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Protein

Noelin

Gene

Olfm1

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

Functioni

Contributes to the regulation of axonal growth in the embryonic and adult central nervous system by inhibiting interactions between RTN4R and LINGO1. Inhibits RTN4R-mediated axon growth cone collapse (PubMed:22923615). May play an important role in regulating the production of neural crest cells by the neural tube (By similarity). May be required for normal responses to olfactory stimuli (PubMed:26107991).By similarity2 Publications

GO - Molecular functioni

  • beta-amyloid binding Source: MGI

GO - Biological processi

  • atrioventricular valve formation Source: AgBase
  • cardiac epithelial to mesenchymal transition Source: AgBase
  • negative regulation of beta-amyloid formation Source: MGI
  • negative regulation of gene expression Source: AgBase
  • negative regulation of neuron migration Source: MGI
  • neuronal signal transduction Source: UniProtKB
  • positive regulation of epithelial to mesenchymal transition Source: AgBase
  • positive regulation of gene expression Source: AgBase
  • protein oligomerization Source: MGI
  • regulation of axon extension Source: UniProtKB
  • regulation of beta-amyloid formation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Noelin
Alternative name(s):
Neuronal olfactomedin-related ER localized protein
Olfactomedin-11 Publication
Pancortin1 Publication
Gene namesi
Name:Olfm1
Synonyms:Noe1, Noel, Noel1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1860437. Olfm1.

Subcellular locationi

Isoform 1 :

GO - Cellular componenti

  • AMPA glutamate receptor complex Source: MGI
  • axon Source: UniProtKB
  • axonal growth cone Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • endoplasmic reticulum Source: UniProtKB
  • extracellular space Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • perikaryon Source: UniProtKB-SubCell
  • synaptic membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Endoplasmic reticulum, Secreted, Synapse

Pathology & Biotechi

Disruption phenotypei

Females have slightly lower body weight than wild-type at birth, but strongly reduced body weight one to eight weeks after birth. Mutant females do not display normal estrus cycle responses to male odor, and have very low fertility due to a strongly decreased rate of ovulation and a low mating rate.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi479 – 485Missing : Abolishes retention in the endoplasmic reticulum so that the protein is secreted. 1 Publication7

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000002007517 – 485NoelinAdd BLAST469

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi33N-linked (GlcNAc...)Sequence analysis1
Glycosylationi103N-linked (GlcNAc...)Sequence analysis1
Glycosylationi187N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi221InterchainCombined sources1 Publication
Disulfide bondi227 ↔ 409PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi288N-linked (GlcNAc...)Sequence analysis1 Publication1
Glycosylationi307N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi394N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
Glycosylationi431N-linked (GlcNAc...)Sequence analysis1 Publication1
Glycosylationi473N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO88998.
PaxDbiO88998.
PeptideAtlasiO88998.
PRIDEiO88998.

PTM databases

PhosphoSitePlusiO88998.

Expressioni

Tissue specificityi

Expressed in the brain cortex, olfactory bulb and vomeronasal neuroepithelium (at protein level) (PubMed:9473566, PubMed:26107991, PubMed:22923615, PubMed:22632720). Detected in brain cortex, hippocampus, dorsal root ganglion and olfactory bulb (PubMed:9473566, PubMed:22923615).4 Publications

Developmental stagei

Expression increases moderately during embryonic development and remains stable in the postnatal brain (PubMed:21228389). Highly expressed in uterus luminal epithelium after embryo implantation (PubMed:26107991).2 Publications

Gene expression databases

BgeeiENSMUSG00000026833.
CleanExiMM_OLFM1.
ExpressionAtlasiO88998. baseline and differential.
GenevisibleiO88998. MM.

Interactioni

Subunit structurei

Homotetramer; disulfide-linked. Dimer of dimers, giving rise to a V-shaped homotretramer (PubMed:25903135). Isoform 1 and isoform 3 interact with RTN4R (PubMed:22923615). Identified in a complex with RTN4R and LINGO1 (PubMed:22923615). 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 OLFM1. 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 OLFM2 (By similarity).By similarity3 Publications

Protein-protein interaction databases

BioGridi207823. 1 interactor.
IntActiO88998. 1 interactor.
STRINGi10090.ENSMUSP00000028177.

