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Protein

Noelin-2

Gene

Olfm2

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

Functioni

Involved in transforming growth factor beta (TGF-beta)-induced smooth muscle differentiation (By similarity). TGF-beta induces expression and nuclear translocation of OLFM2 where it binds to SRF, causing its dissociation from the transcriptional repressor HEY2/HERP1 and facilitating binding of SRF to target genes (By similarity). Plays a role in AMPAR complex organization (PubMed:25218043).By similarity1 Publication

GO - Biological processi

  • locomotory behavior Source: MGI
  • positive regulation of smooth muscle cell differentiation Source: UniProtKB
  • protein secretion Source: MGI
  • visual perception Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Noelin-2
Alternative name(s):
Olfactomedin-2
Gene namesi
Name:Olfm2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:3045350. Olfm2.

Subcellular locationi

  • Secreted By similarity
  • Cell junctionsynapse 1 Publication1 Publication
  • Membrane 1 Publication
  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Nuclear localization is induced by TGF-beta.By similarity

GO - Cellular componenti

  • AMPA glutamate receptor complex Source: MGI
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • extracellular region Source: MGI
  • nucleus Source: UniProtKB
  • synaptic membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane, Nucleus, Secreted, Synapse

Pathology & Biotechi

Disruption phenotypei

No gross abnormalities with normal lifespan but mutants display reduced exploration, locomotion and olfactory sensitivity, reduced amplitude of the first negative wave in the visual evoked potential test, abnormal motor coordination, anxiety-related behavior and changes in AMPAR complex composition.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414By similarityAdd
BLAST
Chaini15 – 448434Noelin-2PRO_0000020079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence analysis
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence analysis
Disulfide bondi189 ↔ 371PROSITE-ProRule annotation
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence analysis
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence analysis
Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence analysis
Glycosylationi435 – 4351N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8BM13.
PaxDbiQ8BM13.
PeptideAtlasiQ8BM13.
PRIDEiQ8BM13.

PTM databases

PhosphoSiteiQ8BM13.

Expressioni

Tissue specificityi

Expressed in the brain (at protein level) (PubMed:22632720). In the developing eye, first detected at 12 dpc in the retinal pigmented epithelium and preferentially expressed in differentiating retinal ganglion cells between 15 and 18 dpc (PubMed:21228389). In the brain, expression is detected mainly in the olfactory bulb, cortex, piriform cortex, olfactory trabeculae, and inferior and superior colliculus (PubMed:25218043). In the adult eye, expression is detected mainly in retinal ganglion cells (PubMed:25218043).3 Publications

Developmental stagei

During embryonic eye development, first detected at 12 dpc with maximum levels at 19.5 dpc and down-regulation of expression postnatally. In brain, levels increase from 13.5 dpc to postnatal day 6 and decrease in the adult.1 Publication

Gene expression databases

BgeeiQ8BM13.
CleanExiMM_OLFM2.
GenevisibleiQ8BM13. MM.

Interactioni

Subunit structurei

Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including OLFM2. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing (PubMed:22632720). Interacts with GRIA2 (PubMed:25218043). Interacts with OLFM1 and OLFM3 (By similarity). Interacts with SRF; the interaction promotes dissociation of SRF from the transcriptional repressor HEY2 (By similarity).By similarity2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034692.

Structurei

3D structure databases

ProteinModelPortaliQ8BM13.
SMRiQ8BM13. Positions 187-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini188 – 440253Olfactomedin-likePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili52 – 7928Sequence analysisAdd
BLAST
Coiled coili130 – 18758Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiENOG410INP8. Eukaryota.
ENOG410ZRHT. LUCA.
GeneTreeiENSGT00760000119005.
HOGENOMiHOG000232069.
HOVERGENiHBG006513.
InParanoidiQ8BM13.
OMAiFAYYTNT.
OrthoDBiEOG75F4CZ.
TreeFamiTF315964.

