NOE2_RAT
ID NOE2_RAT Reviewed; 478 AA.
AC Q568Y7; A6JNL2;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Noelin-2;
DE AltName: Full=Olfactomedin-2;
DE Flags: Precursor;
GN Name=Olfm2;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP 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).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH RUNX2.
RX PubMed=28062493; DOI=10.1161/atvbaha.116.308606;
RA Shi N., Li C.X., Cui X.B., Tomarev S.I., Chen S.Y.;
RT "Olfactomedin 2 regulates smooth muscle phenotypic modulation and vascular
RT remodeling through mediating Runt-related transcription factor 2 binding to
RT serum response factor.";
RL Arterioscler. Thromb. Vasc. Biol. 37:446-454(2017).
CC -!- FUNCTION: Involved in transforming growth factor beta (TGF-beta)-
CC induced smooth muscle differentiation. TGF-beta induces expression and
CC nuclear translocation of OLFM2 where it binds to SRF, causing its
CC dissociation from the transcriptional repressor HEY2/HERP1 and
CC facilitating binding of SRF to target genes. Plays a role in AMPAR
CC complex organization. Is a regulator of vascular smooth-muscle cell
CC (SMC) phenotypic switching, that acts by promoting RUNX2 and inhibiting
CC MYOCD binding to SRF. SMC phenotypic switching is the process through
CC which vascular SMCs undergo transition between a quiescent contractile
CC phenotype and a proliferative synthetic phenotype in response to
CC pathological stimuli. SMC phenotypic plasticity is essential for
CC vascular development and remodeling (PubMed:28062493).
CC {ECO:0000250|UniProtKB:O95897, ECO:0000250|UniProtKB:Q8BM13,
CC ECO:0000269|PubMed:28062493}.
CC -!- SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the 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 OLFM2. 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 GRIA2 (By similarity). Interacts with OLFM1 and OLFM3 (By similarity).
CC Interacts with SRF; the interaction promotes dissociation of SRF from
CC the transcriptional repressor HEY2 (By similarity). Interacts with
CC RUNX2 (PubMed:28062493). {ECO:0000250|UniProtKB:O95897,
CC ECO:0000250|UniProtKB:Q8BM13, ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:28062493}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O95897}. Synapse
CC {ECO:0000305|PubMed:22632720}. Membrane {ECO:0000250|UniProtKB:Q8BM13}.
CC Nucleus {ECO:0000250|UniProtKB:O95897}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95897}. Note=Nuclear localization is induced by
CC TGF-beta. {ECO:0000250|UniProtKB:O95897}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q568Y7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q568Y7-2; Sequence=VSP_044590;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:22632720). Expressed in carotid arteries and the aorta, mainly
CC in aortic SMCs (PubMed:28062493). {ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:28062493}.
CC -!- INDUCTION: Expression in SMCs and carotid arteries is up-regulated upon
CC injury or by PDGFB. {ECO:0000269|PubMed:28062493}.
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DR EMBL; CH473993; EDL78354.1; -; Genomic_DNA.
DR EMBL; CH473993; EDL78355.1; -; Genomic_DNA.
DR EMBL; BC092647; AAH92647.1; -; mRNA.
DR RefSeq; NP_001015017.1; NM_001015017.1. [Q568Y7-1]
DR AlphaFoldDB; Q568Y7; -.
DR SMR; Q568Y7; -.
DR CORUM; Q568Y7; -.
DR STRING; 10116.ENSRNOP00000027829; -.
DR GlyGen; Q568Y7; 7 sites.
DR PaxDb; Q568Y7; -.
DR PRIDE; Q568Y7; -.
DR Ensembl; ENSRNOT00000027829; ENSRNOP00000027829; ENSRNOG00000020519. [Q568Y7-1]
DR GeneID; 313783; -.
DR KEGG; rno:313783; -.
DR UCSC; RGD:1309741; rat. [Q568Y7-1]
DR CTD; 93145; -.
DR RGD; 1309741; Olfm2.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000159148; -.
DR HOGENOM; CLU_035236_0_0_1; -.
DR InParanoid; Q568Y7; -.
DR OMA; KADMRTI; -.
DR OrthoDB; 421994at2759; -.
DR PhylomeDB; Q568Y7; -.
DR TreeFam; TF315964; -.
DR PRO; PR:Q568Y7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000020519; Expressed in frontal cortex and 12 other tissues.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISO:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0099243; C:extrinsic component of synaptic membrane; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; ISO:RGD.
DR GO; GO:1905174; P:regulation of vascular associated smooth muscle cell dedifferentiation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
DR InterPro; IPR031219; Noelin-2.
DR InterPro; IPR022082; Noelin_dom.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR23192:SF27; PTHR23192:SF27; 1.
DR Pfam; PF12308; Noelin-1; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Disulfide bond; Glycoprotein;
KW Membrane; Nucleus; Reference proteome; Secreted; Signal; Synapse.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..478
FT /note="Noelin-2"
FT /id="PRO_0000420686"
FT DOMAIN 218..470
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT COILED 86..109
FT /evidence="ECO:0000255"
FT COILED 160..218
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 219..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 1..45
FT /note="MSVPLLKIGAVLSTMAMVTNWMSQTLPSLVGLNSTVSRAGSSEKI -> MRK
FT LRQTGIAIAGDH (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044590"
SQ SEQUENCE 478 AA; 53870 MW; 688FD06A01B92E77 CRC64;
MSVPLLKIGA VLSTMAMVTN WMSQTLPSLV GLNSTVSRAG SSEKITLFQS PEEGWQLYTS
AQAPDGKCIC TAVIPAQSTC ARDGRSRELR QLMEKVQNVS QSMEVLELRT YRDLQYVRSM
ETLMRSLDAR LRTADGSVSA KSFQELKDRM TELLPLSSVL EQYKADTRTI VRLREEVRNL
SGNLAAIQEE MGAYGYEDLQ QRVMALEARL HACAQKLGCG KLTGVSNPIT IRAMGSRFGS
WMTDTMAPSA DSRVWYMDGY YKGRRVLEFR TLGDFIKGQN FIQHLLPQPW AGTGHVVYNG
SLFYNKYQSN VVVKYHFRSR SVLVQRSLPG AGYNNTFPYS WGGFSDMDFM VDESGLWAVY
TTNQNAGNIV VSRLDPHTLE VVRSWDTGYP KRSAGEAFMI CGVLYVTNSH LAGAKVYFAY
FTNTSSYEYT DVPFHNQYSH ISMLDYNPRE RALYTWNNGH QVLYNVTLFH VISTAGDP
