AINX_RAT
ID AINX_RAT Reviewed; 505 AA.
AC P23565;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Alpha-internexin;
DE Short=Alpha-Inx;
GN Name=Ina; Synonyms=Inexa;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=2311576; DOI=10.1002/j.1460-2075.1990.tb08169.x;
RA Fliegner K.-H., Ching G.Y., Liem R.K.H.;
RT "The predicted amino acid sequence of alpha-internexin is that of a novel
RT neuronal intermediate filament protein.";
RL EMBO J. 9:749-755(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1717465; DOI=10.1016/s0021-9258(18)55018-3;
RA Ching G.Y., Liem R.K.H.;
RT "Structure of the gene for the neuronal intermediate filament protein
RT alpha-internexin and functional analysis of its promoter.";
RL J. Biol. Chem. 266:19459-19468(1991).
RN [3]
RP PROTEIN SEQUENCE OF 46-83; 92-104; 121-130; 152-161; 216-228; 270-278;
RP 291-300; 323-330; 339-366; 387-397; 399-430 AND 439-447, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP SUBUNIT, INTERACTION WITH NEFL; NEFM AND NEFH, AND TISSUE SPECIFICITY.
RX PubMed=9388258; DOI=10.1074/jbc.272.49.31073;
RA Athlan E.S., Mushynski W.E.;
RT "Heterodimeric associations between neuronal intermediate filament
RT proteins.";
RL J. Biol. Chem. 272:31073-31078(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-474, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P46660}.
CC -!- SUBUNIT: Forms homodimers (in vitro) (PubMed:9388258). Forms
CC heterodimers with NEFL, NEFM or NEFH (in vitro) (PubMed:9388258).
CC {ECO:0000269|PubMed:9388258}.
CC -!- INTERACTION:
CC P23565; Q9EPI6: Nsmf; NbExp=5; IntAct=EBI-6899875, EBI-6899705;
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal root ganglion neurons (at
CC protein level). {ECO:0000269|PubMed:9388258}.
CC -!- DEVELOPMENTAL STAGE: Levels of this protein reach a maximum at
CC embryonic day 16 and decline into adulthood.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X52017; CAA36264.1; -; mRNA.
DR EMBL; M73049; AAA41444.1; -; Genomic_DNA.
DR PIR; A41023; A41023.
DR AlphaFoldDB; P23565; -.
DR SMR; P23565; -.
DR BioGRID; 246662; 8.
DR IntAct; P23565; 6.
DR MINT; P23565; -.
DR STRING; 10116.ENSRNOP00000027417; -.
DR iPTMnet; P23565; -.
DR PhosphoSitePlus; P23565; -.
DR World-2DPAGE; 0004:P23565; -.
DR jPOST; P23565; -.
DR PaxDb; P23565; -.
DR PRIDE; P23565; -.
DR UCSC; RGD:2911; rat.
DR RGD; 2911; Ina.
DR eggNOG; ENOG502RAU0; Eukaryota.
DR InParanoid; P23565; -.
DR PhylomeDB; P23565; -.
DR PRO; PR:P23565; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0005883; C:neurofilament; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; ISO:RGD.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042246; P:tissue regeneration; IEP:RGD.
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..505
FT /note="Alpha-internexin"
FT /id="PRO_0000063785"
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..505
FT /note="Tail"
FT REGION 438..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46660"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46660"
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:22673903"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16352"
FT CONFLICT 152..153
FT /note="AQ -> GE (in Ref. 1; CAA36264)"
FT /evidence="ECO:0000305"
FT CONFLICT 239..242
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 56115 MW; 287E548F0DA4D818 CRC64;
MSFGSEHYLC SASSYRKVFG DGSRLSARLS GPGASGSFRS 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 EGEETRFSTS GLSISGLNPL
PNPSYLLPPR ILSSTTSKVS SAGLSLKKEE EEEEEEEEGA SKEVTKKTSK VGESFEETLE
ETVVSTKKTE KSTIEEITTS SSQKM
