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Noelin (Neuronal olfactomedin-related ER localized protein) (Olfactomedin-1) (Pancortin)

 NOE1_MOUSE              Reviewed;         485 AA.
O88998; A3KGE5; O35429; O88999; Q91XK8; Q9QWQ9; Q9QWR0;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-SEP-2018, entry version 148.
RecName: Full=Noelin;
AltName: Full=Neuronal olfactomedin-related ER localized protein;
AltName: Full=Olfactomedin-1 {ECO:0000303|PubMed:25903135};
AltName: Full=Pancortin {ECO:0000303|PubMed:9473566};
Flags: Precursor;
Name=Olfm1; Synonyms=Noe1, Noel, Noel1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
STRAIN=ICR; TISSUE=Brain;
PubMed=9473566; DOI=10.1016/S0169-328X(97)00271-4;
Nagano T., Nakamura A., Mori Y., Maeda M., Takami T., Shiosaka S.,
Takagi H., Sato M.;
"Differentially expressed olfactomedin-related glycoproteins
(Pancortins) in the brain.";
Brain Res. Mol. Brain Res. 53:13-23(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Anholt R., Kulkarni N., Karavanich C.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
DEVELOPMENTAL STAGE.
PubMed=21228389; DOI=10.1167/iovs.10-6356;
Sultana A., Nakaya N., Senatorov V.V., Tomarev S.I.;
"Olfactomedin 2: expression in the eye and interaction with other
olfactomedin domain-containing proteins.";
Invest. Ophthalmol. Vis. Sci. 52:2584-2592(2011).
[6]
FUNCTION, INTERACTION WITH RTN4R, IDENTIFICATION IN A COMPLEX WITH
RTN4R AND LINGO1, AND SUBCELLULAR LOCATION.
PubMed=22923615; DOI=10.1074/jbc.M112.389916;
Nakaya N., Sultana A., Lee H.S., Tomarev S.I.;
"Olfactomedin 1 interacts with the Nogo A receptor complex to regulate
axon growth.";
J. Biol. Chem. 287:37171-37184(2012).
[7]
IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
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.;
"High-resolution proteomics unravel architecture and molecular
diversity of native AMPA receptor complexes.";
Neuron 74:621-633(2012).
[8]
DISRUPTION PHENOTYPE, FUNCTION, DEVELOPMENTAL STAGE, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=26107991; DOI=10.1210/en.2015-1389;
Li R., Diao H., Zhao F., Xiao S., Zowalaty A.E., Dudley E.A.,
Mattson M.P., Ye X.;
"Olfactomedin 1 deficiency leads to defective olfaction and impaired
female fertility.";
Endocrinology 2015:EN20151389-EN20151389(2015).
[9]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 211-478, STRUCTURE BY
ELECTRON MICROSCOPY, COILED COIL, DOMAIN, SUBUNIT, DISULFIDE BONDS,
GLYCOSYLATION AT ASN-307; ASN-394 AND ASN-473, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF 479-VAL--LEU-485.
PubMed=25903135; DOI=10.1074/jbc.M115.653485;
Pronker M.F., Bos T.G., Sharp T.H., Thies-Weesie D.M., Janssen B.J.;
"Olfactomedin-1 has a v-shaped disulfide-linked tetrameric
Structure.";
J. Biol. Chem. 290:15092-15101(2015).
-!- FUNCTION: 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).
{ECO:0000250|UniProtKB:Q9IAK4, ECO:0000269|PubMed:22923615,
ECO:0000269|PubMed:26107991}.
-!- SUBUNIT: 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). {ECO:0000250|UniProtKB:Q99784,
ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:22923615,
ECO:0000269|PubMed:25903135}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22923615,
ECO:0000305|PubMed:22632720}. Cell junction, synapse
{ECO:0000305|PubMed:22632720}. Endoplasmic reticulum
{ECO:0000269|PubMed:22923615}. Cell projection, axon
{ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991}.
Perikaryon {ECO:0000269|PubMed:22923615}.
