NOE1_RAT
ID NOE1_RAT Reviewed; 485 AA.
AC Q62609; Q62606; Q62607; Q62608;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Noelin;
DE AltName: Full=1B426B;
DE AltName: Full=Neuronal olfactomedin-related ER localized protein;
DE AltName: Full=Olfactomedin-1 {ECO:0000303|PubMed:22632720};
DE AltName: Full=Pancortin {ECO:0000303|PubMed:22632720};
DE Flags: Precursor;
GN Name=Olfm1; Synonyms=D2Sut1e, Noe1, Noel, Noel1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7932877; DOI=10.1002/jnr.490380413;
RA Danielson P.E., Forss-Petter S., Battenberg E.L.F., Delecea L., Bloom F.E.,
RA Sutcliffe J.G.;
RT "Four structurally distinct neuron-specific olfactomedin-related
RT glycoproteins produced by differential promoter utilization and alternative
RT mRNA splicing from a single gene.";
RL J. Neurosci. Res. 38:468-478(1994).
RN [2]
RP IDENTIFICATION IN AMPAR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
CC -!- FUNCTION: Contributes to the regulation of axonal growth in the
CC embryonic and adult central nervous system by inhibiting interactions
CC between RTN4R and LINGO1. Inhibits RTN4R-mediated axon growth cone
CC collapse (By similarity). May play an important role in regulating the
CC production of neural crest cells by the neural tube (By similarity).
CC May be required for normal responses to olfactory stimuli (By
CC similarity). {ECO:0000250|UniProtKB:O88998,
CC ECO:0000250|UniProtKB:Q9IAK4}.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers, giving rise
CC to a V-shaped homotretramer. Isoform 1 and isoform 3 interact with
CC RTN4R. Identified in a complex with RTN4R and LINGO1 (By similarity).
CC Peripherally associated with AMPAR complex. AMPAR complex consists of
CC an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2,
CC GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold
CC symmetry. One of the two pairs of distinct binding sites is occupied
CC either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2,
CC CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is
CC complemented by outer core constituents binding directly to the
CC GluA/GRIA proteins at sites distinct from the interaction sites of the
CC inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents, including OLFM1. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing (PubMed:22632720). Interacts with
CC OLFM2 (By similarity). {ECO:0000250|UniProtKB:O88998,
CC ECO:0000250|UniProtKB:Q99784, ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O88998,
CC ECO:0000305|PubMed:22632720}. Synapse {ECO:0000250|UniProtKB:O88998,
CC ECO:0000305|PubMed:22632720}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O88998}. Cell projection, axon
CC {ECO:0000250|UniProtKB:O88998}. Perikaryon
CC {ECO:0000250|UniProtKB:O88998}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=BMZ;
CC IsoId=Q62609-1; Sequence=Displayed;
CC Name=2; Synonyms=BMY;
CC IsoId=Q62609-2; Sequence=VSP_003766, VSP_003767;
CC Name=3; Synonyms=AMZ;
CC IsoId=Q62609-3; Sequence=VSP_003765;
CC Name=4; Synonyms=AMY;
CC IsoId=Q62609-4; Sequence=VSP_003765, VSP_003766, VSP_003767;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:7932877, PubMed:22632720). Expressed in the brain,
CC predominantly in the cortex and hippocampus. In the pituitary only the
CC two A-type and in the adrenal glands only the two B-type forms were
CC detected (PubMed:7932877). {ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:7932877}.
CC -!- DOMAIN: The protein contains a globular N-terminal tetramerization
CC domain, a long stalk formed by the coiled coil region and a C-terminal
CC olfactomedin-like domain. Interactions between dimers are mediated by
CC the coiled coil region. The dimers interact mostly via the N-terminal
CC tetramerization domain, giving rise to a V-shaped overall architecture
CC of the tetramer. {ECO:0000250|UniProtKB:O88998}.
CC -!- PTM: In isoform 3 and isoform 4, the signal peptide is predicted to end
CC in position 17.
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DR EMBL; U03417; AAC04321.1; -; mRNA.
DR EMBL; U03416; AAC04320.1; -; mRNA.
