NR3BB_DANRE
ID NR3BB_DANRE Reviewed; 675 AA.
AC A1XQY3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Neurexin-3b-beta;
DE AltName: Full=Neurexin IIIb-beta;
DE Contains:
DE RecName: Full=Neurexin-3b-beta, soluble form;
DE Contains:
DE RecName: Full=Neurexin-3b-beta, C-terminal fragment;
DE Short=NRXN3-CTF;
DE Flags: Precursor;
GN Name=nrxn3b;
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=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=A1XQY3-1; Sequence=Displayed;
CC Name=1a;
CC IsoId=A1XQY1-1; Sequence=External;
CC Name=2a; Synonyms=Soluble form;
CC IsoId=A1XQY1-2; 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 -!- 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}.
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DR EMBL; DQ641437; ABG25174.1; -; mRNA.
DR AlphaFoldDB; A1XQY3; -.
DR SMR; A1XQY3; -.
DR ZFIN; ZDB-GENE-070206-10; nrxn3b.
DR ChiTaRS; nrxn3b; zebrafish.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative promoter usage; Alternative splicing; Angiogenesis;
KW Cell adhesion; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..675
FT /note="Neurexin-3b-beta"
FT /id="PRO_0000412554"
FT CHAIN 31..536
FT /note="Neurexin-3b-beta, soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412555"
FT CHAIN 537..665
FT /note="Neurexin-3b-beta, C-terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412556"
FT TOPO_DOM 31..599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 81..281
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 313..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 73888 MW; 5E9EFBB243B43F1D CRC64;
MRPHFKTRYP QWLSCMLPLV TGCVFGAVWG SNLDSTVVLS SSTFSHSETQ HHHHLAGAQH
HPPSIAIYRS PASLRGGHAG ATYIFGKGGG LIMYTWPNNE RPSTRTDRLA VGFSTTIKDG
ILVRIDSAPR LGDYIMLHIE EGKVCVTFNI GTVDISVKEM TTEVNDGKYH VVRFTRNGGN
ATLQVDNWPI NEHFPSGNSD IERFQMANKK IPFKYTRPVE DWLHEKGRQL TIFNTQATIS
IGGNDRKRPY QGQLSGLYYN GLKVLNMAAE GHANIKINGS VRLVGDVPTS RSPSRTTTSM
PPEMSTTFIE TTTTLSTTTT RKQRSPPTIQ TTDDIVSSAE CSSDDEDLEE CDGGHTGGEL
VIPVLVEDPI DIPPISTRVP FIPLPPTLHP VLTIIETTKE SLSIATEAGV PCFSDQGRDD
CDDDDGDDDD GDGLVISGFG SGEVFDSSLP PTDDEDFYTT FSLVTDKILT TSTYEGGYKA
LAPKWEEKDF KPKKPSEVGR ITAIPPLPDL RSSAASPVRP EPAPKIPAGK MNNREVKPQP
DIVLLPLPTS FDMDGTKPKG PYITQPMLRT IPSALPTVPG IRRVPPGASE VIRESSSTTG
MVVGIVSAAA LCILILLYAM YKYRNRDEGS YQVDETRNYI SNSAQNNGTV VKDKQPSTKG
ASNKRPKDKD KEYYV
