ID   NXPH1_RAT               Reviewed;         271 AA.
AC   Q63366; Q3KRD4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Neurexophilin-1;
DE            Short=Neurophilin;
DE   Flags: Precursor;
GN   Name=Nxph1; Synonyms=Nph1;
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=8699246; DOI=10.1523/jneurosci.16-14-04360.1996;
RA   Petrenko A.G., Ullrich B., Missler M., Krasnoperov V., Rosahl T.W.,
RA   Suedhof T.C.;
RT   "Structure and evolution of neurexophilin.";
RL   J. Neurosci. 16:4360-4369(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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.
CC       Ligand for alpha-neurexins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highest level in brain.
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.
CC   -!- SIMILARITY: Belongs to the neurexophilin family. {ECO:0000305}.
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DR   EMBL; L27867; AAB18420.1; -; mRNA.
DR   EMBL; BC105770; AAI05771.1; -; mRNA.
DR   RefSeq; NP_037126.1; NM_012994.2.
DR   PDB; 6PNP; X-ray; 1.94 A; B=119-271.
DR   PDB; 6PNQ; X-ray; 1.95 A; B=119-271.
DR   PDBsum; 6PNP; -.
DR   PDBsum; 6PNQ; -.
DR   AlphaFoldDB; Q63366; -.
DR   SMR; Q63366; -.
DR   STRING; 10116.ENSRNOP00000011833; -.
DR   GlyGen; Q63366; 6 sites.
DR   iPTMnet; Q63366; -.
DR   PhosphoSitePlus; Q63366; -.
DR   PaxDb; Q63366; -.
DR   Ensembl; ENSRNOT00000011833; ENSRNOP00000011833; ENSRNOG00000008939.
DR   GeneID; 25501; -.
DR   KEGG; rno:25501; -.
DR   UCSC; RGD:3218; rat.
DR   CTD; 30010; -.
DR   RGD; 3218; Nxph1.
DR   eggNOG; ENOG502QQUX; Eukaryota.
DR   GeneTree; ENSGT00950000182883; -.
DR   InParanoid; Q63366; -.
DR   OrthoDB; 971662at2759; -.
DR   PhylomeDB; Q63366; -.
DR   PRO; PR:Q63366; -.
DR   Proteomes; UP000002494; Chromosome 4.
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   1: Evidence at protein level;
KW   3D-structure; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..271
FT                   /note="Neurexophilin-1"
FT                   /id="PRO_0000020061"
FT   REGION          22..97
FT                   /note="II"
FT   REGION          98..176
FT                   /note="III"
FT   REGION          177..185
FT                   /note="IV (linker domain)"
FT   REGION          186..271
FT                   /note="V (Cys-rich)"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   STRAND          122..129
FT                   /evidence="ECO:0007829|PDB:6PNP"
FT   STRAND          131..143
FT                   /evidence="ECO:0007829|PDB:6PNP"
FT   STRAND          145..168
FT                   /evidence="ECO:0007829|PDB:6PNP"
FT   STRAND          194..207
FT                   /evidence="ECO:0007829|PDB:6PNP"
FT   STRAND          219..232
FT                   /evidence="ECO:0007829|PDB:6PNP"
FT   STRAND          239..256
FT                   /evidence="ECO:0007829|PDB:6PNP"
FT   HELIX           259..261
FT                   /evidence="ECO:0007829|PDB:6PNP"
SQ   SEQUENCE   271 AA;  31017 MW;  472D12D0B071E97A CRC64;
     MQAACWYVLL LLQPTVYLVT CANLTNGGKS ELLKSGNSKS TLKHIWTESS KDLSISRLLS
     QTFRGKENGT DLDLRYDTPE PYSEQDLWDW LRNSTDLQEP RPRAKRRPIV KTGKFKKMFG
     WGDFHSNIKT VKLNLLITGK IVDHGNGTFS VYFRHNSTGQ GNVSVSLVPP TKIVEFDLAQ
     QTVIDAKDSK SFNCRIEYEK VDKATKNTLC NYDPSKTCYQ EQTQSHVSWL CSKPFKVICI
     YISFYSTDYK LVQKVCPDYN YHSDTPYFPS G