DR EMBL; U03415; AAC04319.1; -; mRNA.
DR EMBL; U03414; AAC04317.1; -; mRNA.
DR PIR; I73636; I73636.
DR PIR; I73637; I73637.
DR RefSeq; NP_446025.1; NM_053573.1. [Q62609-1]
DR RefSeq; XP_006233937.1; XM_006233875.3. [Q62609-3]
DR RefSeq; XP_006233938.1; XM_006233876.3. [Q62609-2]
DR RefSeq; XP_006233939.1; XM_006233877.2. [Q62609-4]
DR AlphaFoldDB; Q62609; -.
DR SMR; Q62609; -.
DR CORUM; Q62609; -.
DR STRING; 10116.ENSRNOP00000013443; -.
DR GlyGen; Q62609; 8 sites, 2 N-linked glycans (1 site).
DR jPOST; Q62609; -.
DR PaxDb; Q62609; -.
DR PRIDE; Q62609; -.
DR ABCD; Q62609; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000013443; ENSRNOP00000013443; ENSRNOG00000009862. [Q62609-1]
DR Ensembl; ENSRNOT00000104931; ENSRNOP00000077356; ENSRNOG00000009862. [Q62609-3]
DR GeneID; 93667; -.
DR KEGG; rno:93667; -.
DR UCSC; RGD:620320; rat. [Q62609-1]
DR CTD; 10439; -.
DR RGD; 620320; Olfm1.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000156959; -.
DR HOGENOM; CLU_035236_0_0_1; -.
DR InParanoid; Q62609; -.
DR OMA; ACMQKLX; -.
DR OrthoDB; 421994at2759; -.
DR PhylomeDB; Q62609; -.
DR TreeFam; TF315964; -.
DR PRO; PR:Q62609; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000009862; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; Q62609; RN.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISO:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0099243; C:extrinsic component of synaptic membrane; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0003190; P:atrioventricular valve formation; ISS:AgBase.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:AgBase.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IEA:InterPro.
DR GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:1902003; P:regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR031217; Noelin.
DR InterPro; IPR022082; Noelin_dom.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR23192:SF34; PTHR23192:SF34; 1.
DR Pfam; PF12308; Noelin-1; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Developmental protein;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW Secreted; Signal; Synapse.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..485
FT /note="Noelin"
FT /id="PRO_0000020076"
FT DOMAIN 226..478
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT COILED 87..225
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 221
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:O88998"
FT DISULFID 227..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 1..50
FT /note="MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTRLSAASGGTLDRSTG
FT -> MQPARKLLSLLVLLVMGTELTQ (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:7932877"
FT /id="VSP_003765"
FT VAR_SEQ 153
FT /note="A -> G (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:7932877"
FT /id="VSP_003766"
FT VAR_SEQ 154..485
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:7932877"
FT /id="VSP_003767"
SQ SEQUENCE 485 AA; 55442 MW; 08D0DA6A40B20F29 CRC64;
MSVPLLKIGV VLSTMAMITN WMSQTLPSLV GLNTTRLSAA SGGTLDRSTG VLPTNPEESW
QVYSSAQDSE GRCICTVVAP QQTMCSRDAR TKQLRQLLEK VQNMSQSIEV LDRRTQRDLQ
YVEKMENQMK GLESKFRQVE ESHKQHLARQ FKAIKAKMDE LRPLIPVLEE YKADAKLVLQ
FKEEVQNLTS VLNELQEEIG AYDYDELQSR VSNLEERLRA CMQKLACGKL TGISDPVTVK
TSGSRFGSWM TDPLAPEGDN RVWYMDGYHN NRFVREYKSM VDFMNTDNFT SHRLPHPWSG
TGQVVYNGSI YFNKFQSHII IRFDLKTETI LKTRSLDYAG YNNMYHYAWG GHSDIDLMVD
ENGLWAVYAT NQNAGNIVIS KLDPVSLQIL QTWNTSYPKR SAGEAFIICG TLYVTNGYSG
GTKVHYAYQT NASTYEYIDI PFQNKYSHIS MLDYNPKDRA LYAWNNGHQT LYNVTLFHVI
RSDEL
