NRX1A_MOUSE
ID NRX1A_MOUSE Reviewed; 1514 AA.
AC Q9CS84; G3UWZ9; O88722; Q80Y87; Q8CHE6;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Neurexin-1;
DE AltName: Full=Neurexin I-alpha;
DE AltName: Full=Neurexin-1-alpha;
DE Flags: Precursor;
GN Name=Nrxn1; Synonyms=Kiaa0578;
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 2A).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [2]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-1514 (ISOFORM 4A).
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-437 (ISOFORMS 1A; 2A AND 3A/4A).
RC STRAIN=CD-1; TISSUE=Brain;
RA Graveley B.R., Philipps D.L.;
RT "Sequencing of the neurexin genes.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1126-1514 (ISOFORMS 1A/2A/3A).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1463-1505 (ISOFORMS 1A/2A/3A/4A).
RC STRAIN=C57BL/10; TISSUE=Brain;
RX PubMed=10408888; DOI=10.1006/mcne.1999.0740;
RA Gorecki D.C., Szklarczyk A., Lukasiuk K., Kaczmarek L., Simons J.P.;
RT "Differential seizure-induced and developmental changes of neurexin
RT expression.";
RL Mol. Cell. Neurosci. 13:218-227(1999).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND CALCIUM-DEPENDENT INTERACTION WITH
RP ALPHA-LATROTOXIN.
RX PubMed=9430716; DOI=10.1074/jbc.273.3.1705;
RA Geppert M., Khvotchev M., Krasnoperov V., Goda Y., Missler M., Hammer R.E.,
RA Ichtchenko K., Petrenko A.G., Sudhof T.C.;
RT "Neurexin I alpha is a major alpha-latrotoxin receptor that cooperates in
RT alpha-latrotoxin action.";
RL J. Biol. Chem. 273:1705-1710(1998).
RN [9]
RP INTERACTION WITH SYTL1.
RX PubMed=11243866; DOI=10.1006/bbrc.2001.4512;
RA Fukuda M., Mikoshiba K.;
RT "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem
RT C2 proteins.";
RL Biochem. Biophys. Res. Commun. 281:1226-1233(2001).
RN [10]
RP INTERACTION WITH SYT13.
RX PubMed=11171101; DOI=10.1042/0264-6021:3540249;
RA Fukuda M., Mikoshiba K.;
RT "Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt
RT XIII).";
RL Biochem. J. 354:249-257(2001).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN NEUROTRANSMITTER RELEASE.
RX PubMed=12827191; DOI=10.1038/nature01755;
RA Missler M., Zhang W., Rohlmann A., Kattenstroth G., Hammer R.E.,
RA Gottmann K., Sudhof T.C.;
RT "Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis.";
RL Nature 423:939-948(2003).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=14983056; DOI=10.1073/pnas.0308626100;
RA Kattenstroth G., Tantalaki E., Sudhof T.C., Gottmann K., Missler M.;
RT "Postsynaptic N-methyl-D-aspartate receptor function requires alpha-
RT neurexins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2607-2612(2004).
RN [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17035546; DOI=10.1523/jneurosci.1913-06.2006;
RA Dudanova I., Sedej S., Ahmad M., Masius H., Sargsyan V., Zhang W.,
RA Riedel D., Angenstein F., Schild D., Rupnik M., Missler M.;
RT "Important contribution of alpha-neurexins to Ca2+-triggered exocytosis of
RT secretory granules.";
RL J. Neurosci. 26:10599-10613(2006).
RN [14]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16406382; DOI=10.1016/j.neuroscience.2005.11.040;
RA Sons M.S., Busche N., Strenzke N., Moser T., Ernsberger U., Mooren F.C.,
RA Zhang W., Ahmad M., Steffens H., Schomburg E.D., Plomp J.J., Missler M.;
RT "alpha-Neurexins are required for efficient transmitter release and
RT synaptic homeostasis at the mouse neuromuscular junction.";
RL Neuroscience 138:433-446(2006).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=17347997; DOI=10.1002/cne.21305;
RA Dudanova I., Tabuchi K., Rohlmann A., Sudhof T.C., Missler M.;
RT "Deletion of alpha-neurexins does not cause a major impairment of axonal
RT pathfinding or synapse formation.";
RL J. Comp. Neurol. 502:261-274(2007).