-!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum
{ECO:0000269|PubMed:9473566, ECO:0000305|PubMed:25903135}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=BMZ. {ECO:0000305};
IsoId=O88998-1; Sequence=Displayed;
Name=2; Synonyms=BMY. {ECO:0000305};
IsoId=O88998-2; Sequence=VSP_003763, VSP_003764;
Name=3; Synonyms=AMZ {ECO:0000305};
IsoId=O88998-3; Sequence=VSP_003762;
Name=4; Synonyms=AMY {ECO:0000305};
IsoId=O88998-4; Sequence=VSP_003762, VSP_003763, VSP_003764;
-!- TISSUE SPECIFICITY: 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). {ECO:0000269|PubMed:22632720,
ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991,
ECO:0000269|PubMed:9473566}.
-!- DEVELOPMENTAL STAGE: 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).
{ECO:0000269|PubMed:21228389, ECO:0000269|PubMed:26107991}.
-!- DOMAIN: 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.
{ECO:0000269|PubMed:25903135}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:25903135}.
-!- MISCELLANEOUS: The protein structure is stabilized by calcium
ions. {ECO:0000269|PubMed:25903135}.
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EMBL; D78262; BAA28765.1; -; mRNA.
EMBL; D78263; BAA28766.1; -; mRNA.
EMBL; D78264; BAA28767.1; -; mRNA.
EMBL; D78265; BAA28764.1; -; mRNA.
EMBL; AF028740; AAB84058.1; -; mRNA.
EMBL; AK003031; BAB22520.1; -; mRNA.
EMBL; AL731778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS15833.1; -. [O88998-3]
CCDS; CCDS15834.1; -. [O88998-1]
CCDS; CCDS15835.1; -. [O88998-2]
RefSeq; NP_001033701.1; NM_001038612.1. [O88998-2]
RefSeq; NP_001033703.1; NM_001038614.1. [O88998-4]
UniGene; Mm.43278; -.
PDB; 5AMO; X-ray; 2.40 A; A/B=17-478.
PDBsum; 5AMO; -.
DisProt; DP00936; -.
ProteinModelPortal; O88998; -.
SMR; O88998; -.
BioGrid; 207823; 1.
CORUM; O88998; -.
IntAct; O88998; 1.
STRING; 10090.ENSMUSP00000028177; -.
iPTMnet; O88998; -.
PhosphoSitePlus; O88998; -.
MaxQB; O88998; -.
PaxDb; O88998; -.
PeptideAtlas; O88998; -.
PRIDE; O88998; -.
Ensembl; ENSMUST00000102879; ENSMUSP00000099943; ENSMUSG00000026833. [O88998-2]
GeneID; 56177; -.
KEGG; mmu:56177; -.
UCSC; uc008iya.1; mouse. [O88998-4]
UCSC; uc008iyc.1; mouse. [O88998-2]
CTD; 10439; -.
MGI; MGI:1860437; Olfm1.
eggNOG; ENOG410INP4; Eukaryota.
eggNOG; ENOG41104PB; LUCA.
GeneTree; ENSGT00760000119005; -.
HOVERGEN; HBG006513; -.
InParanoid; O88998; -.
PhylomeDB; O88998; -.
ChiTaRS; Olfm1; mouse.
PRO; PR:O88998; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026833; Expressed in 326 organ(s), highest expression level in prefrontal cortex.
CleanEx; MM_OLFM1; -.
ExpressionAtlas; O88998; baseline and differential.
Genevisible; O88998; MM.
GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0097060; C:synaptic membrane; IDA:MGI.
GO; GO:0001540; F:amyloid-beta binding; IDA:MGI.
GO; GO:0003190; P:atrioventricular valve formation; ISS:AgBase.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISS:AgBase.
GO; GO:2001223; P:negative regulation of neuron migration; IDA:MGI.
GO; GO:0023041; P:neuronal signal transduction; IDA:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
GO; GO:0051259; P:protein complex oligomerization; IDA:MGI.
GO; GO:1902003; P:regulation of amyloid-beta formation; IDA:MGI.
GO; GO:0030516; P:regulation of axon extension; IDA:UniProtKB.
InterPro; IPR031217; Noelin.
InterPro; IPR022082; Noelin_dom.
