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NRX3A_RAT
ID   NRX3A_RAT               Reviewed;        1578 AA.
AC   Q07310; Q07280; Q07311; Q07312; Q07313; Q07314;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Neurexin-3;
DE   AltName: Full=Neurexin III-alpha;
DE   AltName: Full=Neurexin-3-alpha;
DE   Flags: Precursor;
GN   Name=Nrxn3;
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], AND ALTERNATIVE SPLICING.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=8341647; DOI=10.1073/pnas.90.14.6410;
RA   Ushkaryov Y.A., Suedhof T.C.;
RT   "Neurexin III alpha: extensive alternative splicing generates membrane-
RT   bound and soluble forms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6410-6414(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   PubMed=7695896; DOI=10.1016/0896-6273(95)90306-2;
RA   Ullrich B., Ushkaryov Y.A., Suedhof T.C.;
RT   "Cartography of neurexins: more than 1000 isoforms generated by alternative
RT   splicing and expressed in distinct subsets of neurons.";
RL   Neuron 14:497-507(1995).
RN   [3]
RP   PROTEIN SEQUENCE OF N-TERMINUS, AND INTERACTION WITH NXPH1.
RX   PubMed=9856994; DOI=10.1074/jbc.273.52.34716;
RA   Missler M., Hammer R.E., Suedhof T.C.;
RT   "Neurexophilin binding to alpha-neurexins. A single LNS domain functions as
RT   an independently folding ligand-binding unit.";
RL   J. Biol. Chem. 273:34716-34723(1998).
RN   [4]
RP   INTERACTION WITH CASK.
RX   PubMed=8786425; DOI=10.1523/jneurosci.16-08-02488.1996;
RA   Hata Y., Butz S., Suedhof T.C.;
RT   "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent
RT   protein kinase domain identified by interaction with neurexins.";
RL   J. Neurosci. 16:2488-2494(1996).
RN   [5]
RP   INTERACTION WITH ALPHA-DYSTROGLYCAN.
RX   PubMed=11470830; DOI=10.1083/jcb.200105003;
RA   Sugita S., Saito F., Tang J., Satz J., Campbell K., Suedhof T.C.;
RT   "A stoichiometric complex of neurexins and dystroglycan in brain.";
RL   J. Cell Biol. 154:435-445(2001).
CC   -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC       recognition and cell adhesion. May mediate intracellular signaling.
CC   -!- SUBUNIT: The laminin G-like domain 2 binds to NXPH1. Isoforms alpha 4B
CC       bind to alpha-dystroglycan. The cytoplasmic C-terminal region binds to
CC       CASK. {ECO:0000269|PubMed:11470830, ECO:0000269|PubMed:8786425,
CC       ECO:0000269|PubMed:9856994}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Secreted. Note=Some isoforms seems to
CC       be secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=19;
CC         Comment=There are five major alternatively spliced sites, each of
CC         which may be spliced in up to twelve different ways. Combinatorial
CC         splicing at each of these five sites may lead to the generation of at
CC         least 288 isoforms but for simplicity only individual splice events
CC         are explicitly described below. Isoforms Alpha 5A to isoform Alpha 5H
CC         lack the transmembrane domain. Experimental confirmation may be
CC         lacking for some isoforms.;
CC       Name=1; Synonyms=Alpha-5I;
CC         IsoId=Q07310-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha-1B;
CC         IsoId=Q07310-2; Sequence=VSP_003524;
CC       Name=3; Synonyms=Alpha-1C;
CC         IsoId=Q07310-3; Sequence=VSP_003521;
CC       Name=4; Synonyms=Alpha-1D;
CC         IsoId=Q07310-4; Sequence=VSP_003521, VSP_003524;
CC       Name=5; Synonyms=Alpha-1E;
CC         IsoId=Q07310-5; Sequence=VSP_003523;
CC       Name=6; Synonyms=Alpha-1F;
CC         IsoId=Q07310-6; Sequence=VSP_003522;
CC       Name=7; Synonyms=Alpha-3B;
CC         IsoId=Q07310-7; Sequence=VSP_003525;
CC       Name=8; Synonyms=Alpha-4B;
CC         IsoId=Q07310-8; Sequence=VSP_003526;
CC       Name=9; Synonyms=Alpha-5A;
CC         IsoId=Q07310-9; Sequence=VSP_003528, VSP_003529;
CC       Name=10; Synonyms=Alpha-5B;
CC         IsoId=Q07310-10; Sequence=VSP_003527, VSP_003528, VSP_003529;
CC       Name=11; Synonyms=Alpha-5C;
CC         IsoId=Q07310-11; Sequence=VSP_003528, VSP_003530;
CC       Name=12; Synonyms=Alpha-5D;
CC         IsoId=Q07310-12; Sequence=VSP_003527, VSP_003528, VSP_003530;
CC       Name=13; Synonyms=Alpha-5E;
CC         IsoId=Q07310-13; Sequence=VSP_003528, VSP_003531;
CC       Name=14; Synonyms=Alpha-5F;
CC         IsoId=Q07310-14; Sequence=VSP_003527, VSP_003528, VSP_003531;
CC       Name=15; Synonyms=Alpha-5G;
CC         IsoId=Q07310-15; Sequence=VSP_003528, VSP_003532;
CC       Name=16; Synonyms=Alpha-5H;
CC         IsoId=Q07310-16; Sequence=VSP_003527, VSP_003528, VSP_003532;
CC       Name=17; Synonyms=Alpha-5J;
CC         IsoId=Q07310-17; Sequence=VSP_003527;
CC       Name=18; Synonyms=Alpha-5K;
CC         IsoId=Q07310-18; Sequence=VSP_003528;
CC       Name=19; Synonyms=Alpha-5L;
CC         IsoId=Q07310-19; Sequence=VSP_003527, VSP_003528;
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR   EMBL; L14851; AAA02853.1; -; mRNA.
