NRX3B_MOUSE
ID NRX3B_MOUSE Reviewed; 567 AA.
AC Q8C985; E9Q3Q9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Neurexin-3-beta;
DE AltName: Full=Neurexin III-beta;
DE Contains:
DE RecName: Full=Neurexin-3-beta, soluble form;
DE Contains:
DE RecName: Full=Neurexin-3-beta, C-terminal fragment;
DE Short=NRXN3-CTF;
DE Flags: Precursor;
GN Name=Nrxn3;
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 [LARGE SCALE MRNA] (ISOFORM 1B).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH CBLN1.
RX PubMed=21410790; DOI=10.1111/j.1460-9568.2011.07638.x;
RA Matsuda K., Yuzaki M.;
RT "Cbln family proteins promote synapse formation by regulating distinct
RT neurexin signaling pathways in various brain regions.";
RL Eur. J. Neurosci. 33:1447-1461(2011).
RN [5]
RP INTERACTION WITH CBLN1; CBLN2 AND CBLN4.
RX PubMed=22220752; DOI=10.1111/j.1471-4159.2012.07648.x;
RA Wei P., Pattarini R., Rong Y., Guo H., Bansal P.K., Kusnoor S.V.,
RA Deutch A.Y., Parris J., Morgan J.I.;
RT "The Cbln family of proteins interact with multiple signaling pathways.";
RL J. Neurochem. 121:717-729(2012).
RN [6]
RP INTERACTION WITH CBLN1; CBLN2 AND CBLN4.
RX PubMed=29782851; DOI=10.1016/j.brainres.2018.05.022;
RA Rong Y., Bansal P.K., Wei P., Guo H., Correia K., Parris J., Morgan J.I.;
RT "Glycosylation of Cblns attenuates their receptor binding.";
RL Brain Res. 1694:129-139(2018).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion. May play a role in angiogenesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Weakly interacts with CBLN1 and CBLN2 (PubMed:21410790,
CC PubMed:22220752, PubMed:29782851). Very weak binding, if any, to CBLN4
CC (PubMed:22220752, PubMed:29782851). {ECO:0000269|PubMed:21410790,
CC ECO:0000269|PubMed:22220752, ECO:0000269|PubMed:29782851}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Comment=A number of isoforms, alpha-type and beta-type are produced
CC by alternative promoter usage. Beta-type isoforms differ from
CC alpha-type isoforms in their N-terminus.;
CC Name=1b;
CC IsoId=Q8C985-1; Sequence=Displayed;
CC Name=1a;
CC IsoId=Q6P9K9-1; Sequence=External;
CC Name=2a;
CC IsoId=Q6P9K9-2; Sequence=External;
CC -!- PTM: Proccessed by alpha-secretase leading to the formation of an
CC extracellular soluble protein as well as a C-terminal membrane-embedded
CC fragment (CTF). Proteolysis of these CTFs by gamma-secretase releases
CC intracellular domains (ICDs) and extracellular peptides (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31344.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK042730; BAC31344.1; ALT_FRAME; mRNA.
DR EMBL; AC115709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC171335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01025627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR974428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR974583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU041252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS79143.1; -. [Q8C985-1]
DR RefSeq; NP_001239003.1; NM_001252074.2. [Q8C985-1]
DR AlphaFoldDB; Q8C985; -.
DR SMR; Q8C985; -.
DR BioGRID; 201853; 1.
DR IntAct; Q8C985; 1.
DR PhosphoSitePlus; Q8C985; -.
DR MaxQB; Q8C985; -.
DR PeptideAtlas; Q8C985; -.
DR PRIDE; Q8C985; -.
DR ProteomicsDB; 293904; -. [Q8C985-1]
DR Antibodypedia; 106; 252 antibodies from 31 providers.
DR DNASU; 18191; -.
DR Ensembl; ENSMUST00000110130; ENSMUSP00000105757; ENSMUSG00000066392. [Q8C985-1]
DR GeneID; 18191; -.
DR UCSC; uc007oke.3; mouse. [Q8C985-1]
DR CTD; 9369; -.
DR MGI; MGI:1096389; Nrxn3.
DR VEuPathDB; HostDB:ENSMUSG00000066392; -.
DR GeneTree; ENSGT00940000154618; -.
DR OrthoDB; 35129at2759; -.
DR BioGRID-ORCS; 18191; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Nrxn3; mouse.
DR Proteomes; UP000000589; Chromosome 12.
DR Bgee; ENSMUSG00000066392; Expressed in rostral migratory stream and 189 other tissues.
DR ExpressionAtlas; Q8C985; baseline and differential.
DR Genevisible; Q8C985; MM.
DR GO; GO:0098982; C:GABA-ergic synapse; IMP:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; ISA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR GO; GO:0030534; P:adult behavior; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR GO; GO:0035176; P:social behavior; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR GO; GO:0071625; P:vocalization behavior; ISO:MGI.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Angiogenesis;
KW Cell adhesion; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..567
FT /note="Neurexin-3-beta"
FT /id="PRO_0000412558"
FT CHAIN 36..480
FT /note="Neurexin-3-beta, soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412559"
FT CHAIN 481..567
FT /note="Neurexin-3-beta, C-terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412560"
FT TOPO_DOM 36..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 83..283
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 567 AA; 62376 MW; 0CB4D38095C2B752 CRC64;
MHLRIHPRRS PPRRPAWTLG IWSLFWGCIV SSVWSSSNVA SSSSSSPGSH SQQEHHFHGS
KHHSVPISIY RSPVSLRGGH AGATYIFGKS GGLILYTWPA NDRPSTRSDR LAVGFSTTVK
DGILVRIDSA PGLGDFLQLH IEQGKIGVVF NIGTVDISIK EERTPVNDGK YHVVRFTRNG
GNATLQVDNW PVNEHYPTGN TDNERLQMVK QKIPFKYNRP VEEWLQEKGR QLTIFNTQAQ
IAIGGKDKGR LFQGQLSGLY YDGLKVLNMA AENNPNIKIN GSVRLVGEVP SVSGTTQTTS
MPPEMSTTVM ETTTTMATTT TRKNRSTASI QPTSDDLVSS AECSSDDEDF VECEPSTGRS
DKSLSTSIFE GGYKAHAPKW ESKDFRPNKV SETSRTTTTS LSPELIRFTA SSSSGMVPKL
PAGKMNNRDL KPQPDIVLLP LPTAYELDST KLKSPLITSP MFRNVPTANP TEPGIRRVPG
ASEVIRESSS TTGMVVGIVA AAALCILILL YAMYKYRNRD EGSYQVDETR NYISNSAQSN
GTLMKEKQAS SKSGHKKQKN KDKEYYV