InterPro; IPR003112; Olfac-like_dom.
InterPro; IPR011044; Quino_amine_DH_bsu.
PANTHER; PTHR23192:SF34; PTHR23192:SF34; 1.
Pfam; PF12308; Noelin-1; 1.
Pfam; PF02191; OLF; 1.
SMART; SM00284; OLF; 1.
SUPFAM; SSF50969; SSF50969; 2.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS51132; OLF; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell projection;
Coiled coil; Complete proteome; Developmental protein; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Reference proteome; Secreted;
Signal; Synapse.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 485 Noelin.
/FTId=PRO_0000020075.
DOMAIN 226 478 Olfactomedin-like. {ECO:0000255|PROSITE-
ProRule:PRU00446}.
COILED 87 227 {ECO:0000255,
ECO:0000305|PubMed:25903135}.
MOTIF 482 485 Endoplasmic reticulum retention signal.
{ECO:0000305|PubMed:25903135}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000305|PubMed:25903135}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5AMO, ECO:0000255,
ECO:0000269|PubMed:25903135}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5AMO, ECO:0000255,
ECO:0000269|PubMed:25903135}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000305|PubMed:25903135}.
CARBOHYD 473 473 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5AMO, ECO:0000255,
ECO:0000269|PubMed:25903135}.
DISULFID 221 221 Interchain. {ECO:0000244|PDB:5AMO,
ECO:0000269|PubMed:25903135}.
DISULFID 227 409 {ECO:0000244|PDB:5AMO,
ECO:0000255|PROSITE-ProRule:PRU00446,
ECO:0000269|PubMed:25903135}.
VAR_SEQ 1 50 MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTRLSAAS
GGTLDRSTG -> MQPARKLLSLLVLLVMGTELTQ (in
isoform 3 and isoform 4).
{ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.2}.
/FTId=VSP_003762.
VAR_SEQ 153 153 A -> G (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_003763.
VAR_SEQ 154 485 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_003764.
MUTAGEN 479 485 Missing: Abolishes retention in the
endoplasmic reticulum so that the protein
is secreted.
{ECO:0000269|PubMed:25903135}.
CONFLICT 69 69 S -> M (in Ref. 2; AAB84058).
{ECO:0000305}.
CONFLICT 329 329 A -> M (in Ref. 2; AAB84058).
{ECO:0000305}.
CONFLICT 429 429 Q -> R (in Ref. 2; AAB84058).
{ECO:0000305}.
HELIX 212 225 {ECO:0000244|PDB:5AMO}.
STRAND 230 233 {ECO:0000244|PDB:5AMO}.
STRAND 237 241 {ECO:0000244|PDB:5AMO}.
STRAND 245 250 {ECO:0000244|PDB:5AMO}.
STRAND 262 266 {ECO:0000244|PDB:5AMO}.
STRAND 268 270 {ECO:0000244|PDB:5AMO}.
STRAND 273 279 {ECO:0000244|PDB:5AMO}.
HELIX 280 285 {ECO:0000244|PDB:5AMO}.
STRAND 290 293 {ECO:0000244|PDB:5AMO}.
STRAND 298 301 {ECO:0000244|PDB:5AMO}.
STRAND 304 306 {ECO:0000244|PDB:5AMO}.
STRAND 309 314 {ECO:0000244|PDB:5AMO}.
STRAND 317 324 {ECO:0000244|PDB:5AMO}.
TURN 325 328 {ECO:0000244|PDB:5AMO}.
STRAND 329 335 {ECO:0000244|PDB:5AMO}.
STRAND 355 360 {ECO:0000244|PDB:5AMO}.
STRAND 363 369 {ECO:0000244|PDB:5AMO}.
TURN 371 374 {ECO:0000244|PDB:5AMO}.
STRAND 375 382 {ECO:0000244|PDB:5AMO}.
TURN 384 386 {ECO:0000244|PDB:5AMO}.
STRAND 389 398 {ECO:0000244|PDB:5AMO}.
TURN 399 401 {ECO:0000244|PDB:5AMO}.
STRAND 405 416 {ECO:0000244|PDB:5AMO}.