DR   EMBL; L14851; AAA02854.1; -; mRNA.
DR   EMBL; L14851; AAA02855.1; -; mRNA.
DR   EMBL; L14851; AAA02856.1; -; mRNA.
DR   EMBL; L14851; AAA02857.1; -; mRNA.
DR   EMBL; L14851; AAA02858.1; -; mRNA.
DR   PIR; I48216; I48216.
DR   RefSeq; NP_446269.2; NM_053817.2. [Q07310-1]
DR   AlphaFoldDB; Q07310; -.
DR   SMR; Q07310; -.
DR   BioGRID; 250475; 3.
DR   ELM; Q07310; -.
DR   IntAct; Q07310; 1.
DR   MINT; Q07310; -.
DR   STRING; 10116.ENSRNOP00000060600; -.
DR   GlyGen; Q07310; 7 sites.
DR   iPTMnet; Q07310; -.
DR   PhosphoSitePlus; Q07310; -.
DR   PaxDb; Q07310; -.
DR   PRIDE; Q07310; -.
DR   GeneID; 116508; -.
DR   KEGG; rno:116508; -.
DR   UCSC; RGD:620212; rat. [Q07310-1]
DR   CTD; 9369; -.
DR   RGD; 620212; Nrxn3.
DR   eggNOG; KOG3514; Eukaryota.
DR   InParanoid; Q07310; -.
DR   OrthoDB; 35129at2759; -.
DR   PhylomeDB; Q07310; -.
DR   Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030534; P:adult behavior; ISO:RGD.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0007612; P:learning; ISO:RGD.
DR   GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR   GO; GO:0035176; P:social behavior; ISO:RGD.
DR   GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR   GO; GO:0071625; P:vocalization behavior; ISO:RGD.
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   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Metal-binding; Reference proteome; Repeat; Secreted; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:9856994"
FT   CHAIN           28..1578
FT                   /note="Neurexin-3"
FT                   /id="PRO_0000019500"
FT   TOPO_DOM        28..1503
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1504..1524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1525..1578
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..202
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          198..235
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          260..444
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          451..643
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          647..684
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          689..861
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          875..1050
FT                   /note="Laminin G-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1053..1090
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1094..1294
FT                   /note="Laminin G-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          1328..1352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1546..1578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1560..1578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         308
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         378
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        761
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        202..213
FT                   /evidence="ECO:0000250"
FT   DISULFID        207..222
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..234
FT                   /evidence="ECO:0000250"
FT   DISULFID        408..444
FT                   /evidence="ECO:0000250"
FT   DISULFID        614..643
FT                   /evidence="ECO:0000250"
FT   DISULFID        651..662
FT                   /evidence="ECO:0000250"
FT   DISULFID        656..671
FT                   /evidence="ECO:0000250"
FT   DISULFID        673..683
FT                   /evidence="ECO:0000250"
FT   DISULFID        1022..1050
FT                   /evidence="ECO:0000250"
FT   DISULFID        1057..1068
FT                   /evidence="ECO:0000250"
FT   DISULFID        1062..1077
FT                   /evidence="ECO:0000250"
FT   DISULFID        1079..1089
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         237..256
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003522"
FT   VAR_SEQ         237..242
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003521"
FT   VAR_SEQ         243..256
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003523"
FT   VAR_SEQ         253..256
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003524"
FT   VAR_SEQ         754..763
