NXPH1_BOVIN
ID NXPH1_BOVIN Reviewed; 271 AA.
AC Q5E9M6; Q08DQ7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Neurexophilin-1;
DE Flags: Precursor;
GN Name=NXPH1;
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; BT020894; AAX08911.1; -; mRNA.
DR EMBL; BC123618; AAI23619.1; -; mRNA.
DR RefSeq; NP_001029934.1; NM_001034762.1.
DR AlphaFoldDB; Q5E9M6; -.
DR SMR; Q5E9M6; -.
DR STRING; 9913.ENSBTAP00000009085; -.
DR PaxDb; Q5E9M6; -.
DR PRIDE; Q5E9M6; -.
DR GeneID; 614571; -.
DR KEGG; bta:614571; -.
DR CTD; 30010; -.
DR eggNOG; ENOG502QQUX; Eukaryota.
DR InParanoid; Q5E9M6; -.
DR OrthoDB; 971662at2759; -.
DR Proteomes; UP000009136; 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; 1.
DR PIRSF; PIRSF038019; Neurexophilin; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..271
FT /note="Neurexophilin-1"
FT /id="PRO_0000250711"
FT REGION 22..97
FT /note="II"
FT /evidence="ECO:0000250"
FT REGION 98..176
FT /note="III"
FT /evidence="ECO:0000250"
FT REGION 177..185
FT /note="IV (linker domain)"
FT /evidence="ECO:0000250"
FT REGION 186..271
FT /note="V (Cys-rich)"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 271 AA; 31018 MW; 59BF7C3153DAC1D9 CRC64;
MQAACWYVLL LLQPTVYLVT CANLTNGGKS ELLKSGGSKS TLKHIWTESS KDLSISRLLS
QTFRGKENDT DLDLRYDTPE PYSEQDLWDW LRNSTDLQEP RPRAKRRPIV KTGKFKKMFG
WGDFHSNIKT VKLNLLITGK IVDHGNGTFS VYFRHNSTGQ GNVSVSLVPP TKIVEFDLAQ
QTVIDAKDSK SFNCRIEYEK VDKATKNTLC NYDPSKTCYQ EQTQSHVSWL CSKPFKVICI
YISFYSTDYK LVQKVCPDYN YHSDTPYFPS G