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Database: UniProt
Entry: Q99PJ0
LinkDB: Q99PJ0
Original site: Q99PJ0 
ID   NTRI_MOUSE              Reviewed;         344 AA.
AC   Q99PJ0;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Neurotrimin;
DE   Flags: Precursor;
GN   Name=Ntm; Synonyms=Hnt, Nt;
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 [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RA   Kim T.H., Choi S.C., Kim J., Jeon J.W., Kim K.D., Lee S.H.;
RT   "Cloning and expression of mouse neurotrimin gene in the developing nervous
RT   system.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Neural cell adhesion molecule.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC       {ECO:0000305}.
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DR   EMBL; AF282980; AAK00276.1; -; mRNA.
DR   EMBL; BC023307; AAH23307.1; -; mRNA.
DR   CCDS; CCDS90526.1; -.
DR   AlphaFoldDB; Q99PJ0; -.
DR   SMR; Q99PJ0; -.
DR   IntAct; Q99PJ0; 2.
DR   MINT; Q99PJ0; -.
DR   STRING; 10090.ENSMUSP00000074578; -.
DR   GlyConnect; 2559; 4 N-Linked glycans (1 site).
DR   GlyCosmos; Q99PJ0; 7 sites, 4 glycans.
DR   GlyGen; Q99PJ0; 9 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR   iPTMnet; Q99PJ0; -.
DR   PhosphoSitePlus; Q99PJ0; -.
DR   SwissPalm; Q99PJ0; -.
DR   MaxQB; Q99PJ0; -.
DR   PaxDb; 10090-ENSMUSP00000074578; -.
DR   PeptideAtlas; Q99PJ0; -.
DR   ProteomicsDB; 293772; -.
DR   Antibodypedia; 33124; 244 antibodies from 31 providers.
DR   Ensembl; ENSMUST00000115237.8; ENSMUSP00000110892.2; ENSMUSG00000059974.11.
DR   UCSC; uc009oqt.1; mouse.
DR   AGR; MGI:2446259; -.
DR   MGI; MGI:2446259; Ntm.
DR   VEuPathDB; HostDB:ENSMUSG00000059974; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   GeneTree; ENSGT00940000158679; -.
DR   InParanoid; Q99PJ0; -.
DR   OMA; DESWSVK; -.
DR   PhylomeDB; Q99PJ0; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   ChiTaRS; Ntm; mouse.
DR   PRO; PR:Q99PJ0; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q99PJ0; Protein.
DR   Bgee; ENSMUSG00000059974; Expressed in primary motor cortex and 225 other cell types or tissues.
DR   ExpressionAtlas; Q99PJ0; baseline and differential.
DR   Genevisible; Q99PJ0; MM.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
DR   PANTHER; PTHR42757; IGLON FAMILY OF IMMUNOGLOBULIN SUPERFAMILY-RELATED; 1.
DR   PANTHER; PTHR42757:SF9; NEUROTRIMIN; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW   Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..321
FT                   /note="Neurotrimin"
FT                   /id="PRO_0000015112"
FT   PROPEP          322..344
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000015113"
FT   DOMAIN          39..126
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          136..218
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          222..309
FT                   /note="Ig-like C2-type 3"
FT   LIPID           321
FT                   /note="GPI-anchor amidated asparagine; alternate"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine; alternate"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        157..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        243..295
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        75
FT                   /note="L -> P (in Ref. 1; AAK00276)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="S -> G (in Ref. 1; AAK00276)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="T -> I (in Ref. 1; AAK00276)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="E -> Q (in Ref. 1; AAK00276)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213
FT                   /note="R -> P (in Ref. 1; AAK00276)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="I -> F (in Ref. 1; AAK00276)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   344 AA;  37984 MW;  C885BBA52C148554 CRC64;
     MGVCGYLFLP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID
     NRVTRVAWLN RSTILYAGND KWCLDPRVVL LSNTQTQYSI EIQNVDVYDE GPYTCSVQTD
     NHPKTSRVHL IVQVSPKIVE ISSDISINEG NNISLTCIAT GRPEPTVTWR HISPKAVGFV
     SEDEYLEIQG ITREQSGEYE CSASNDVAAP VVRRVKVTVN YPPYISEAKG TGVPVGQKGT
     LQCEASAVPS AEFQWFKDDK RLVEGKKGVK VENRPFLSKL TFFNVSEHDY GNYTCVASNK
     LGHTNASIML FGPGAVSEVN NGTSRRAGCI WLLPLLVLHL LLKF
//
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