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NR1AA_DANRE
ID   NR1AA_DANRE             Reviewed;        1491 AA.
AC   A1XQX0;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Neurexin-1a;
DE   AltName: Full=Neurexin Ia-alpha;
DE   AltName: Full=Neurexin-1a-alpha;
DE   Flags: Precursor;
GN   Name=nrxn1a;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RX   PubMed=17041151; DOI=10.1093/molbev/msl147;
RA   Rissone A., Monopoli M., Beltrame M., Bussolino F., Cotelli F., Arese M.;
RT   "Comparative genome analysis of the neurexin gene family in Danio rerio:
RT   insights into their functions and evolution.";
RL   Mol. Biol. Evol. 24:236-252(2007).
CC   -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC       recognition and cell adhesion.
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=2;
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=Alpha;
CC         IsoId=A1XQX0-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=A1XQX1-1; Sequence=External;
CC   -!- DEVELOPMENTAL STAGE: After the very early developmental stages, the
CC       expression levels decrease and remain relatively constant until around
CC       24 h, with the onset of an increase of expression that continues till
CC       the larval stages. {ECO:0000269|PubMed:17041151}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR   EMBL; DQ641424; ABG25161.1; -; mRNA.
DR   RefSeq; NP_001073490.1; NM_001080021.2. [A1XQX0-1]
DR   AlphaFoldDB; A1XQX0; -.
DR   SMR; A1XQX0; -.
DR   STRING; 7955.ENSDARP00000087526; -.
DR   PaxDb; A1XQX0; -.
DR   Ensembl; ENSDART00000111239; ENSDARP00000102322; ENSDARG00000061647. [A1XQX0-1]
DR   GeneID; 565531; -.
DR   KEGG; dre:565531; -.
DR   CTD; 565531; -.
DR   ZFIN; ZDB-GENE-070206-1; nrxn1a.
DR   eggNOG; KOG3514; Eukaryota.
DR   GeneTree; ENSGT00940000163749; -.
DR   InParanoid; A1XQX0; -.
DR   OrthoDB; 35129at2759; -.
DR   PhylomeDB; A1XQX0; -.
DR   TreeFam; TF321302; -.
DR   Reactome; R-DRE-6794361; Neurexins and neuroligins.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000061647; Expressed in brain and 7 other tissues.
DR   ExpressionAtlas; A1XQX0; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0002040; P:sprouting angiogenesis; IMP:ZFIN.
DR   CDD; cd00110; LamG; 6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
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; PS50026; EGF_3; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE   2: Evidence at transcript level;
KW   Alternative promoter usage; Alternative splicing; Calcium; Cell adhesion;
KW   Disulfide bond; EGF-like domain; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..1491
FT                   /note="Neurexin-1a"
FT                   /id="PRO_0000412537"
FT   TOPO_DOM        28..1415
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1416..1436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1437..1491
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..208
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          198..236
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          263..460
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          467..661
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          665..702
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          707..880
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          894..1069