Structurei

Secondary structure

1485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi212 – 225Combined sources14
Beta strandi230 – 233Combined sources4
Beta strandi237 – 241Combined sources5
Beta strandi245 – 250Combined sources6
Beta strandi262 – 266Combined sources5
Beta strandi268 – 270Combined sources3
Beta strandi273 – 279Combined sources7
Helixi280 – 285Combined sources6
Beta strandi290 – 293Combined sources4
Beta strandi298 – 301Combined sources4
Beta strandi304 – 306Combined sources3
Beta strandi309 – 314Combined sources6
Beta strandi317 – 324Combined sources8
Turni325 – 328Combined sources4
Beta strandi329 – 335Combined sources7
Beta strandi355 – 360Combined sources6
Beta strandi363 – 369Combined sources7
Turni371 – 374Combined sources4
Beta strandi375 – 382Combined sources8
Turni384 – 386Combined sources3
Beta strandi389 – 398Combined sources10
Turni399 – 401Combined sources3
Beta strandi405 – 416Combined sources12
Beta strandi418 – 421Combined sources4
Beta strandi423 – 429Combined sources7
Turni430 – 433Combined sources4
Beta strandi434 – 436Combined sources3
Beta strandi450 – 455Combined sources6
Turni456 – 459Combined sources4
Beta strandi460 – 464Combined sources5
Beta strandi466 – 476Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AMOX-ray2.40A/B17-478[»]
ProteinModelPortaliO88998.
SMRiO88998.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini226 – 478Olfactomedin-likePROSITE-ProRule annotationAdd BLAST253

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili87 – 227Sequence analysis1 PublicationAdd BLAST141

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi482 – 485Endoplasmic reticulum retention signal1 Publication4

Domaini

The protein contains a globular N-terminal tetramerization domain, a long stalk formed by the coiled coil region and a C-terminal olfactomedin-like domain. Interactions between dimers are mediated by the coiled coil region. The dimers interact mostly via the N-terminal tetramerization domain, giving rise to a V-shaped overall architecture of the tetramer.1 Publication

Sequence similaritiesi

Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiENOG410INP4. Eukaryota.
ENOG41104PB. LUCA.
GeneTreeiENSGT00760000119005.
HOVERGENiHBG006513.
InParanoidiO88998.
PhylomeDBiO88998.

Family and domain databases

InterProiIPR031217. Noelin.
IPR022082. Noelin_dom.
IPR003112. Olfac-like_dom.
IPR011044. Quino_amine_DH_bsu.
[Graphical view]
PANTHERiPTHR23192:SF34. PTHR23192:SF34. 1 hit.
PfamiPF12308. Noelin-1. 1 hit.
PF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
SUPFAMiSSF50969. SSF50969. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51132. OLF. 1 hit.
[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 1 (identifier: O88998-1) [UniParc]FASTAAdd to basket
Also known as: BMZ.Curated

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
MSVPLLKIGV VLSTMAMITN WMSQTLPSLV GLNTTRLSAA SGGTLDRSTG
60 70 80 90 100
VLPTNPEESW QVYSSAQDSE GRCICTVVAP QQTMCSRDAR TKQLRQLLEK
110 120 130 140 150
VQNMSQSIEV LDRRTQRDLQ YVEKMENQMK GLETKFKQVE ESHKQHLARQ
160 170 180 190 200
FKAIKAKMDE LRPLIPVLEE YKADAKLVLQ FKEEVQNLTS VLNELQEEIG
210 220 230 240 250
AYDYDELQSR VSNLEERLRA CMQKLACGKL TGISDPVTVK TSGSRFGSWM
260 270 280 290 300
TDPLAPEGDN RVWYMDGYHN NRFVREYKSM VDFMNTDNFT SHRLPHPWSG
310 320 330 340 350
TGQVVYNGSI YFNKFQSHII IRFDLKTEAI LKTRSLDYAG YNNMYHYAWG
360 370 380 390 400
GHSDIDLMVD ENGLWAVYAT NQNAGNIVIS KLDPVSLQIL QTWNTSYPKR
410 420 430 440 450
SAGEAFIICG TLYVTNGYSG GTKVHYAYQT NASTYEYIDI PFQNKYSHIS
460 470 480
MLDYNPKDRA LYAWNNGHQT LYNVTLFHVI RSDEL
Length:485
Mass (Da):55,398
Last modified:November 1, 1998 - v1
Checksum:i6429574ECD814944
GO
Isoform 2 (identifier: O88998-2) [UniParc]FASTAAdd to basket
Also known as: BMY.Curated

The sequence of this isoform differs from the canonical sequence as follows:
     153-153: A → G
     154-485: Missing.

Show »
Length:153
Mass (Da):17,232
Checksum:iC47571A8DCAE09E9
GO
Isoform 3 (identifier: O88998-3) [UniParc]FASTAAdd to basket
Also known as: AMZCurated

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTRLSAASGGTLDRSTG → MQPARKLLSLLVLLVMGTELTQ

Show »
Length:457
Mass (Da):52,674
Checksum:iCA2AD328E37A0F16
GO
Isoform 4 (identifier: O88998-4) [UniParc]FASTAAdd to basket
Also known as: AMYCurated

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTRLSAASGGTLDRSTG → MQPARKLLSLLVLLVMGTELTQ
     153-153: A → G
     154-485: Missing.