RN [16]
RP INTERACTION WITH NLGN4L.
RX PubMed=18434543; DOI=10.1073/pnas.0801383105;
RA Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V.,
RA Sudhof T.C.;
RT "Unusually rapid evolution of neuroligin-4 in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=19822762; DOI=10.1073/pnas.0910297106;
RA Etherton M.R., Blaiss C.A., Powell C.M., Sudhof T.C.;
RT "Mouse neurexin-1alpha deletion causes correlated electrophysiological and
RT behavioral changes consistent with cognitive impairments.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17998-18003(2009).
RN [18]
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 [19]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CBLN1; CBLN2 AND
RP CBLN4.
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 [20]
RP INTERACTION WITH CASK.
RX PubMed=25385611; DOI=10.1073/pnas.1416515111;
RA Li Y., Wei Z., Yan Y., Wan Q., Du Q., Zhang M.;
RT "Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem
RT reveals a highly specific assembly mechanism for the apical Crumbs
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:17444-17449(2014).
RN [21]
RP ALTERNATIVE PROMOTER USAGE (ISOFORM 6), AND ALTERNATIVE SPLICING.
RX PubMed=25737549; DOI=10.1073/pnas.1502849112;
RA Yan Q., Weyn-Vanhentenryck S.M., Wu J., Sloan S.A., Zhang Y., Chen K.,
RA Wu J.Q., Barres B.A., Zhang C.;
RT "Systematic discovery of regulated and conserved alternative exons in the
RT mammalian brain reveals NMD modulating chromatin regulators.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3445-3450(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1132-1334 (ISOFORM 5A) IN COMPLEX
RP WITH CALCIUM, SUBUNIT, INTERACTION WITH NLGN1 AND NLGN2, AND ALTERNATIVE
RP SPLICING.
RX PubMed=18334216; DOI=10.1016/j.str.2007.12.024;
RA Koehnke J., Jin X., Trbovic N., Katsamba P.S., Brasch J., Ahlsen G.,
RA Scheiffele P., Honig B., Palmer A.G. III, Shapiro L.;
RT "Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and
RT dynamics of splice insertion sequence 4.";
RL Structure 16:410-421(2008).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 1132-1334, AND INTERACTION WITH
RP NLGN1; NLGN2 AND NLGN3.
RX PubMed=20624592; DOI=10.1016/j.neuron.2010.06.001;
RA Koehnke J., Katsamba P.S., Ahlsen G., Bahna F., Vendome J., Honig B.,
RA Shapiro L., Jin X.;
RT "Splice form dependence of beta-neurexin/neuroligin binding interactions.";
RL Neuron 67:61-74(2010).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions,
CC exocytosis of secretory granules and regulation of signal transmission.
CC Function is isoform-specific. Alpha-type isoforms have a long N-
CC terminus with six laminin G-like domains and play an important role in
CC synaptic signal transmission. Alpha-type isoforms play a role in the
CC regulation of calcium channel activity and Ca(2+)-triggered
CC neurotransmitter release at synapses and at neuromuscular junctions.
CC They play an important role in Ca(2+)-triggered exocytosis of secretory
CC granules in pituitary gland. They may affect their functions at
CC synapses and in endocrine cells via their interactions with proteins
CC from the exocytotic machinery. Likewise, alpha-type isoforms play a
CC role in regulating the activity of postsynaptic NMDA receptors, a
CC subtype of glutamate-gated ion channels. Both alpha-type and beta-type
CC isoforms may play a role in the formation or maintenance of synaptic
CC junctions via their interactions (via the extracellular domains) with
CC neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de
CC novo formation of presynaptic structures. May be involved in
CC specification of excitatory synapses. Alpha-type isoforms were first
CC identified as receptors for alpha-latrotoxin from spider venom.