FT                   /note="DCIRINCNSS -> G (in isoform 7)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003525"
FT   VAR_SEQ         1210..1239
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003526"
FT   VAR_SEQ         1369..1371
FT                   /note="Missing (in isoform 10, isoform 12, isoform 14,
FT                   isoform 16, isoform 17 and isoform 19)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003527"
FT   VAR_SEQ         1372..1478
FT                   /note="Missing (in isoform 9, isoform 10, isoform 11,
FT                   isoform 12, isoform 13, isoform 14, isoform 15, isoform 16,
FT                   isoform 18 and isoform 19)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003528"
FT   VAR_SEQ         1479..1578
FT                   /note="ANPTEPGIRRVPGASEVIRESNSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT                   DEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV -> VLERRII
FT                   LNLKTNAHPKSLQSKTC (in isoform 11 and isoform 12)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003530"
FT   VAR_SEQ         1479..1578
FT                   /note="ANPTEPGIRRVPGASEVIRESNSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT                   DEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV -> DILLKSF
FT                   (in isoform 13 and isoform 14)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003531"
FT   VAR_SEQ         1479..1578
FT                   /note="ANPTEPGIRRVPGASEVIRESNSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT                   DEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV -> ATTTTKK
FT                   SNFQECGNSICPRAFLHNFLL (in isoform 15 and isoform 16)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003532"
FT   VAR_SEQ         1479..1578
FT                   /note="ANPTEPGIRRVPGASEVIRESNSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT                   DEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV -> ARSSNAA
FT                   RITPCRPYMDMATHLHIYPSHLHLLCSTLIDTPLPFPHPFFPMLPPSLALLKFMCCHPP
FT                   P (in isoform 9 and isoform 10)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003529"
SQ   SEQUENCE   1578 AA;  173994 MW;  936CF8529143D0C7 CRC64;
     MSFTLHSVFF TLKVSSFLGS LVGLCLGLEF MGLPNQWARY LRWDASTRSD LSFQFKTNVS
     TGLLLYLDDG GVCDFLCLSL VDGRVQLRFS MDCAETTVLS NKQVNDSSWH FLMVSRDRVR
     TGLVIDGEGQ SGELRAQRPY MDVVSDLFLG GGPADIRPSA LTLDGVQNMP GFKGLMLDLK
     YGNSEPRLLG SQSVQLEAEG PCGERPCENG GICFLLDGHP TCDCSTTGYG GTLCSEDVSQ
     GPGLSHLMMS EQGRSKAREE NVATFRGSEY LSYDLSQNPI QSSSSEITLS FKTWQRNGLI
     LHTGKSADYV NLALKDGAVS LVINLGSGAF EAIVEPVNGK FNDNAWHDVK VTRNLRQVTI
     SVDGILTTTG YTQEDYTMLG SDDSSYVGPS PSTADLPGSP VSNNFMGCLK EVVYKNNDIR
     LELSRLARIG ATKMKIYGEV VFKCENVATL DPINFETPEA YISLPKWNTK RMGSISFDFR
     TTEPNGLILL THGKPQERKD VRSQKNTKVD FFAVELLDGN LYLLLDMGSG TIKVKATQKK
     ANDGEWYHVD IQRDGRSGTI SVNSRRTPFT ASGQSEILDL EGDMYLGGLP ENRAGLILPT
     ELWTAMLNYG YVGCIRDLFI DGRSKNIRQL AEMQNAAGVK SSCSRMSAKQ CDSYPCKNNA
     VCKDGWNRFI CDCTGTGYWG RTCEREASIL SYDGSMYMKV IMPMVMHTEA EDVSFRFMSQ
     RAYGLLVATT SRDSADTLRL ELDGGRVKLM VNLDCIRINC NSSKGPETLY AGQKLNDNEW
     HTVRVVRRGK SLKLTVDDDV AEGTMVGDHT RLEFHNIETG IMTEKRYISV VPSSFIGHLQ
     SLMFNGLLYI DLCKNGDIDY CELKARFGLR NIIADPVTFK TKSSYLTLAT LQAYTSMHLF
     FQFKTTSADG FILFNSGDGN NFIAVELVKG YIHYVFDLGN GPNVIKGNSD RPLNDNQWHN
     VVITRDNSNT HSLKVDTKVV TQVINGAKNL DLKGDLYMAG LAQGMYSNLP KLVASRDGFQ
     GCLASVDLNG RLPDLINDAL HRSGQIDRGC EGPSTTCQED SCANQGVCMQ QWEGFTCDCS
     MTSYSGNQCN DPGATYIFGK SGGLILYTWP ANDRPSTRSD RLAVGFSTTV KDGVLVRIDS
     APGLGDFLQL HIEQGKIGVV FNIGTVDISI KEERTPVNDG KYHVVRFTRN GANATLQVDN
     WPVNEHYPTG NTDNERRQMV KQKIPFKYNR PVEEWLQEKG RQLTIFNTQA QIAIGGKDKG
     RLFQGQLSGL YYDGLKVLNM AAENNPNIKI NGSVRLVGEV PSVSGTTHTT SMPPEMSTTV
     METTTTMATT TTRKNRSTAS IQPTSDDLVS SAECSSDDED FVECEPSTGR SDKSLSTSIF
     EGGYKAHAPK WESKDFRPNK VSETSRTTTT SLSPELIRFT ASSSSGMVPK LPAGKMNNRD
     LKPQPDIVLL PLPTAYELDS TKLKSPLITC PMFRNVPTAN PTEPGIRRVP GASEVIRESN
     STTGMVVGIV AAAALCILIL LYAMYKYRNR DEGSYQVDET RNYISNSAQS NGTLMKEKQA
     SSKSGHKKQK NKDKEYYV
 
 
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