GFAP_BOVIN
ID GFAP_BOVIN Reviewed; 428 AA.
AC Q28115; Q0P5L4; Q866S9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glial fibrillary acidic protein;
DE Short=GFAP;
GN Name=GFAP;
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 [MRNA].
RC TISSUE=Subcommissural organ;
RX PubMed=10571109; DOI=10.1007/s004419900077;
RA Bouchard P., Ravet V., Meiniel R., Creveaux I., Meiniel A., Vellet A.,
RA Vigues B.;
RT "Use of a heterologous monoclonal antibody for cloning and detection of
RT glial fibrillary acidic protein in the bovine ventricular ependyma.";
RL Cell Tissue Res. 298:207-216(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-416.
RA Guertler M., Alter T., Froeb A., Lange B., Johne R., Luecker E.,
RA Fehlhaber K.;
RT "Nucleotide sequence of the bovine glial fibrillary acidic protein (GFAP)
RT gene.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 197-227.
RX PubMed=8010535;
RA Kirkpatrick B.W., Hart G.L.;
RT "Conformation polymorphisms and targeted marker development.";
RL Anim. Genet. 25:77-82(1994).
CC -!- FUNCTION: GFAP, a class-III intermediate filament, is a cell-specific
CC marker that, during the development of the central nervous system,
CC distinguishes astrocytes from other glial cells.
CC -!- SUBUNIT: Interacts with SYNM. {ECO:0000250|UniProtKB:P03995}.
CC -!- INTERACTION:
CC Q28115; Q96RG2: PASK; Xeno; NbExp=2; IntAct=EBI-907866, EBI-1042651;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14136}.
CC Note=Associated with intermediate filaments.
CC {ECO:0000250|UniProtKB:P14136}.
CC -!- PTM: Phosphorylated by PKN1. {ECO:0000250|UniProtKB:P14136}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; Y08255; CAA69422.1; -; mRNA.
DR EMBL; BC119892; AAI19893.1; -; mRNA.
DR EMBL; AY174179; AAO18221.1; ALT_TERM; Genomic_DNA.
DR EMBL; L19867; AAA51413.1; -; Genomic_DNA.
DR PIR; PC2280; PC2280.
DR RefSeq; NP_776490.2; NM_174065.2.
DR AlphaFoldDB; Q28115; -.
DR SMR; Q28115; -.
DR IntAct; Q28115; 2.
DR MINT; Q28115; -.
DR STRING; 9913.ENSBTAP00000017997; -.
DR iPTMnet; Q28115; -.
DR PaxDb; Q28115; -.
DR PeptideAtlas; Q28115; -.
DR PRIDE; Q28115; -.
DR Ensembl; ENSBTAT00000017997; ENSBTAP00000017997; ENSBTAG00000013534.
DR GeneID; 281189; -.
DR KEGG; bta:281189; -.
DR CTD; 2670; -.
DR VEuPathDB; HostDB:ENSBTAG00000013534; -.
DR VGNC; VGNC:29323; GFAP.
DR eggNOG; ENOG502RKU6; Eukaryota.
DR GeneTree; ENSGT00940000159539; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; Q28115; -.
DR OMA; QIHVEMD; -.
DR OrthoDB; 655109at2759; -.
DR TreeFam; TF330122; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000013534; Expressed in midbrain and 81 other tissues.
DR ExpressionAtlas; Q28115; baseline and differential.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:1904714; P:regulation of chaperone-mediated autophagy; IBA:GO_Central.
DR InterPro; IPR027701; GFAP.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR PANTHER; PTHR45652:SF9; PTHR45652:SF9; 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 Citrullination; Coiled coil; Cytoplasm; Intermediate filament; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..428
FT /note="Glial fibrillary acidic protein"
FT /id="PRO_0000063804"
FT DOMAIN 65..373
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..68
FT /note="Head"
FT REGION 69..100
FT /note="Coil 1A"
FT REGION 101..111
FT /note="Linker 1"
FT REGION 112..210
FT /note="Coil 1B"
FT REGION 211..226
FT /note="Linker 12"
FT REGION 227..248
FT /note="Coil 2A"
FT REGION 249..252
FT /note="Linker 2"
FT REGION 253..373
FT /note="Coil 2B"
FT REGION 374..428
FT /note="Tail"
FT MOD_RES 7
FT /note="Phosphothreonine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P14136"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P03995"
FT MOD_RES 13
FT /note="Phosphoserine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P14136"
FT MOD_RES 26
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="Phosphoserine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P14136"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 266
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47819"
FT MOD_RES 402
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 412
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT CONFLICT 265
FT /note="A -> R (in Ref. 1; CAA69422 and 3; AAO18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="L -> V (in Ref. 1; CAA69422 and 3; AAO18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..312
FT /note="ER -> DA (in Ref. 1; CAA69422 and 3; AAO18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="R -> Q (in Ref. 3; AAO18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="K -> P (in Ref. 1; CAA69422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 49512 MW; 8DCCDF3E848BAD05 CRC64;
MERRRVTSAT RRSYVSSSEM VVGGRRLGPG TRLSLARMPP PLPARVDFSL AGALNSGFKE
TRASERAEMM ELNDRFASYI EKVRFLEQQN KALAAELNQL RAKEPTKLAD VYQAELRELR
LRLDQLTANS ARLEVERDNL AQDLGTLRQK LQDETNQRLE AENNLAAYRQ EADEATLARL
DLERKIESLE EEIRFLRKIH EEEVRELQEQ LAQQQVHVEM DVAKPDLTAA LREIRTQYEA
VASSNMHEAE EWYRSKFADL NDAAARNAEL LRQAKHEAND YRRQLQALTC DLESLRGTNE
SLERQMREQE ERHAREAASY QEALARLEEE GQSLKDEMAR HLQEYQDLLN VKLALDIEIA
TYRKLLEGEE NRITIPVQTF SNLQIRETSL DTKSVSEGHL KRNIVVKTVE MRDGEVIKES
KQEHKDVM
