NR3AB_DANRE
ID NR3AB_DANRE Reviewed; 672 AA.
AC A1XQY0;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Neurexin-3a-beta;
DE AltName: Full=Neurexin IIIb-beta;
DE Contains:
DE RecName: Full=Neurexin-3a-beta, soluble form;
DE Contains:
DE RecName: Full=Neurexin-3a-beta, C-terminal fragment;
DE Short=NRXN3-CTF;
DE Flags: Precursor;
GN Name=nrxn3a;
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=A1XQY0-1; Sequence=Displayed;
CC Name=1a;
CC IsoId=A1XQX8-1; Sequence=External;
CC Name=2a; Synonyms=Soluble form;
CC IsoId=A1XQX8-2; 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 -!- MISCELLANEOUS: [Isoform 1b]: Produced by alternative promoter usage.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; DQ641434; ABG25171.1; -; mRNA.
DR AlphaFoldDB; A1XQY0; -.
DR SMR; A1XQY0; -.
DR ZFIN; ZDB-GENE-070206-9; nrxn3a.
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; IEA:UniProtKB-KW.
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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..672
FT /note="Neurexin-3a-beta"
FT /id="PRO_0000412550"
FT CHAIN 36..535
FT /note="Neurexin-3a-beta, soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412551"
FT CHAIN 536..672
FT /note="Neurexin-3a-beta, C-terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412552"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 89..289
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 72745 MW; 783B6D47EB065C47 CRC64;
MRPSRVAAPF RGGRQGLSPW MWSLTLGCIV GSVWSSSPGL DNSVVAAGPP GVATSYTHPE
HPVHNPRHHA SPISIYRSPA FLRSGHAGTT YIFGKGGGLL SFNWPANERP STRTDRLTVG
FSTSLKDGIL IRIDSAPGLG DYLMLHIEQG KIGVTFNIGT ADITVQESST AVNDGKYHVV
RFTRNGGNAT LQVDNWAINE HFPSGNSDNE RIQMANKKIP FKYARPVEEW LQEKGRQLTI
FNTQATITIG GSDRKRPFQG QLSGLYYNGL KVLNMAAQGN PNIKINGSVR LVGEVPAAGS
ARTTALPPEM STTFIETTTT MSTTTTRKHR TPPTIQTTDD MVSSAECSSD DEDFAECEGH
AGGLGGELVF PVIVKDPLEL PSVATRTPSI PFPPTLTIIE TTKESLSMAT EAGVPCLSDG
GSDDCGDDDD DDDDDGLMIS GYGSGEAYDS NLPPTDDEDF YTTFSLVTDK TLSSSTFEGG
YKAHAPKWGS KDFRPNKVFD SGRTTTASFS PKLSRSTTTS TPPKLPAGKM NHRELKPQPD
IVLLPLPTSY EVDNTKMKSP LITSPMFRNV PTAIPTEPGI RRVPGASEVV RESSSTTGMV
VGIVAAAALC ILILLYAMYK YRNRDEGSYQ VDETRNYITN SAQSNGAVMK DKQQSTKSGN
KKQKNKDKEY YV
