NXPH3_RAT
ID NXPH3_RAT Reviewed; 252 AA.
AC Q9Z2N5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Neurexophilin-3;
DE Flags: Precursor;
GN Name=Nxph3; Synonyms=Nph3;
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].
RC TISSUE=Brain;
RX PubMed=9570794; DOI=10.1523/jneurosci.18-10-03630.1998;
RA Missler M., Suedhof T.C.;
RT "Neurexophilins form a conserved family of neuropeptide-like
RT glycoproteins.";
RL J. Neurosci. 18:3630-3638(1998).
CC -!- FUNCTION: May be signaling molecules that resemble neuropeptides.
CC Ligand for alpha-neurexins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain. Detected in several other tissues.
CC -!- PTM: May be proteolytically processed at the boundary between the N-
CC terminal non-conserved and the central conserved domain in neuron-like
CC cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neurexophilin family. {ECO:0000305}.
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DR EMBL; AF042713; AAD02226.1; -; mRNA.
DR RefSeq; NP_067711.1; NM_021679.1.
DR AlphaFoldDB; Q9Z2N5; -.
DR SMR; Q9Z2N5; -.
DR STRING; 10116.ENSRNOP00000007133; -.
DR GlyGen; Q9Z2N5; 4 sites.
DR PaxDb; Q9Z2N5; -.
DR GeneID; 59315; -.
DR KEGG; rno:59315; -.
DR CTD; 11248; -.
DR RGD; 620693; Nxph3.
DR eggNOG; ENOG502QSZ5; Eukaryota.
DR InParanoid; Q9Z2N5; -.
DR OrthoDB; 1098941at2759; -.
DR PhylomeDB; Q9Z2N5; -.
DR PRO; PR:Q9Z2N5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR InterPro; IPR010450; Nxph.
DR InterPro; IPR026845; NXPH/NXPE.
DR PANTHER; PTHR17103; PTHR17103; 1.
DR Pfam; PF06312; Neurexophilin; 1.
DR PIRSF; PIRSF038019; Neurexophilin; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..252
FT /note="Neurexophilin-3"
FT /id="PRO_0000020067"
FT REGION 23..75
FT /note="II"
FT REGION 27..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..157
FT /note="III"
FT REGION 158..166
FT /note="IV (linker domain)"
FT REGION 167..252
FT /note="V (Cys-rich)"
FT COMPBIAS 28..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 252 AA; 28225 MW; 5FF10603CE66D8BA CRC64;
MQLTRCCFVF LVQGSLYLVI CGQEDGPPGS EDPEHDDHEG QPRPRVPRKR GHISPKSRPL
ANSTLLGLLA PPGEVWGILG QPPNRPKQSP LPSTKVKKIF GWGDFYSNIK TVALNLLVTG
KIVDHGNGTF SVHFRHNATG QGNISISLVP PSKAVEFHQE QQIFIEAKAS KIFNCRMEWE
KVERGRRTSL CTHDPAKICS RDHAQSSATW SCSQPFKIVC VYIAFYSTDY RLVQKVCPDY
NYHSDTPYYP SG