FT                   /note="Laminin G-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1072..1109
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1113..1314
FT                   /note="Laminin G-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          1318..1408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1457..1491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1473..1491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         309
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         394
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        202..214
FT                   /evidence="ECO:0000250"
FT   DISULFID        208..223
FT                   /evidence="ECO:0000250"
FT   DISULFID        225..235
FT                   /evidence="ECO:0000250"
FT   DISULFID        424..460
FT                   /evidence="ECO:0000250"
FT   DISULFID        632..661
FT                   /evidence="ECO:0000250"
FT   DISULFID        669..680
FT                   /evidence="ECO:0000250"
FT   DISULFID        674..689
FT                   /evidence="ECO:0000250"
FT   DISULFID        691..701
FT                   /evidence="ECO:0000250"
FT   DISULFID        1041..1069
FT                   /evidence="ECO:0000250"
FT   DISULFID        1076..1087
FT                   /evidence="ECO:0000250"
FT   DISULFID        1081..1096
FT                   /evidence="ECO:0000250"
FT   DISULFID        1098..1108
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1491 AA;  164313 MW;  BC00B3E400CE8473 CRC64;
     MSFSMRNGAH LIWIGLLVCC LVDMGASMEF TGAEGQWARF PMWNACCESE MSFNMKTKSA
     HGLLVYFDDE GFCDFLELLI HNGRLSLRFS IFCAEPATVF SDTAVNDSRW HAVTLRRNFK
     NTTLVVDEEI KWVEVKSKRR DMTVFSHLFL GGIPPELRSV ALRLTSSAIK DEVPYKGWIT
     NLRVNGSEPV LIGSDGVNSD ICEADHICLN GGVCSIVNDE PICDCSETGF QGKDCSEEEA
     YVGGLAHLMM GDQGKRKERE EYMATFKGSE YFCYDLSPNP IQSSSDEITL SFKTLQRNGL
     MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG KFNDNAWHDV KVTRNLRQHS
     GIGHAMVNKL HCSVTISVDG ILTTTGYTQE DYTMLGSDDF FYVGGSPSTA DLPGSPVSNN
     FMGCLKEVVY KNNDVRLELS RLAKLGDPKM KVSGVVAFKC ENVATLDPVT FETPESFITL
     DKWSAKKAGS ISFDFRTTEP NGLLLFSHGK PKPQQQKDPK SPKTLKVDFF AIEMLDGHLY
     LLLDMGSGTT KTRAVNKKVN DGEWYHVDFQ RDGRSGTISV NSIRTPYNAP GESEILDLDD
     KLYLGGLPED RAGLIFPTEV WTALLNYGYV GCVRDLFMDG QSKDIRRIAE AQRAVGVKPS
     CSKEPPKQCL SNPCLNSGTC REGWNRYVCD CSGTGYLGRS CERDATILSY DGSKFMKIQL
     PVVMHTEAED VSLRFRSQRA YGVLMATTSQ NSADTLRLEL DGGRVRLTVN LDCIRINCTT
     SKGPETIFSG QNLNDNEWHT VRVVRRGKSL KLMVDDLQPS EGQITGDHTQ LEFHNVETGI
     VTEKRYMPAV PSNFIGHLQG LSFNGMSYID LCKNGDIDYC ELNAMIGYRS IVADPVTFKS
     RSSYVTLPTL QAYYSMHLFF QFKTTSPDGL ILYNRGDGND FIVVELVKGY LHYVSDLGNG
     AHLIKGNSNT PLNDNHWHNV MISRDTNNLH TVKIDTKITT QTTMGAKNLD LKGDLYVGGV
     AKDMYKDLPK LVHSKEGFQG CLASVDLNGR LPDLQSDALS TAGQVERGCE GPSTTCQEDS
     CSNQGVCLQQ WEGFSCDCSM TSYGGPLCND PGTTYIFGRD GGLIVYTWPP NDRPSTRADR
     LAVGFSTQQK DAVLVRVDSS SGLGDYLQLQ IERGNIKVVF NVGTDDINIE ETSKFVNDGK
     YHIVRFTRSG GNATLQVDDL PVIERYPSGN IDNERLAIAR QRIPYRLGRV VDDWLLDKGR
     QLTIFNSQTT IKIGGWEKGS RPFQGQLSGL YYNGLKVLNM AAEGDPNVRV EGSARLVGDM
     PSSSITPQSS VSAAGNRSET SPSITDITTT TASNRQGKQT TTPQDDLLVA SAECPSDDED
     IDPCDPSSGG LAHPPLPEAK GYPSPEVIRE SSSTTGMVVG IVAAAALCIL ILLYAMYKYR
     NRDEGSYHVD ESRNYISNSA TQPNGAAVKE KPIGVPKNKK DKKNKDKEYY V
 
 
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