AINX_MOUSE
ID AINX_MOUSE Reviewed; 501 AA.
AC P46660; Q61958; Q8VCW5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Alpha-internexin;
DE Short=Alpha-Inx;
DE AltName: Full=66 kDa neurofilament protein;
DE Short=NF-66;
DE Short=Neurofilament-66;
GN Name=Ina;
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 [GENOMIC DNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Spleen;
RX PubMed=7959004; DOI=10.1016/0378-1119(94)90163-5;
RA Chien C.-L., Liem R.K.H.;
RT "Characterization of the mouse gene encoding the neuronal intermediate
RT filament protein alpha-internexin.";
RL Gene 149:289-292(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8734438; DOI=10.1007/bf02527709;
RA Chan S.O., Chiu F.C.;
RT "The 66-kDa neurofilament protein (NF-66): sequence analysis and
RT evolution.";
RL Neurochem. Res. 21:449-455(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP PROTEIN SEQUENCE OF 17-24; 29-39; 46-83; 92-130; 139-145; 152-177; 202-210;
RP 216-228; 270-288; 291-300; 310-316; 323-366; 378-430; 431-438 AND 471-487,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP 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).
RN [8]
RP FUNCTION.
RX PubMed=22723690; DOI=10.1523/jneurosci.1081-12.2012;
RA Yuan A., Sasaki T., Kumar A., Peterhoff C.M., Rao M.V., Liem R.K.,
RA Julien J.P., Nixon R.A.;
RT "Peripherin is a subunit of peripheral nerve neurofilaments: implications
RT for differential vulnerability of CNS and peripheral nervous system
RT axons.";
RL J. Neurosci. 32:8501-8508(2012).
CC -!- FUNCTION: Class-IV neuronal intermediate filament that is able to self-
CC assemble. It is involved in the morphogenesis of neurons. It may form
CC an independent structural network without the involvement of other
CC neurofilaments or it may cooperate with NEFL to form the filamentous
CC backbone to which NEFM and NEFH attach to form the cross-bridges (By
CC similarity). May also cooperate with the neuronal intermediate filament
CC protein PRPH to form filamentous networks (PubMed:22723690).
CC {ECO:0000250, ECO:0000269|PubMed:22723690}.
CC -!- SUBUNIT: Forms homodimers (in vitro) (By similarity). Forms
CC heterodimers with NEFL, NEFM or NEFH (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P23565}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; L27220; AAA62617.1; -; Genomic_DNA.
DR EMBL; L36390; AAB37740.1; -; mRNA.
DR EMBL; BC018383; AAH18383.1; -; mRNA.
DR CCDS; CCDS38013.1; -.
DR PIR; I53868; I53868.
DR RefSeq; NP_666212.3; NM_146100.4.
DR AlphaFoldDB; P46660; -.
DR SMR; P46660; -.
DR BioGRID; 230487; 41.
DR IntAct; P46660; 19.
DR MINT; P46660; -.
DR STRING; 10090.ENSMUSP00000041347; -.
DR iPTMnet; P46660; -.
DR PhosphoSitePlus; P46660; -.
DR SwissPalm; P46660; -.
DR UCD-2DPAGE; P46660; -.
DR EPD; P46660; -.
DR jPOST; P46660; -.
DR MaxQB; P46660; -.
DR PaxDb; P46660; -.
DR PeptideAtlas; P46660; -.
DR PRIDE; P46660; -.
DR ProteomicsDB; 296007; -.
DR Antibodypedia; 1538; 498 antibodies from 41 providers.
DR DNASU; 226180; -.
DR Ensembl; ENSMUST00000037636; ENSMUSP00000041347; ENSMUSG00000034336.
DR GeneID; 226180; -.
DR KEGG; mmu:226180; -.
DR UCSC; uc008huk.1; mouse.
DR CTD; 9118; -.
DR MGI; MGI:96568; Ina.
DR VEuPathDB; HostDB:ENSMUSG00000034336; -.
DR eggNOG; ENOG502RAU0; Eukaryota.
DR GeneTree; ENSGT00940000154418; -.
DR HOGENOM; CLU_012560_7_3_1; -.
DR InParanoid; P46660; -.
DR OMA; EHYLCSA; -.
DR OrthoDB; 888678at2759; -.
DR PhylomeDB; P46660; -.
DR TreeFam; TF330122; -.
DR BioGRID-ORCS; 226180; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Ina; mouse.
DR PRO; PR:P46660; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P46660; protein.
DR Bgee; ENSMUSG00000034336; Expressed in cortical plate and 165 other tissues.
DR Genevisible; P46660; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005883; C:neurofilament; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IMP:SynGO.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IMP:SynGO.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IGI:MGI.
DR InterPro; IPR027703; Alpha-Inx.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR PANTHER; PTHR45652:SF18; PTHR45652:SF18; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Developmental protein; Differentiation;
KW Direct protein sequencing; Glycoprotein; Intermediate filament;
KW Neurogenesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..501
FT /note="Alpha-internexin"
FT /id="PRO_0000063784"
FT DOMAIN 94..407
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..87
FT /note="Head"
FT REGION 88..129
FT /note="Coil 1A"
FT REGION 130..142
FT /note="Linker 1"
FT REGION 143..238
FT /note="Coil 1B"
FT REGION 239..262
FT /note="Linker 2"
FT REGION 263..408
FT /note="Coil 2"
FT REGION 409..501
FT /note="Tail"
FT REGION 441..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16352"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16352"
FT CONFLICT 28
FT /note="R -> P (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="G -> A (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="E -> Q (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="L -> R (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="Q -> E (in Ref. 1; AAA62617)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Q -> L (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="S -> T (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 318..319
FT /note="QL -> HV (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="H -> D (in Ref. 1; AAA62617)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="L -> F (in Ref. 1; AAA62617)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="A -> G (in Ref. 1; AAA62617)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="E -> N (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="A -> T (in Ref. 1; AAA62617 and 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="G -> R (in Ref. 1; AAA62617)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="E -> D (in Ref. 1; AAA62617 and 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="E -> EEEE (in Ref. 1; AAA62617)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="E -> D (in Ref. 1; AAA62617 and 2; AAB37740)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="S -> L (in Ref. 2; AAB37740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 55383 MW; B3DEF649DEB29C3B CRC64;
MSFGSEHYLC SASSYRKVFG DSSRLSARLS GPGGSGSFRS QSLSRSNVAS TAACSSASSL
GLGLAYRRLP ASDGLDLSQA AARTNEYKII RTNEKEQLQG LNDRFAVFIE KVHQLETQNR
ALEAELAALR QRHAEPSRVG ELFQRELREL RAQLEEASSA RAQALLERDG LAEEVQRLRA
RCEEESRGRE GAERALKAQQ RDVDGATLAR LDLEKKVESL LDELAFVRQV HDEEVAELLA
TLQASSQAAA EVDVAVAKPD LTSALREIRA QYESLAAKNL QSAEEWYKSK FANLNEQAAR
STEAIRASRE EIHEYRRQLQ ARTIEIEGLR GANESLERQI LELEERHSAE VAGYQDSIGQ
LESDLRNTKS EMARHLREYQ DLLNVKMALD IEIAAYRKLL EGEETRFSTG GLSISGLNPL
PNPSYLLPPR ILSSTASKVS SAGLSLKKEE EEEEEEASKE VSKKTSKVGE GFEETLGEAV
ISTKKTGKSA TEESTSSSQK M