CC {ECO:0000269|PubMed:12827191, ECO:0000269|PubMed:14983056,
CC ECO:0000269|PubMed:16406382, ECO:0000269|PubMed:17035546,
CC ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:9430716}.
CC -!- SUBUNIT: Interacts (via laminin G-like domain 2 and/or laminin G-like
CC domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer
CC interacts with one NRXN1 dimer (By similarity). Interacts (via
CC cytoplasmic C-terminal region) with CASK (via the PDZ, SH3 and
CC guanylate kinase-like domains) (PubMed:25385611). Interacts (via
CC cytoplasmic C-terminus) with CASKIN1 and APBA1 (By similarity).
CC Interacts (via laminin G-like domain 2) with NXPH1 and NXPH3 (By
CC similarity). Alpha-type isoforms (neurexin-1-alpha) interact (via
CC laminin G-like domain 2 and/or laminin G-like domain 6) with DAG1 (via
CC alpha-dystroglycan chain). Alpha-type isoforms interact with alpha-
CC latrotoxin from spider venom. Interacts with LRRTM1, LRRTM2, LRRTM3 and
CC LRRTM4 (By similarity). Interacts (via laminin G-like domain 2 and/or
CC laminin G-like domain 6) with NLGN1, NLGN2, NLGN3 and NLGN4L; these
CC interactions are calcium-dependent. Interacts with SYT13 and SYTL1.
CC Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q28146, ECO:0000250|UniProtKB:Q63372,
CC ECO:0000269|PubMed:11171101, ECO:0000269|PubMed:11243866,
CC ECO:0000269|PubMed:18334216, ECO:0000269|PubMed:18434543,
CC ECO:0000269|PubMed:20624592, ECO:0000269|PubMed:21410790,
CC ECO:0000269|PubMed:25385611}.
CC -!- INTERACTION:
CC Q9CS84; O14522: PTPRT; Xeno; NbExp=2; IntAct=EBI-399696, EBI-728180;
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000269|PubMed:21410790}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:21410790}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
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=1a;
CC IsoId=Q9CS84-1; Sequence=Displayed;
CC Name=2a; Synonyms=Alpha-2B;
CC IsoId=Q9CS84-2; Sequence=VSP_003484;
CC Name=3a; Synonyms=Alpha-2C;
CC IsoId=Q9CS84-3; Sequence=VSP_003485;
CC Name=4a;
CC IsoId=Q9CS84-4; Sequence=VSP_003485, VSP_016401;
CC Name=1b;
CC IsoId=P0DI97-1; Sequence=External;
CC Name=5a;
CC IsoId=Q9CS84-5; Sequence=VSP_003484, VSP_043946;
CC Name=6;
CC IsoId=Q9CS84-6; Sequence=VSP_058203, VSP_058204, VSP_016401;
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but mice display subtle
CC behavorial deficits. Females show deficits in nest building and taking
CC care of pups. Mice lacking the alpha-type isoforms of NRXN1, NRXN2 and
CC NRXN3 are born at the expected Mendelian rate, but die during the first
CC day after birth, probably due to neurological defects in the brainstem
CC that impair normal breathing. These mice express normal levels of the
CC beta-type isoforms of NRXN1, NRXN2 and NRXN3. Mice show reduced density
CC of synapses in the brainstem, especially a reduction in the numbers of
CC GABA-releasing synapses. Their brains display a reduced frequency of
CC spontaneous neurotransmitter release, and decreased neurotransmitter
CC release in response to an action potential. Likewise, the activity of
CC voltage-gated calcium channels is strongly decreased. A small
CC proportion (5-10%) of mice lacking the alpha-type isoforms of both
CC NRXN1 and NRXN2 survive to adulthood; these mice do not show any gross
CC anatomical defects in their brains or changes in the distribution of
CC synaptic proteins, but they have fewer synapses in the neocortex and
CC show defects in neurotransmitter release at neuromuscular junctions.
