ID   NXPH2_BOVIN             Reviewed;         264 AA.
AC   Q28145;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Neurexophilin-2;
DE            Short=Neurophilin-2;
DE   Flags: Precursor;
GN   Name=NXPH2; Synonyms=NPH2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
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   PROTEIN SEQUENCE OF 166-180.
RX   PubMed=8420960; DOI=10.1016/s0021-9258(18)53934-x;
RA   Petrenko A.G., Lazaryeva V.D., Geppert M., Tarasyuk T.A., Moomaw C.,
RA   Khokhlatchev A.V., Ushkaryov Y.A., Slaughter C., Nasimov I.V.,
RA   Suedhof T.C.;
RT   "Polypeptide composition of the alpha-latrotoxin receptor. High affinity
RT   binding protein consists of a family of related high molecular weight
RT   polypeptides complexed to a low molecular weight protein.";
RL   J. Biol. Chem. 268:1860-1867(1993).
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, only in a scattered subpopulation of neurons
CC       that probably represent inhibitory interneurons.
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; L27868; AAB18419.1; -; mRNA.
DR   RefSeq; NP_776831.1; NM_174406.2.
DR   AlphaFoldDB; Q28145; -.
DR   SMR; Q28145; -.
DR   STRING; 9913.ENSBTAP00000024152; -.
DR   PaxDb; Q28145; -.
DR   Ensembl; ENSBTAT00000024152; ENSBTAP00000024152; ENSBTAG00000018147.
DR   GeneID; 281956; -.
DR   KEGG; bta:281956; -.
DR   CTD; 11249; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018147; -.
DR   VGNC; VGNC:32381; NXPH2.
DR   eggNOG; ENOG502QUPW; Eukaryota.
DR   GeneTree; ENSGT00950000182883; -.
DR   HOGENOM; CLU_067114_2_1_1; -.
DR   InParanoid; Q28145; -.
DR   OMA; WDWLANV; -.
DR   OrthoDB; 971662at2759; -.
DR   TreeFam; TF333047; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000018147; Expressed in occipital lobe and 41 other tissues.
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; 1.
DR   PIRSF; PIRSF038019; Neurexophilin; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..264
FT                   /note="Neurexophilin-2"
FT                   /id="PRO_0000020062"
FT   REGION          23..90
FT                   /note="II"
FT   REGION          91..169
FT                   /note="III"
FT   REGION          170..178
FT                   /note="IV (linker domain)"
FT   REGION          179..264
FT                   /note="V (Cys-rich)"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   264 AA;  29977 MW;  592FEE9300B34A86 CRC64;
     MRLRPLPLVV VPGLLQLLFC DSEKVVHATE GLDWEDKDAT GTLVGNVVHS RIINPLRLFV
     KQSPVPKPGH LAYADSMENF WDWLANITEV QEPLARTKRR PIVKTGKFKK MFGWGDFHSN
     IKTVKLNLLI TGKIVDHGNG TFSVYFRHNS TGLGNVSVSL VPPSKVVEFE VSPQSTLETK
     ESKSFNCRIE YEKTDRAKKT ALCNFDPSKI CYQEQTQSHV SWLCSKPFKV ICIYIAFYSV
     DYKLVQKVCP DYNYHSETPY LSSG