Family and domain databases

InterProiIPR031219. Noelin-2.
IPR022082. Noelin_dom.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR23192:SF27. PTHR23192:SF27. 1 hit.
PfamiPF12308. Noelin-1. 1 hit.
PF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
PROSITEiPS51132. OLF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BM13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKLRQTGTT IAGGQTLFQS PEEGWQLYTS AQAPDGKCVC TAVIPAQSTC
60 70 80 90 100
ARDGRSRELR QLMEKVQNVS QSMEVLELRT FRDLQYVRSM ETLMRSLDAR
110 120 130 140 150
LRAADGSVSA KSFQELKDRM TELLPLSSVL EQYKADTRTI VRLREEVRNL
160 170 180 190 200
SGNLAAIQEE MGAYGYEDLQ QRVMALEARL HACAQKLGCG KLTGVSNPIT
210 220 230 240 250
IRAMGSRFGS WMTDTMAPSA DSRVWYMDGY YKGRRVLEFR TLGDFIKGQN
260 270 280 290 300
FIQHLLPQPW AGTGHVVYNG SLFYNKYQSN VVVKYHFRSR SVLVQRSLPG
310 320 330 340 350
AGYNNTFPYS WGGFSDMDFM VDESGLWAVY TTNQNAGNIV VSRLDPHTLE
360 370 380 390 400
VVRSWDTGYP KRSAGEAFMI CGVLYVTNSH LAGAKVYFAY FTNTSSYEYT
410 420 430 440
DVPFHNQYSH ISMLDYNPRE RALYTWNNGH QVLYNVTLFH VISTAGDP
Length:448
Mass (Da):50,720
Last modified:July 27, 2011 - v2
Checksum:iC29ADDE209697A5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti405 – 4051H → N in BAC29750 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037199 mRNA. Translation: BAC29750.1.
CH466522 Genomic DNA. Translation: EDL25128.1.
BC115981 mRNA. Translation: AAI15982.1.
BC117536 mRNA. Translation: AAI17537.1.
CCDSiCCDS40546.1.
RefSeqiNP_776138.2. NM_173777.3.
UniGeneiMm.293552.

Genome annotation databases

EnsembliENSMUST00000034692; ENSMUSP00000034692; ENSMUSG00000032172.
GeneIDi244723.
KEGGimmu:244723.
UCSCiuc009oje.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037199 mRNA. Translation: BAC29750.1.
CH466522 Genomic DNA. Translation: EDL25128.1.
BC115981 mRNA. Translation: AAI15982.1.
BC117536 mRNA. Translation: AAI17537.1.
CCDSiCCDS40546.1.
RefSeqiNP_776138.2. NM_173777.3.
UniGeneiMm.293552.

3D structure databases

ProteinModelPortaliQ8BM13.
SMRiQ8BM13. Positions 187-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034692.

PTM databases

PhosphoSiteiQ8BM13.

Proteomic databases

MaxQBiQ8BM13.
PaxDbiQ8BM13.
PeptideAtlasiQ8BM13.
PRIDEiQ8BM13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034692; ENSMUSP00000034692; ENSMUSG00000032172.
GeneIDi244723.
KEGGimmu:244723.
UCSCiuc009oje.1. mouse.

Organism-specific databases

CTDi93145.
MGIiMGI:3045350. Olfm2.

Phylogenomic databases

eggNOGiENOG410INP8. Eukaryota.
ENOG410ZRHT. LUCA.
GeneTreeiENSGT00760000119005.
HOGENOMiHOG000232069.
HOVERGENiHBG006513.
InParanoidiQ8BM13.
OMAiFAYYTNT.
OrthoDBiEOG75F4CZ.
TreeFamiTF315964.

Miscellaneous databases

PROiQ8BM13.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BM13.
CleanExiMM_OLFM2.
GenevisibleiQ8BM13. MM.

Family and domain databases

InterProiIPR031219. Noelin-2.
IPR022082. Noelin_dom.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR23192:SF27. PTHR23192:SF27. 1 hit.
PfamiPF12308. Noelin-1. 1 hit.
PF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
PROSITEiPS51132. OLF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Skin.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
  4. "Olfactomedin 2: expression in the eye and interaction with other olfactomedin domain-containing proteins."
    Sultana A., Nakaya N., Senatorov V.V., Tomarev S.I.
    Invest. Ophthalmol. Vis. Sci. 52:2584-2592(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "High-resolution proteomics unravel architecture and molecular diversity of native AMPA receptor complexes."
    Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S., Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U., Fakler B.
    Neuron 74:621-633(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Deletion of olfactomedin 2 induces changes in the AMPA receptor complex and impairs visual, olfactory, and motor functions in mice."
    Sultana A., Nakaya N., Dong L., Abu-Asab M., Qian H., Tomarev S.I.
    Exp. Neurol. 261:802-811(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GRIA2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiNOE2_MOUSE
AccessioniPrimary (citable) accession number: Q8BM13
Secondary accession number(s): Q0VFZ0, Q0VG58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.