NXPH2_HUMAN
ID NXPH2_HUMAN Reviewed; 264 AA.
AC O95156; B7WP24; Q494R1; Q75QC3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Neurexophilin-2;
DE Flags: Precursor;
GN Name=NXPH2; Synonyms=NPH2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neuroblastoma;
RA Kawasaki A., Ohira M., Miyazaki K., Nakagawara A.;
RT "Cloning of a full-length human neurexophilin2 gene.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-264.
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 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: Expressed in brain and kidney.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB162675; BAD11132.1; -; mRNA.
DR EMBL; AC092620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101462; AAI01463.1; -; mRNA.
DR EMBL; BC101463; AAI01464.1; -; mRNA.
DR EMBL; BC104741; AAI04742.1; -; mRNA.
DR EMBL; AF043467; AAD02280.1; -; mRNA.
DR CCDS; CCDS46421.1; -.
DR RefSeq; NP_009157.1; NM_007226.2.
DR AlphaFoldDB; O95156; -.
DR SMR; O95156; -.
DR BioGRID; 116410; 34.
DR IntAct; O95156; 15.
DR STRING; 9606.ENSP00000272641; -.
DR GlyGen; O95156; 4 sites.
DR iPTMnet; O95156; -.
DR PhosphoSitePlus; O95156; -.
DR BioMuta; NXPH2; -.
DR MassIVE; O95156; -.
DR PaxDb; O95156; -.
DR PeptideAtlas; O95156; -.
DR PRIDE; O95156; -.
DR ProteomicsDB; 50673; -.
DR Antibodypedia; 51377; 105 antibodies from 23 providers.
DR DNASU; 11249; -.
DR Ensembl; ENST00000272641.4; ENSP00000272641.3; ENSG00000144227.5.
DR GeneID; 11249; -.
DR KEGG; hsa:11249; -.
DR MANE-Select; ENST00000272641.4; ENSP00000272641.3; NM_007226.3; NP_009157.1.
DR UCSC; uc002tvi.4; human.
DR CTD; 11249; -.
DR DisGeNET; 11249; -.
DR GeneCards; NXPH2; -.
DR HGNC; HGNC:8076; NXPH2.
DR HPA; ENSG00000144227; Tissue enhanced (brain, kidney, ovary).
DR MIM; 604635; gene.
DR neXtProt; NX_O95156; -.
DR OpenTargets; ENSG00000144227; -.
DR PharmGKB; PA31864; -.
DR VEuPathDB; HostDB:ENSG00000144227; -.
DR eggNOG; ENOG502QUPW; Eukaryota.
DR GeneTree; ENSGT00950000182883; -.
DR HOGENOM; CLU_067114_2_1_1; -.
DR InParanoid; O95156; -.
DR OMA; WDWLANV; -.
DR OrthoDB; 971662at2759; -.
DR PhylomeDB; O95156; -.
DR TreeFam; TF333047; -.
DR PathwayCommons; O95156; -.
DR SignaLink; O95156; -.
DR BioGRID-ORCS; 11249; 8 hits in 1059 CRISPR screens.
DR GenomeRNAi; 11249; -.
DR Pharos; O95156; Tdark.
DR PRO; PR:O95156; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95156; protein.
DR Bgee; ENSG00000144227; Expressed in pons and 74 other tissues.
DR Genevisible; O95156; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS:UniProtKB.
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..264
FT /note="Neurexophilin-2"
FT /id="PRO_0000020063"
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"
FT CONFLICT 7..12
FT /note="PLVVVP -> ARVLVT (in Ref. 4; AAD02280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29938 MW; E793B5AD69FD0E71 CRC64;
MRLRPLPLVV VPGLLQLLFC DSKEVVHATE GLDWEDKDAP GTLVGNVVHS RIISPLRLFV
KQSPVPKPGP MAYADSMENF WDWLANITEI QEPLARTKRR PIVKTGKFKK MFGWGDFHSN
IKTVKLNLLI TGKIVDHGNG TFSVYFRHNS TGLGNVSVSL VPPSKVVEFE VSPQSTLETK
ESKSFNCRIE YEKTDRAKKT ALCNFDPSKI CYQEQTQSHV SWLCSKPFKV ICIYIAFYSV
DYKLVQKVCP DYNYHSETPY LSSG
