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NXPH3_MOUSE
ID   NXPH3_MOUSE             Reviewed;         252 AA.
AC   Q91VX5;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Neurexophilin-3;
DE   Flags: Precursor;
GN   Name=Nxph3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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).
RN   [2]
RP   TISSUE SPECIFICITY.
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.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highest level in brain, present also in lung,
CC       kidney and testis. {ECO:0000269|PubMed:9570794}.
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; BC007167; AAH07167.1; -; mRNA.
DR   CCDS; CCDS25278.1; -.
DR   RefSeq; NP_570928.1; NM_130858.3.
DR   AlphaFoldDB; Q91VX5; -.
DR   SMR; Q91VX5; -.
DR   IntAct; Q91VX5; 2.
DR   STRING; 10090.ENSMUSP00000058254; -.
DR   GlyConnect; 2543; 5 N-Linked glycans (1 site).
DR   GlyGen; Q91VX5; 4 sites, 5 N-linked glycans (1 site).
DR   iPTMnet; Q91VX5; -.
DR   PhosphoSitePlus; Q91VX5; -.
DR   PaxDb; Q91VX5; -.
DR   PRIDE; Q91VX5; -.
DR   ProteomicsDB; 293817; -.
DR   Antibodypedia; 30401; 178 antibodies from 25 providers.
DR   DNASU; 104079; -.
DR   Ensembl; ENSMUST00000058866; ENSMUSP00000058254; ENSMUSG00000046719.
DR   GeneID; 104079; -.
DR   KEGG; mmu:104079; -.
DR   UCSC; uc007lal.1; mouse.
DR   CTD; 11248; -.
DR   MGI; MGI:1336188; Nxph3.
DR   VEuPathDB; HostDB:ENSMUSG00000046719; -.
DR   eggNOG; ENOG502QSZ5; Eukaryota.
DR   GeneTree; ENSGT00950000182883; -.
DR   HOGENOM; CLU_067114_2_0_1; -.
DR   InParanoid; Q91VX5; -.
DR   OMA; PSKTCYH; -.
DR   OrthoDB; 1098941at2759; -.
DR   PhylomeDB; Q91VX5; -.
DR   TreeFam; TF333047; -.
DR   BioGRID-ORCS; 104079; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q91VX5; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q91VX5; protein.
DR   Bgee; ENSMUSG00000046719; Expressed in cortical plate and 121 other tissues.
DR   ExpressionAtlas; Q91VX5; baseline and differential.
DR   Genevisible; Q91VX5; MM.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
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_0000020066"
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;  28183 MW;  A770645706435A7C CRC64;
     MQLTRCCFVF LVQGSLYLVI CGQDDGPPGS EDPEHDDHEG QPRPRVPRKR GHISPKSRPL
     ANSTLLGLLA PPGEVWGVLG QPPNRPKQSP LPSTKVKKIF GWGDFYSNIK TVALNLLVTG
     KIVDHGNGTF SVHFRHNATG QGNISISLVP PSKAVEFHQE QQIFIEAKAS KIFNCRMEWE
     KVERGRRTSL CTHDPAKICS RDHAQSSATW SCSQPFKVVC VYIAFYSTDY RLVQKVCPDY
     NYHSDTPYYP SG
 
 
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