Show »
Length:125
Mass (Da):14,508
Checksum:i6EE703826C61DF78
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69S → M in AAB84058 (Ref. 2) Curated1
Sequence conflicti329A → M in AAB84058 (Ref. 2) Curated1
Sequence conflicti429Q → R in AAB84058 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0037621 – 50MSVPL…DRSTG → MQPARKLLSLLVLLVMGTEL TQ in isoform 3 and isoform 4. 2 PublicationsAdd BLAST50
Alternative sequenceiVSP_003763153A → G in isoform 2 and isoform 4. 1 Publication1
Alternative sequenceiVSP_003764154 – 485Missing in isoform 2 and isoform 4. 1 PublicationAdd BLAST332

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78262 mRNA. Translation: BAA28765.1.
D78263 mRNA. Translation: BAA28766.1.
D78264 mRNA. Translation: BAA28767.1.
D78265 mRNA. Translation: BAA28764.1.
AF028740 mRNA. Translation: AAB84058.1.
AK003031 mRNA. Translation: BAB22520.1.
AL731778 Genomic DNA. Translation: CAM46249.1.
CCDSiCCDS15833.1. [O88998-3]
CCDS15834.1. [O88998-1]
CCDS15835.1. [O88998-2]
RefSeqiNP_001033701.1. NM_001038612.1. [O88998-2]
NP_001033703.1. NM_001038614.1. [O88998-4]
UniGeneiMm.43278.

Genome annotation databases

EnsembliENSMUST00000102879; ENSMUSP00000099943; ENSMUSG00000026833. [O88998-2]
GeneIDi56177.
KEGGimmu:56177.
UCSCiuc008iya.1. mouse. [O88998-4]
uc008iyc.1. mouse. [O88998-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78262 mRNA. Translation: BAA28765.1.
D78263 mRNA. Translation: BAA28766.1.
D78264 mRNA. Translation: BAA28767.1.
D78265 mRNA. Translation: BAA28764.1.
AF028740 mRNA. Translation: AAB84058.1.
AK003031 mRNA. Translation: BAB22520.1.
AL731778 Genomic DNA. Translation: CAM46249.1.
CCDSiCCDS15833.1. [O88998-3]
CCDS15834.1. [O88998-1]
CCDS15835.1. [O88998-2]
RefSeqiNP_001033701.1. NM_001038612.1. [O88998-2]
NP_001033703.1. NM_001038614.1. [O88998-4]
UniGeneiMm.43278.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AMOX-ray2.40A/B17-478[»]
ProteinModelPortaliO88998.
SMRiO88998.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207823. 1 interactor.
IntActiO88998. 1 interactor.
STRINGi10090.ENSMUSP00000028177.

PTM databases

PhosphoSitePlusiO88998.

Proteomic databases

MaxQBiO88998.
PaxDbiO88998.
PeptideAtlasiO88998.
PRIDEiO88998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102879; ENSMUSP00000099943; ENSMUSG00000026833. [O88998-2]
GeneIDi56177.
KEGGimmu:56177.
UCSCiuc008iya.1. mouse. [O88998-4]
uc008iyc.1. mouse. [O88998-2]

Organism-specific databases

CTDi10439.
MGIiMGI:1860437. Olfm1.

Phylogenomic databases

eggNOGiENOG410INP4. Eukaryota.
ENOG41104PB. LUCA.
GeneTreeiENSGT00760000119005.
HOVERGENiHBG006513.
InParanoidiO88998.
PhylomeDBiO88998.

Miscellaneous databases

ChiTaRSiOlfm1. mouse.
PROiO88998.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026833.
CleanExiMM_OLFM1.
ExpressionAtlasiO88998. baseline and differential.
GenevisibleiO88998. MM.

Family and domain databases

InterProiIPR031217. Noelin.
IPR022082. Noelin_dom.
IPR003112. Olfac-like_dom.
IPR011044. Quino_amine_DH_bsu.
[Graphical view]
PANTHERiPTHR23192:SF34. PTHR23192:SF34. 1 hit.
PfamiPF12308. Noelin-1. 1 hit.
PF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
SUPFAMiSSF50969. SSF50969. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51132. OLF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNOE1_MOUSE
AccessioniPrimary (citable) accession number: O88998
Secondary accession number(s): A3KGE5
, O35429, O88999, Q91XK8, Q9QWQ9, Q9QWR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The protein structure is stabilized by calcium ions.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.