CC {ECO:0000269|PubMed:12827191, ECO:0000269|PubMed:14983056,
CC ECO:0000269|PubMed:16406382, ECO:0000269|PubMed:17035546,
CC ECO:0000269|PubMed:17347997, ECO:0000269|PubMed:19822762,
CC ECO:0000269|PubMed:9430716}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000303|PubMed:25737549}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47146.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAC41433.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB093249; BAC41433.2; ALT_INIT; mRNA.
DR EMBL; AC101872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC170901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC171209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT486002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047146; AAH47146.1; ALT_SEQ; mRNA.
DR EMBL; AF387674; AAK70469.1; -; Genomic_DNA.
DR EMBL; AF387674; AAK70470.1; -; Genomic_DNA.
DR EMBL; AF387674; AAK70471.1; -; Genomic_DNA.
DR EMBL; AK017578; BAB30815.1; -; mRNA.
DR EMBL; AJ006802; CAA07257.1; -; mRNA.
DR CCDS; CCDS57113.1; -. [Q9CS84-2]
DR CCDS; CCDS84339.1; -. [Q9CS84-6]
DR RefSeq; NP_001333891.1; NM_001346962.1. [Q9CS84-6]
DR RefSeq; NP_064648.3; NM_020252.3. [Q9CS84-2]
DR RefSeq; NP_796258.2; NM_177284.2.
DR RefSeq; XP_006523874.1; XM_006523811.3. [Q9CS84-3]
DR RefSeq; XP_006523875.1; XM_006523812.3. [Q9CS84-4]
DR RefSeq; XP_006523879.1; XM_006523816.3. [Q9CS84-5]
DR PDB; 3BOD; X-ray; 1.70 A; A=1132-1334.
DR PDB; 3MW2; X-ray; 2.69 A; A/B=1132-1334.
DR PDB; 6PNP; X-ray; 1.94 A; A=283-480.
DR PDB; 6PNQ; X-ray; 1.95 A; A=283-480.
DR PDBsum; 3BOD; -.
DR PDBsum; 3MW2; -.
DR PDBsum; 6PNP; -.
DR PDBsum; 6PNQ; -.
DR AlphaFoldDB; Q9CS84; -.
DR SMR; Q9CS84; -.
DR BioGRID; 201851; 5.
DR IntAct; Q9CS84; 8.
DR MINT; Q9CS84; -.
DR GlyConnect; 2539; 4 N-Linked glycans (3 sites).
DR GlyGen; Q9CS84; 4 sites, 4 N-linked glycans (3 sites).
DR iPTMnet; Q9CS84; -.
DR PhosphoSitePlus; Q9CS84; -.
DR MaxQB; Q9CS84; -.
DR PaxDb; Q9CS84; -.
DR PeptideAtlas; Q9CS84; -.
DR PRIDE; Q9CS84; -.
DR ProteomicsDB; 293898; -. [Q9CS84-1]
DR ProteomicsDB; 293899; -. [Q9CS84-2]
DR ProteomicsDB; 293900; -. [Q9CS84-3]
DR ProteomicsDB; 293901; -. [Q9CS84-4]
DR ProteomicsDB; 293902; -. [Q9CS84-5]
DR ProteomicsDB; 293903; -. [Q9CS84-6]
DR ABCD; Q9CS84; 1 sequenced antibody.
DR Antibodypedia; 30173; 296 antibodies from 37 providers.
DR DNASU; 18189; -.
DR Ensembl; ENSMUST00000054059; ENSMUSP00000057294; ENSMUSG00000024109. [Q9CS84-3]
DR Ensembl; ENSMUST00000072671; ENSMUSP00000072458; ENSMUSG00000024109. [Q9CS84-4]
DR Ensembl; ENSMUST00000160844; ENSMUSP00000125407; ENSMUSG00000024109. [Q9CS84-2]
DR Ensembl; ENSMUST00000161402; ENSMUSP00000124116; ENSMUSG00000024109. [Q9CS84-1]
DR Ensembl; ENSMUST00000174331; ENSMUSP00000133491; ENSMUSG00000024109. [Q9CS84-5]
DR Ensembl; ENSMUST00000197268; ENSMUSP00000142815; ENSMUSG00000024109. [Q9CS84-6]
DR GeneID; 18189; -.