STRAND 418 421 {ECO:0000244|PDB:5AMO}.
STRAND 423 429 {ECO:0000244|PDB:5AMO}.
TURN 430 433 {ECO:0000244|PDB:5AMO}.
STRAND 434 436 {ECO:0000244|PDB:5AMO}.
STRAND 450 455 {ECO:0000244|PDB:5AMO}.
TURN 456 459 {ECO:0000244|PDB:5AMO}.
STRAND 460 464 {ECO:0000244|PDB:5AMO}.
STRAND 466 476 {ECO:0000244|PDB:5AMO}.
SEQUENCE 485 AA; 55398 MW; 6429574ECD814944 CRC64;
MSVPLLKIGV VLSTMAMITN WMSQTLPSLV GLNTTRLSAA SGGTLDRSTG VLPTNPEESW
QVYSSAQDSE GRCICTVVAP QQTMCSRDAR TKQLRQLLEK VQNMSQSIEV LDRRTQRDLQ
YVEKMENQMK GLETKFKQVE ESHKQHLARQ FKAIKAKMDE LRPLIPVLEE YKADAKLVLQ
FKEEVQNLTS VLNELQEEIG AYDYDELQSR VSNLEERLRA CMQKLACGKL TGISDPVTVK
TSGSRFGSWM TDPLAPEGDN RVWYMDGYHN NRFVREYKSM VDFMNTDNFT SHRLPHPWSG
TGQVVYNGSI YFNKFQSHII IRFDLKTEAI LKTRSLDYAG YNNMYHYAWG GHSDIDLMVD
ENGLWAVYAT NQNAGNIVIS KLDPVSLQIL QTWNTSYPKR SAGEAFIICG TLYVTNGYSG
GTKVHYAYQT NASTYEYIDI PFQNKYSHIS MLDYNPKDRA LYAWNNGHQT LYNVTLFHVI
RSDEL


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EIAAB27475 Mouse,Mus musculus,Noe3,Noelin-3,Olfactomedin-3,Olfm3,Optimedin
EIAAB27472 Homo sapiens,Human,NOE2,Noelin-2,Olfactomedin-2,OLFM2
EIAAB27473 Homo sapiens,Human,NOE3,Noelin-3,Olfactomedin-3,OLFM3,Optimedin,UNQ1924_PRO4399
Olfm-101AP Noelin-1 Olfactomedin-1) antibodies Polyclonal anbtibody Host: Rabbit Affinity purifed 200ul
Olfm-101AP Noelin-1 Olfactomedin-1) antibodies WB control: PC-Olfm Host: Rabbit Affinity purifed 100-150ul
Olfm-101AP Noelin-1 Olfactomedin-1) antibodies Antigenic peptide: P-Olfm Host: Rabbit Affinity purifed 100ul
Olfm-101AP Noelin-1 Olfactomedin-1) antibodies FITC-conjugates: Olfm-FITC Host: Rabbit Affinity purifed 200ul
Olfm-101AP Noelin-1 Olfactomedin-1) antibodies Biotin Conjugates: Olfm-Biotin Host: Rabbit Affinity purifed 200ul
30-712 OLFM4 is a member of the olfactomedin-related protein family. The exact function of its gene has not yet been determined.This gene was originally cloned from human myeloblasts and found to be selectiv 0.1 mg
E0563p Rat ELISA Kit FOR Olfactomedin-like protein 3 96T
KS6A5_CHICK Rat ELISA Kit FOR Olfactomedin-like protein 3 96T
E6947h Human Olfactomedin Like Protein 2B ELISA Kit 96T
E7376h Human Olfactomedin Like Protein 2A ELISA Kit 96T
E6924h Human Olfactomedin Like Protein 1 ELISA Kit 96T
E0112h Bovine ELISA Kit FOR Olfactomedin-like protein 2B 96T
E0151h Bovine ELISA Kit FOR Olfactomedin-like protein 3 96T
ERD23_MOUSE Bovine ELISA Kit FOR Olfactomedin-like protein 2B 96T
UTP11_HUMAN Bovine ELISA Kit FOR Olfactomedin-like protein 2B 96T


 

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