NRN1_BOVIN
ID NRN1_BOVIN Reviewed; 142 AA.
AC Q2KIC6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Neuritin;
DE Flags: Precursor;
GN Name=NRN1;
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].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC112687; AAI12688.1; -; mRNA.
DR RefSeq; NP_001039903.1; NM_001046438.1.
DR AlphaFoldDB; Q2KIC6; -.
DR STRING; 9913.ENSBTAP00000013021; -.
DR PaxDb; Q2KIC6; -.
DR Ensembl; ENSBTAT00000013021; ENSBTAP00000013021; ENSBTAG00000009873.
DR GeneID; 538730; -.
DR KEGG; bta:538730; -.
DR CTD; 51299; -.
DR VEuPathDB; HostDB:ENSBTAG00000009873; -.
DR VGNC; VGNC:32265; NRN1.
DR eggNOG; ENOG502RZNR; Eukaryota.
DR GeneTree; ENSGT00530000063853; -.
DR HOGENOM; CLU_135101_0_0_1; -.
DR InParanoid; Q2KIC6; -.
DR OMA; KCDAVFR; -.
DR OrthoDB; 1469106at2759; -.
DR TreeFam; TF332589; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000009873; Expressed in occipital lobe and 92 other tissues.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; 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; PTHR15902; 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_0000262510"
FT PROPEP 117..142
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000262511"
FT LIPID 116
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 142 AA; 15279 MW; AF3150CC8D76D1DF CRC64;
MGLKLNGRYI SLILAVQIAY LVQAVRAAGK CDAVFKGFSD CLLKLGDSMA NYPQGLDDKT
NIKTVCTYWE DFHSCTVTAL TDCQEGAKDM WDKLRKESKN LNIQGSLFEL CGGGNGAAGP
LLPALPVLLV SLSAALATWL SF