DR UCSC; uc008dvz.2; mouse. [Q9CS84-2]
DR UCSC; uc008dwa.2; mouse. [Q9CS84-4]
DR CTD; 9378; -.
DR MGI; MGI:1096391; Nrxn1.
DR VEuPathDB; HostDB:ENSMUSG00000024109; -.
DR GeneTree; ENSGT00940000154292; -.
DR HOGENOM; CLU_001710_0_1_1; -.
DR InParanoid; Q9CS84; -.
DR OMA; PYDVYVA; -.
DR OrthoDB; 35129at2759; -.
DR PhylomeDB; Q9CS84; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 18189; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Nrxn1; mouse.
DR EvolutionaryTrace; Q9CS84; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CS84; protein.
DR Bgee; ENSMUSG00000024109; Expressed in medial dorsal nucleus of thalamus and 178 other tissues.
DR ExpressionAtlas; Q9CS84; baseline and differential.
DR Genevisible; Q9CS84; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0042734; C:presynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0036057; C:slit diaphragm; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR GO; GO:0033130; F:acetylcholine receptor binding; IDA:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0097109; F:neuroligin family protein binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:MGI.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISO:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; IDA:BHF-UCL.
DR GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:BHF-UCL.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; ISO:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IGI:MGI.
DR GO; GO:0090129; P:positive regulation of synapse maturation; IDA:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; IDA:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0060134; P:prepulse inhibition; IMP:BHF-UCL.
DR GO; GO:0099054; P:presynapse assembly; ISO:MGI.
DR GO; GO:2000821; P:regulation of grooming behavior; IMP:BHF-UCL.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IMP:SynGO.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0035176; P:social behavior; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0099542; P:trans-synaptic signaling by endocannabinoid; IMP:SynGO.
DR GO; GO:0042297; P:vocal learning; ISO:MGI.
DR GO; GO:0071625; P:vocalization behavior; ISO:MGI.
DR CDD; cd00110; LamG; 6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; SSF49899; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing; Calcium;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Metal-binding; Reference proteome;
KW Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1514
FT /note="Neurexin-1"
FT /id="PRO_0000043164"
FT TOPO_DOM 31..1438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1439..1459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1460..1514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..217
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 219..256
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 283..480
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 487..679
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 683..720
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 725..898
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 912..1087
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1090..1127
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1133..1331
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 197..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1507
FT /note="Interaction with CASK"
FT /evidence="ECO:0000269|PubMed:25385611"
FT COMPBIAS 1481..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 772
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 789
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 848
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 1200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 1282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 1284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..243
FT /evidence="ECO:0000250"
FT DISULFID 245..255
FT /evidence="ECO:0000250"
FT DISULFID 444..480
FT /evidence="ECO:0000250"
FT DISULFID 650..679
FT /evidence="ECO:0000250"
FT DISULFID 687..698
FT /evidence="ECO:0000250"
FT DISULFID 692..707
