AINX_BOVIN
ID AINX_BOVIN Reviewed; 499 AA.
AC Q08DH7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Alpha-internexin;
DE Short=Alpha-Inx;
GN Name=INA;
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=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). Forms
CC heterodimers with NEFL, NEFM or NEFH (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P23565}.
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; BC123743; AAI23744.1; -; mRNA.
DR RefSeq; NP_001069426.1; NM_001075958.1.
DR AlphaFoldDB; Q08DH7; -.
DR SMR; Q08DH7; -.
DR STRING; 9913.ENSBTAP00000003517; -.
DR PaxDb; Q08DH7; -.
DR PRIDE; Q08DH7; -.
DR Ensembl; ENSBTAT00000003517; ENSBTAP00000003517; ENSBTAG00000002717.
DR GeneID; 532236; -.
DR KEGG; bta:532236; -.
DR CTD; 9118; -.
DR VEuPathDB; HostDB:ENSBTAG00000002717; -.
DR VGNC; VGNC:30191; INA.
DR eggNOG; ENOG502RAU0; Eukaryota.
DR GeneTree; ENSGT00940000154418; -.
DR HOGENOM; CLU_012560_7_3_1; -.
DR InParanoid; Q08DH7; -.
DR OMA; EHYLCSA; -.
DR OrthoDB; 888678at2759; -.
DR TreeFam; TF330122; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000002717; Expressed in retina and 51 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0005883; C:neurofilament; IEA:Ensembl.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Developmental protein; Differentiation;
KW Glycoprotein; Intermediate filament; Neurogenesis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..499
FT /note="Alpha-internexin"
FT /id="PRO_0000285855"
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..499
FT /note="Tail"
FT REGION 431..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..459
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:0000250|UniProtKB:P46660"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23565"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16352"
SQ SEQUENCE 499 AA; 55396 MW; F83EAC87139B08C8 CRC64;
MSFGSEHYLC ASSSYRKVFG DGSRLSSRLS GAGGSGSFRS QSLSRSNVAS SAACSSASSL
GLGLAYRRSP ASDGLDLSQA AARTNEYKII RTNEKEQLQG LNDRFAVFIE KVHQLETQNR
ALEAELAALR QRHAEPSRVG ELFQRELRDL RAQLEEASSA RAQALLERDG LAEEVQRLRA
RCEEESRGRE GAERALKAQQ RDVDGATLAR LDLEKKVESL LDELAFVRQV HDEEVAELLA
TLQASSQAAA EVDVAVAKPD LSSALREIRA QYESLAAKNL QSAEEWYKSK FANLNEQAAR
STEAIRASRE EIHEYRRQLQ ARTIEIEGLR GANESLERQI LELEERHSAE VASYQDNIGQ
LENDLRNTKS EMARHLREYQ DLLNVKMALD IEIAAYRKLL EGEETRFSTS GLSISGLNPL
PNPSYLLPPR ILSSTTSKGS ATGLSLKKEE EEEEASKIAS KKTSQIGESF EEILEETVIS
TKKTEKSNIE ETTISSQKI
