NR1BA_DANRE
ID NR1BA_DANRE Reviewed; 1470 AA.
AC A1XQX2;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Neurexin-1b;
DE AltName: Full=Neurexin Ib-alpha;
DE AltName: Full=Neurexin-1b-alpha;
DE Flags: Precursor;
GN Name=nrxn1b;
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=A1XQX2-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=A1XQX3-1; 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; DQ641426; ABG25163.1; -; mRNA.
DR AlphaFoldDB; A1XQX2; -.
DR SMR; A1XQX2; -.
DR STRING; 7955.ENSDARP00000123742; -.
DR PaxDb; A1XQX2; -.
DR PRIDE; A1XQX2; -.
DR ZFIN; ZDB-GENE-070206-3; nrxn1b.
DR eggNOG; KOG3514; Eukaryota.
DR InParanoid; A1XQX2; -.
DR PhylomeDB; A1XQX2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1470
FT /note="Neurexin-1b"
FT /id="PRO_0000412539"
FT TOPO_DOM 23..1397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1398..1418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1419..1470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..206
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 196..234
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 251..441
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 448..641
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 645..682
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 687..881
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 874..1049
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1052..1089
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1093..1291
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1448..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 200..212
FT /evidence="ECO:0000250"
FT DISULFID 206..221
FT /evidence="ECO:0000250"
FT DISULFID 223..233
FT /evidence="ECO:0000250"
FT DISULFID 405..441
FT /evidence="ECO:0000250"
FT DISULFID 612..641
FT /evidence="ECO:0000250"
FT DISULFID 649..660
FT /evidence="ECO:0000250"
FT DISULFID 654..669
FT /evidence="ECO:0000250"
FT DISULFID 671..681
FT /evidence="ECO:0000250"
FT DISULFID 1021..1049
FT /evidence="ECO:0000250"
FT DISULFID 1056..1067
FT /evidence="ECO:0000250"
FT DISULFID 1061..1076
FT /evidence="ECO:0000250"
FT DISULFID 1078..1088
FT /evidence="ECO:0000250"
SQ SEQUENCE 1470 AA; 161208 MW; 589A777C16BDE5E2 CRC64;
MMILHLGAHL LFIGLIVCKA NAGSSLRFTG SDEQWVAFPM WNACCESEMS FSVKTTHLNG
LLVYFDDEGF CDFLELHVHV GKLRLCFSIF CAESTCVLSD VAINDNRWHS VSIMRNFRNT
TLIVDDEVKW EEVKSKRRDM TVFSHLFLGG IPSELRSVSL QLTSKTVKDH TSFTGWIMDV
KVNDSEPAII SSAGVHEDLC GSENTCLNGG VCSVVEDKPT CDCSQTGYQG KDCSEGLAHL
MMLDRGMEEY VATFRGSEYF CYDLSLNPIQ SSSDEITLSF RTLQRNGLML HTGKIADYVN
LALKNGAVSL VINLGSGAFE ALVEPVNGKF NDNEWHDVKV LRNLRQHSGV GYAMVTISVD
GILTTTGYTQ EEYTMLGSDD FLYVGGSPST ADLPGSPVSN NFMGCLREVV YKNNDAELEL
SRLAYQGDPK LQIHGVVAFK CESVATLDAI TFETPESFLT LPKWNAKKSG SISFDFRTTE
PNGLLLFSCG RAKQHNKEAK SPVTLKVDFF AIEMLDGLLY LLLDMGSGTT KTLALNKKVN
DGEWYHVDFQ RDGKSGTISI NSVRTPYLCP GDSELLDLDD PLYLGGVPES SSGTVFPTGA
WSALLNYGYV GCVRDLFIDG RSVDVRRAAE LQRAAGVKPS CGKEPSGKCV SEPCLNRGVC
REGWSRYICD CTGTGFLGHS CERDATILSF DGSKFLKVQF SAAMHTEAED VSLRFRSLRA
YGVLMASTST HTTDTLRLEL EAGRVRLTVN LDCNRINCTT SKGPESLFAG QNLNDDEWHT
VRVIRRGKSL KLSVDDLPTV DGEIPGDHTQ LEFHNIETGI ITGKRQLPTM PSNFIGHLQS
LMFNGKPYID LCKNGDIDYC QTNAPIGFKS IIADPVTFKS CSSYVTLPSL QAYYYMYLFF
QFKTTSADGL ILYNSGDGND FIAVELVKGY LHYISDLGNG AHLIKGNSIK PLNDNHWHNV
MISRDPNNLH TVRIDTKTTS QTTLGAKNLD LKGDLFVGGV PEQMYKDLPK LVHAKEGFQG
CLASVDLNGR LPDLMTEALV CIGQIERGCE GPSSSCEEDS CANQGVCLQQ WENFTCDCSM
TTYAGPLCAD PGSTYVFGRQ GGVITYSWPP HDRPSTRVDR LALGFITLME DATLVRVDSS
AGLGDYLKLH IVKGNVVAVF NVGTYDINIE ENGKLVNDGN YHIVRLTRSG GNATLQVDDL
PVIERFPPGH IDSHRLGTGR LPYRRLVEES LPKNGRQLTI FNSQMTIRIG GWQKQQVSGF
QGQMSGFYYN GLKVFSMAAD GDPNVRMEGS VRLVGELQSS STPHGGATVY QSSVTEISST
TSNTITITYS TPADEQQTTD ELLVASAECP SDDEDIDPCE PSSGTLCCFV PPAGPTGPAI
SSFPGPAEVF RESNGTTGMV VGIVAGAALC ILILLYAMYK YRNRDEGSYH VDESRNYICN
SNGAALKEKN TADDDSGSKS KKNKNKEYYV