FT /evidence="ECO:0000250"
FT DISULFID 709..719
FT /evidence="ECO:0000250"
FT DISULFID 1059..1087
FT /evidence="ECO:0000250"
FT DISULFID 1094..1105
FT /evidence="ECO:0000250"
FT DISULFID 1099..1114
FT /evidence="ECO:0000250"
FT DISULFID 1116..1126
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1372
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:25737549"
FT /id="VSP_058203"
FT VAR_SEQ 379..393
FT /note="Missing (in isoform 3a and isoform 4a)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003485"
FT VAR_SEQ 387..393
FT /note="Missing (in isoform 2a and isoform 5a)"
FT /evidence="ECO:0000303|PubMed:12465718, ECO:0000303|Ref.5"
FT /id="VSP_003484"
FT VAR_SEQ 1247..1276
FT /note="Missing (in isoform 5a)"
FT /evidence="ECO:0000305"
FT /id="VSP_043946"
FT VAR_SEQ 1373..1381
FT /note="GKPPTKEPI -> MDMRWHCEN (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:25737549"
FT /id="VSP_058204"
FT VAR_SEQ 1410..1412
FT /note="Missing (in isoform 4a and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:25737549"
FT /id="VSP_016401"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6PNQ"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 368..378
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:6PNQ"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 442..454
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:6PNP"
FT HELIX 459..465
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:6PNP"
FT STRAND 1132..1145
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1154..1164
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1168..1181
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1184..1190
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1193..1202
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1205..1208
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1216..1218
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1220..1227
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1230..1235
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1241..1243
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1265..1277
FT /evidence="ECO:0007829|PDB:3MW2"
FT STRAND 1286..1292
FT /evidence="ECO:0007829|PDB:3BOD"
FT HELIX 1294..1296
FT /evidence="ECO:0007829|PDB:3MW2"
FT STRAND 1302..1309
FT /evidence="ECO:0007829|PDB:3BOD"
FT HELIX 1314..1319
FT /evidence="ECO:0007829|PDB:3BOD"
FT STRAND 1325..1333
FT /evidence="ECO:0007829|PDB:3BOD"
SQ SEQUENCE 1514 AA; 166169 MW; 412281FE441F0EFC CRC64;
MGTALVQRGG CCLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR
RQFRNTTLYI DRAEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF
KGWIRDVRVN SSQALPVDGG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ
AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP
IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG
KFNDNAWHDV KVTRNLRQHS GIGHAMVNKL HCSVTISVDG ILTTTGYTQE DYTMLGSDDF
FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDVRLELS RLAKQGDPKM KIHGVVAFKC
ENVATLDPIT FETPESFISL PKWNAKKTGS ISFDFRTTEP NGLILFSHGK PRHQKDAKHP
QMIKVDFFAI EMLDGHLYLL LDMGSGTIKI KALQKKVNDG EWYHVDFQRD GRSGTISVNT
LRTPYTAPGE SEILDLDDEL YLGGLPENKA GLVFPTEVWT ALLNYGYVGC IRDLFIDGQS
KDIRQMAEIQ STAGVKPSCS KETAKPCLSN PCKNNGMCRD GWNRYVCDCS GTGYLGRSCE
REATVLSYDG SMFMKIQLPV VMHTEAEDVS LRFRSQRAYG ILMATTSRDS ADTLRLELDA
GRVKLTVNLD CIRINCNSSK GPETLFAGYN LNDNEWHTVR VVRRGKSLKL TVDDQQAMTG
QMAGDHTRLE FHNIETGIIT ERRYLSSVPS NFIGHLQSLT FNGMAYIDLC KNGDIDYCEL
NARFGFRNII ADPVTFKTKS SYVALATLQA YTSMHLFFQF KTTSLDGLIL YNSGDGNDFI
VVELVKGYLH YVFDLGNGAN LIKGSSNKPL NDNQWHNVMI SRDTSNLHTV KIDTKITTQI
TAGARNLDLK SDLYIGGVAK ETYKSLPKLV HAKEGFQGCL ASVDLNGRLP DLISDALFCN
GQIERGCEGP STTCQEDSCS NQGVCLQQWD GFSCDCSMTS FSGPLCNDPG TTYIFSKGGG
QITYKWPPND RPSTRADRLA IGFSTVQKEA VLVRVDSSSG LGDYLELHIH QGKIGVKFNV
GTDDIAIEES NAIINDGKYH VVRFTRSGGN ATLQVDSWPV IERYPAGNND NERLAIARQR
IPYRLGRVVD EWLLDKGRQL TIFNSQATII IGGKEQGQPF QGQLSGLYYN GLKVLNMAAE
NDANIAIVGN VRLVGEVPSS MTTESTATAM QSEMSTSIME TTTTLATSTA RRGKPPTKEP
ISQTTDDILV ASAECPSDDE DIDPCEPSSG GLANPTRVGG REPYPGSAEV IRESSSTTGM
VVGIVAAAAL CILILLYAMY KYRNRDEGSY HVDESRNYIS NSAQSNGAVV KEKQPSSAKS
ANKNKKNKDK EYYV
