PRIDEiP97300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085651; ENSMUSP00000082793; ENSMUSG00000032336. [P97300-1]
ENSMUST00000176250; ENSMUSP00000135250; ENSMUSG00000032336. [P97300-4]
ENSMUST00000176557; ENSMUSP00000135541; ENSMUSG00000032336. [P97300-3]
ENSMUST00000176916; ENSMUSP00000134977; ENSMUSG00000032336. [P97300-4]
ENSMUST00000177292; ENSMUSP00000135199; ENSMUSG00000032336. [P97300-2]
GeneIDi20320.
KEGGimmu:20320.
UCSCiuc009pxd.1. mouse. [P97300-1]
uc009pxe.1. mouse. [P97300-3]
uc009pxf.1. mouse. [P97300-4]

Organism-specific databases

CTDi27020.
MGIiMGI:108077. Nptn.

Phylogenomic databases

eggNOGiENOG410IJET. Eukaryota.
ENOG4111V1Q. LUCA.
GeneTreeiENSGT00390000010516.
HOGENOMiHOG000263411.
HOVERGENiHBG008120.
InParanoidiP97300.
OMAiTINTAYG.
OrthoDBiEOG7V1FQN.
PhylomeDBiP97300.
TreeFamiTF326759.

Miscellaneous databases

ChiTaRSiNptn. mouse.
PROiP97300.
SOURCEiSearch...

Gene expression databases

BgeeiP97300.
CleanExiMM_NPTN.
ExpressionAtlasiP97300. baseline and differential.
GenevisibleiP97300. MM.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR027112. Neuroplastin.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
[Graphical view]
PANTHERiPTHR10075:SF5. PTHR10075:SF5. 1 hit.
PIRSFiPIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of novel secreted and membrane proteins isolated by the signal sequence trap method."
    Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M., Hamada T., Sato T., Nakano T., Honjo T.
    Genomics 37:273-280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Strain: NOD.
    Tissue: Brain, Testis and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 150-159 AND 260-271, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Isoform specific expression of the SDR-1 protein, alpha and beta in subregions of adult rodent brain."
    Lopez N.D., Kinoshita A., Taniwaki M., Tada H., Shirozu M., Nakano T., Tashiro K., Honjo T.
    Biomed. Res. 20:43-49(1999)
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
  6. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-283.
    Strain: C57BL/6J.
    Tissue: Plasma.
  7. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186; ASN-196; ASN-199; ASN-228; ASN-275 AND ASN-283.
    Tissue: Myoblast.
  8. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-228; ASN-275 AND ASN-283.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiNPTN_MOUSE
AccessioniPrimary (citable) accession number: P97300
Secondary accession number(s): Q3U519, Q8C637, Q8C6H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 15, 2010
Last modified: June 8, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.