NTRI_MOUSE
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 03-AUG-2022, entry version 151.
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 GlyGen; Q99PJ0; 7 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q99PJ0; -.
DR PhosphoSitePlus; Q99PJ0; -.
DR SwissPalm; Q99PJ0; -.
DR MaxQB; Q99PJ0; -.
DR PaxDb; Q99PJ0; -.
DR PeptideAtlas; Q99PJ0; -.
DR PRIDE; Q99PJ0; -.
DR ProteomicsDB; 293772; -.
DR Antibodypedia; 33124; 218 antibodies from 31 providers.
DR Ensembl; ENSMUST00000115237; ENSMUSP00000110892; ENSMUSG00000059974.
DR UCSC; uc009oqt.1; mouse.
DR MGI; MGI:2446259; Ntm.
DR VEuPathDB; HostDB:ENSMUSG00000059974; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000158679; -.
DR InParanoid; Q99PJ0; -.
DR OMA; PITKRDF; -.
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 222 other tissues.
DR ExpressionAtlas; Q99PJ0; baseline and differential.
DR Genevisible; Q99PJ0; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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; -; 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 Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 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
