NXPH4_RAT
ID NXPH4_RAT Reviewed; 304 AA.
AC Q9Z2N4; Q642D9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Neurexophilin-4;
DE Flags: Precursor;
GN Name=Nxph4; Synonyms=Nph4;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May be signaling molecules that resemble neuropeptides and
CC that act by binding to alpha-neurexins and possibly other receptors.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain and kidney.
CC -!- PTM: May be proteolytically processed in neuron-like cells.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neurexophilin family. {ECO:0000305}.
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DR EMBL; AF042714; AAD02227.1; -; mRNA.
DR EMBL; BC081805; AAH81805.1; -; mRNA.
DR RefSeq; NP_067712.2; NM_021680.2.
DR RefSeq; XP_017450561.1; XM_017595072.1.
DR AlphaFoldDB; Q9Z2N4; -.
DR SMR; Q9Z2N4; -.
DR STRING; 10116.ENSRNOP00000050310; -.
DR GlyGen; Q9Z2N4; 4 sites.
DR iPTMnet; Q9Z2N4; -.
DR PhosphoSitePlus; Q9Z2N4; -.
DR PaxDb; Q9Z2N4; -.
DR GeneID; 59316; -.
DR KEGG; rno:59316; -.
DR UCSC; RGD:628723; rat.
DR CTD; 11247; -.
DR RGD; 628723; Nxph4.
DR eggNOG; ENOG502QPNQ; Eukaryota.
DR InParanoid; Q9Z2N4; -.
DR OrthoDB; 1030335at2759; -.
DR PhylomeDB; Q9Z2N4; -.
DR TreeFam; TF333047; -.
DR PRO; PR:Q9Z2N4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR InterPro; IPR010450; Nxph.
DR InterPro; IPR026845; NXPH/NXPE.
DR PANTHER; PTHR17103; PTHR17103; 1.
DR Pfam; PF06312; Neurexophilin; 2.
DR PIRSF; PIRSF038019; Neurexophilin; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..304
FT /note="Neurexophilin-4"
FT /id="PRO_0000020069"
FT REGION 24..84
FT /note="II"
FT REGION 85..163
FT /note="III"
FT REGION 164..220
FT /note="IV (linker domain)"
FT REGION 221..304
FT /note="V (Cys-rich)"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 191
FT /note="P -> T (in Ref. 2; AAH81805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 32945 MW; AD2B30B351DEDB4D CRC64;
MRLLPEWLLL LFGPWLLRKV ISGQIVESGR PQYLDLRPAM AGGGARGQQL PVPASSEGLN
PVRSWSWAWP ANHTGALARP GAAGGPPVPR TKRKPSIKAA RAKKIFGWGD FYFRVHTLKF
SLLVTGKIVD HVNGTFSVYF RHNSSSLGNL SVSIVPPSKR VEFGGVWLPG PAPHPLQSTL
ALEGVLPGLG PPLGMAGQGL GGNLGGALAG PLGGALGVPG AKESRAFNCH VEYEKTNRAR
KHRPCLYDPS QVCFTEHTQS QAAWLCAKPF KVICIFVSFL SFDYKLVQKV CPDYNFQSEH
PYFG