NOE3_MOUSE
ID NOE3_MOUSE Reviewed; 478 AA.
AC P63056; Q8BKV2; Q8BLL6; Q8QZW0; Q8R4K3; Q8R4K4;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Noelin-3;
DE AltName: Full=Olfactomedin-3;
DE AltName: Full=Optimedin;
DE Flags: Precursor;
GN Name=Olfm3; Synonyms=Noe3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH MYOC.
RC STRAIN=129/Sv; TISSUE=Brain;
RX PubMed=12019210; DOI=10.1093/hmg/11.11.1291;
RA Torrado M., Trivedi R., Zinovieva R., Karavanova I., Tomarev S.I.;
RT "Optimedin: a novel olfactomedin-related protein that interacts with
RT myocilin.";
RL Hum. Mol. Genet. 11:1291-1301(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain, Cerebellum, Hypothalamus, Retina, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=21228389; DOI=10.1167/iovs.10-6356;
RA Sultana A., Nakaya N., Senatorov V.V., Tomarev S.I.;
RT "Olfactomedin 2: expression in the eye and interaction with other
RT olfactomedin domain-containing proteins.";
RL Invest. Ophthalmol. Vis. Sci. 52:2584-2592(2011).
RN [4]
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).
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 OLFM3. 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). Homodimer.
CC Interacts with MYOC (PubMed:12019210). Interacts with OLFM2 (By
CC similarity). {ECO:0000250|UniProtKB:Q96PB7,
CC ECO:0000269|PubMed:12019210, ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22632720}. Synapse
CC {ECO:0000305|PubMed:22632720}. Note=Isoform 2 is secreted more
CC efficiently than isoform 1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B;
CC IsoId=P63056-1, Q8QZW0-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=P63056-2, Q8QZW0-2;
CC Sequence=VSP_007747;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:22632720}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development starting
CC from 7 dpc. Expression increases moderately during embryonic
CC development and remains stable in the postnatal brain.
CC {ECO:0000269|PubMed:21228389}.
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DR EMBL; AF442824; AAL87043.1; -; mRNA.
DR EMBL; AF442825; AAL87044.1; -; mRNA.
DR EMBL; AK038569; BAC30048.1; -; mRNA.
DR EMBL; AK044325; BAC31867.1; -; mRNA.
DR EMBL; AK044605; BAC32000.1; -; mRNA.
DR EMBL; AK045482; BAC32389.1; -; mRNA.
DR EMBL; AK049612; BAC33841.1; -; mRNA.
DR EMBL; AK079315; BAC37605.1; -; mRNA.
DR CCDS; CCDS17779.1; -. [P63056-2]
DR CCDS; CCDS17780.1; -.
DR RefSeq; NP_694797.1; NM_153157.3. [P63056-1]
DR RefSeq; NP_703188.1; NM_153458.3. [P63056-2]
DR AlphaFoldDB; P63056; -.
DR SMR; P63056; -.
DR BioGRID; 230899; 3.
DR STRING; 10090.ENSMUSP00000060985; -.
DR GlyGen; P63056; 5 sites.
DR PhosphoSitePlus; P63056; -.
DR MaxQB; P63056; -.
DR PaxDb; P63056; -.
DR PeptideAtlas; P63056; -.
DR PRIDE; P63056; -.
DR ProteomicsDB; 252981; -.
DR ProteomicsDB; 252982; -. [P63056-2]
DR Antibodypedia; 33701; 152 antibodies from 21 providers.
DR Ensembl; ENSMUST00000051309; ENSMUSP00000060985; ENSMUSG00000027965. [P63056-1]
DR Ensembl; ENSMUST00000081752; ENSMUSP00000080448; ENSMUSG00000027965. [P63056-2]
DR GeneID; 229759; -.
DR KEGG; mmu:229759; -.
DR UCSC; uc008rbn.2; mouse.
DR CTD; 118427; -.
DR MGI; MGI:2387329; Olfm3.
DR VEuPathDB; HostDB:ENSMUSG00000027965; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000156998; -.
DR HOGENOM; CLU_035236_0_0_1; -.
DR InParanoid; P63056; -.
DR OMA; XELKEKM; -.
DR OrthoDB; 421994at2759; -.
DR PhylomeDB; P63056; -.
DR TreeFam; TF315964; -.
DR BioGRID-ORCS; 229759; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Olfm3; mouse.
DR PRO; PR:P63056; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P63056; protein.
DR Bgee; ENSMUSG00000027965; Expressed in cerebellum lobe and 88 other tissues.
DR ExpressionAtlas; P63056; baseline and differential.
DR Genevisible; P63056; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR031216; Noelin-3.
DR InterPro; IPR022082; Noelin_dom.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR23192:SF36; PTHR23192:SF36; 1.
DR Pfam; PF12308; Noelin-1; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Synapse.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..478
FT /note="Noelin-3"
FT /id="PRO_0000020081"
FT DOMAIN 218..470
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT COILED 77..217
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
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 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..43
FT /note="MSAPLLKLGAVLSTMAMISNWMSQTLPSLVGLNTTRLSAPDTL -> MQARS
FT SFLNLLLLSLLAGLDPSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12019210,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007747"
FT CONFLICT 118
FT /note="E -> K (in Ref. 2; BAC31867)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="H -> P (in Ref. 2; BAC33841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 54886 MW; ED4250E58213787D CRC64;
MSAPLLKLGA VLSTMAMISN WMSQTLPSLV GLNTTRLSAP DTLTQISPKE GWQVYSSAQD
PDGRCICTVV APEQNLCSRD AKSRQLRQLL EKVQNMSQSI EVLNLRTQRD FQYVLKMETQ
MKGLKAKFRQ IEDDRKTLMT KHFQELKEKM DELLPLIPVL EQYKTDAKLI TQFKEEIRNL
SSVLTGIQEE IGAYDYEELH QRVLSLETRL RDCMKKLTCG KLMKITGPIT VKTSGTRFGA
WMTDPLASEK NNRVWYMDSY TNNKIVREYK SIADFVSGAE SRTYNLPFKW AGTNHVVYNG
SLYFNKYQSN IIIKYSFDLG RVLAQRSLEY AGFHNVYPYT WGGFSDIDLM ADEIGLWAVY
ATNQNAGNIV ISQLNQDTLE VMKSWSTGYP KRSAGESFMI CGTLYVTNSH LTGAKVYYSY
STKTSTYEYT DIPFHNQYFH ISMLDYNARD RALYAWNNGH QVLFNVTLFH IIKTEDDT
