ID   NRN1_HUMAN              Reviewed;         142 AA.
AC   Q9NPD7; B2RA93; Q7Z4Y1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-MAY-2024, entry version 140.
DE   RecName: Full=Neuritin;
DE   Flags: Precursor;
GN   Name=NRN1; Synonyms=NRN;
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=Adrenal cortex;
RX   PubMed=9122250; DOI=10.1073/pnas.94.6.2648;
RA   Naeve G.S., Ramakrishnan M., Kramer R., Hevroni D., Citri Y., Theill L.E.;
RT   "Neuritin: a gene induced by neural activity and neurotrophins that
RT   promotes neuritogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:2648-2653(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhou H., Huang X., Zhou Y., Hu S., Tang X., Yuan J., Qiang B.;
RT   "Isolation and cloning of a novel human cDNA encoding rat neuritin
RT   homolog.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Fan Y.X., Yu L., Zhang X.N., Xin Y.R., Wang X.K., Zhao S.Y.;
RT   "Cloning of a novel human cDNA homologous to Rattus norvegicus neuritin
RT   mRNA.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pericardium;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Uterus;
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: Promotes neurite outgrowth and especially branching of
CC       neuritic processes in primary hippocampal and cortical cells.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the outer core of AMPAR complex. AMPAR complex
CC       consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC       (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC       in a twofold symmetry. One of the two pairs of distinct binding sites
CC       is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC       CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC       complex is complemented by outer core constituents binding directly to
CC       the GluA/GRIA proteins at sites distinct from the interaction sites of
CC       the inner core constituents. Outer core constituents include at least
CC       PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC       inner and outer core serve as a platform for other, more peripherally
CC       associated AMPAR constituents. Alone or in combination, these auxiliary
CC       subunits control the gating and pharmacology of the AMPAR complex and
CC       profoundly impact their biogenesis and protein processing (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}. Synapse {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neuritin 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; AF136631; AAF62371.1; -; mRNA.
DR   EMBL; AF114833; AAP97232.1; -; mRNA.
DR   EMBL; AL136307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK314095; BAG36790.1; -; mRNA.
DR   EMBL; CH471087; EAW55184.1; -; Genomic_DNA.
DR   EMBL; BC002683; AAH02683.1; -; mRNA.
DR   EMBL; BC042019; AAH42019.1; -; mRNA.
DR   CCDS; CCDS4495.1; -.
DR   RefSeq; NP_001265639.1; NM_001278710.1.
DR   RefSeq; NP_001265640.1; NM_001278711.1.
DR   RefSeq; NP_057672.1; NM_016588.2.
DR   AlphaFoldDB; Q9NPD7; -.
DR   BioGRID; 119450; 39.
DR   IntAct; Q9NPD7; 23.
DR   STRING; 9606.ENSP00000480483; -.
DR   iPTMnet; Q9NPD7; -.
DR   PhosphoSitePlus; Q9NPD7; -.
DR   BioMuta; NRN1; -.
DR   MassIVE; Q9NPD7; -.
DR   PaxDb; 9606-ENSP00000480483; -.
DR   PeptideAtlas; Q9NPD7; -.
DR   ProteomicsDB; 81975; -.
DR   Pumba; Q9NPD7; -.
DR   Antibodypedia; 24561; 214 antibodies from 31 providers.
DR   DNASU; 51299; -.
DR   Ensembl; ENST00000244766.7; ENSP00000244766.2; ENSG00000124785.9.
DR   Ensembl; ENST00000616243.1; ENSP00000484055.1; ENSG00000124785.9.
DR   GeneID; 51299; -.
DR   KEGG; hsa:51299; -.
DR   MANE-Select; ENST00000244766.7; ENSP00000244766.2; NM_016588.3; NP_057672.1.
DR   UCSC; uc003mwu.4; human.
DR   AGR; HGNC:17972; -.
DR   CTD; 51299; -.
DR   DisGeNET; 51299; -.
DR   GeneCards; NRN1; -.
DR   HGNC; HGNC:17972; NRN1.
DR   HPA; ENSG00000124785; Tissue enhanced (brain).
DR   MIM; 607409; gene.
DR   neXtProt; NX_Q9NPD7; -.
DR   OpenTargets; ENSG00000124785; -.
DR   PharmGKB; PA38477; -.
DR   VEuPathDB; HostDB:ENSG00000124785; -.
DR   eggNOG; ENOG502RZNR; Eukaryota.
DR   GeneTree; ENSGT00530000063853; -.
DR   HOGENOM; CLU_135101_0_0_1; -.
DR   InParanoid; Q9NPD7; -.
DR   OMA; CAYWEDF; -.
DR   OrthoDB; 5346986at2759; -.
DR   PhylomeDB; Q9NPD7; -.
DR   TreeFam; TF332589; -.
DR   PathwayCommons; Q9NPD7; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   SignaLink; Q9NPD7; -.
DR   SIGNOR; Q9NPD7; -.
DR   BioGRID-ORCS; 51299; 11 hits in 1149 CRISPR screens.
DR   ChiTaRS; NRN1; human.
DR   GenomeRNAi; 51299; -.
DR   Pharos; Q9NPD7; Tbio.
DR   PRO; PR:Q9NPD7; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9NPD7; Protein.
DR   Bgee; ENSG00000124785; Expressed in cerebellar cortex and 179 other cell types or tissues.
DR   ExpressionAtlas; Q9NPD7; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:1990138; P:neuron projection extension; IBA:GO_Central.
DR   InterPro; IPR026144; Neuritin_fam.
DR   PANTHER; PTHR15902:SF1; NEURITIN; 1.
DR   PANTHER; PTHR15902; NEURITIN-RELATED; 1.
DR   Pfam; PF15056; NRN1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Signal; Synapse.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..116
FT                   /note="Neuritin"
FT                   /id="PRO_0000262512"
FT   PROPEP          117..142
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000262513"
FT   LIPID           116
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        48..49
FT                   /note="SM -> TW (in Ref. 3; AAP97232)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55..56
FT                   /note="GL -> AW (in Ref. 3; AAP97232)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113..115
FT                   /note="SGN -> RAT (in Ref. 3; AAP97232)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   142 AA;  15333 MW;  6C3C3DAC8D6392E6 CRC64;
     MGLKLNGRYI SLILAVQIAY LVQAVRAAGK CDAVFKGFSD CLLKLGDSMA NYPQGLDDKT
     NIKTVCTYWE DFHSCTVTAL TDCQEGAKDM WDKLRKESKN LNIQGSLFEL CGSGNGAAGS
     LLPAFPVLLV SLSAALATWL SF
//