GFAP_RAT
ID GFAP_RAT Reviewed; 430 AA.
AC P47819; A7REI0; Q7TQ31; Q9R1Q3; Q9Z2S0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Glial fibrillary acidic protein;
DE Short=GFAP;
GN Name=Gfap;
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] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RX PubMed=1629938; DOI=10.1002/jnr.490320102;
RA Feinstein D.L., Weinmaster G.A., Milner R.J.;
RT "Isolation of cDNA clones encoding rat glial fibrillary acidic protein:
RT expression in astrocytes and in Schwann cells.";
RL J. Neurosci. Res. 32:1-14(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=10336251;
RX DOI=10.1002/(sici)1097-4547(19990501)56:3<219::aid-jnr1>3.0.co;2-2;
RA Condorelli D.F., Nicoletti V.G., Barresi V., Conticello S.G., Caruso A.,
RA Tendi E.A., Giuffrida Stella A.M.;
RT "Structural features of the rat GFAP gene and identification of a novel
RT alternative transcript.";
RL J. Neurosci. Res. 56:219-228(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-152.
RC TISSUE=Liver;
RX PubMed=7897704; DOI=10.1002/jnr.490390610;
RA Condorelli D.F., Nicoletti V.G., Barresi V., Caruso A., Conticello S.,
RA de Vellis J., Giuffrida-Stella A.;
RT "Tissue-specific DNA methylation patterns of the rat glial fibrillary
RT acidic protein gene.";
RL J. Neurosci. Res. 39:694-707(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 375-430 (ISOFORM 3).
RX PubMed=17203480; DOI=10.1002/glia.20475;
RA Blechingberg J., Holm I.E., Nielsen K.B., Jensen T.H., Joergensen A.L.,
RA Nielsen A.L.;
RT "Identification and characterization of GFAPkappa, a novel glial fibrillary
RT acidic protein isoform.";
RL Glia 55:497-507(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 389-421 (ISOFORM 2).
RX PubMed=12837269; DOI=10.1016/s0888-7543(03)00106-x;
RA Singh R., Nielsen A.L., Johansen M.G., Jorgensen A.L.;
RT "Genetic polymorphism and sequence evolution of an alternatively spliced
RT exon of the glial fibrillary acidic protein gene, GFAP.";
RL Genomics 82:185-193(2003).
RN [7]
RP PROTEIN SEQUENCE OF 11-21; 28-68; 87-93; 110-119; 123-150; 161-171;
RP 188-199; 208-234; 238-256; 259-274; 286-298; 318-365; 375-388; 396-403 AND
RP 410-429, PARTIAL PROTEIN SEQUENCE (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=2153890; DOI=10.1016/0169-328x(90)90066-m;
RA Nichols N.R., Osterburg H.H., Masters J.N., Millar S.L., Finch C.E.;
RT "Messenger RNA for glial fibrillary acidic protein is decreased in rat
RT brain following acute and chronic corticosterone treatment.";
RL Brain Res. Mol. Brain Res. 7:1-7(1990).
RN [9]
RP PHOSPHORYLATION AT THR-108 AND THR-381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-80; THR-148; SER-267;
RP SER-321 AND SER-383, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: 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 -!- SUBUNIT: [Isoform 2]: Interacts with PSEN1 (via N-terminus).
CC {ECO:0000250|UniProtKB:P14136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14136}.
CC Note=Associated with intermediate filaments.
CC {ECO:0000250|UniProtKB:P14136}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=GFAP alpha {ECO:0000303|PubMed:17203480};
CC IsoId=P47819-1; Sequence=Displayed;
CC Name=2; Synonyms=GFAP delta {ECO:0000269|PubMed:10336251}, GFAP epsilon
CC {ECO:0000303|PubMed:12837269};
CC IsoId=P47819-2; Sequence=VSP_017054;
CC Name=3; Synonyms=GFAP kappa {ECO:0000303|PubMed:17203480};
CC IsoId=P47819-3; Sequence=VSP_061021, VSP_061022;
CC -!- TISSUE SPECIFICITY: Expressed in the cortex and hippocampus. Expression
CC decreases following acute and chronic corticosterone treatment.
CC {ECO:0000269|PubMed:2153890}.
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; U03700; AAA20540.1; -; mRNA.
DR EMBL; AF028784; AAD01873.1; -; Genomic_DNA.
DR EMBL; AF028784; AAD01874.2; -; Genomic_DNA.
DR EMBL; BC088851; AAH88851.1; -; mRNA.
DR EMBL; Z48978; CAA88842.1; -; Genomic_DNA.
DR EMBL; DQ979831; ABL14185.1; -; mRNA.
DR EMBL; AY142198; AAN87911.1; -; Genomic_DNA.
DR PIR; I56572; I56572.
DR RefSeq; NP_058705.2; NM_017009.2. [P47819-1]
DR AlphaFoldDB; P47819; -.
DR SMR; P47819; -.
DR BioGRID; 246558; 5.
DR IntAct; P47819; 4.
DR MINT; P47819; -.
DR STRING; 10116.ENSRNOP00000032389; -.
DR iPTMnet; P47819; -.
DR PhosphoSitePlus; P47819; -.
DR SwissPalm; P47819; -.
DR World-2DPAGE; 0004:P47819; -.
DR jPOST; P47819; -.
DR PaxDb; P47819; -.
DR PRIDE; P47819; -.
DR ABCD; P47819; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000034401; ENSRNOP00000032389; ENSRNOG00000002919. [P47819-1]
DR Ensembl; ENSRNOT00000093266; ENSRNOP00000076226; ENSRNOG00000002919. [P47819-2]
DR GeneID; 24387; -.
DR KEGG; rno:24387; -.
DR UCSC; RGD:2679; rat. [P47819-1]
DR CTD; 2670; -.
DR RGD; 2679; Gfap.
DR eggNOG; ENOG502RKU6; Eukaryota.
DR GeneTree; ENSGT00940000159539; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; P47819; -.
DR OMA; QIHVEMD; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P47819; -.
DR PRO; PR:P47819; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002919; Expressed in Ammon's horn and 14 other tissues.
DR ExpressionAtlas; P47819; baseline and differential.
DR Genevisible; P47819; RN.
DR GO; GO:0097450; C:astrocyte end-foot; ISO:RGD.
DR GO; GO:0097449; C:astrocyte projection; IDA:MGI.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0097386; C:glial cell projection; ISO:RGD.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; IDA:MGI.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:RGD.
DR GO; GO:0014002; P:astrocyte development; ISO:RGD.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; ISO:RGD.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0045103; P:intermediate filament-based process; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0031102; P:neuron projection regeneration; ISO:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
DR GO; GO:0010625; P:positive regulation of Schwann cell proliferation; ISO:RGD.
DR GO; GO:1904714; P:regulation of chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051580; P:regulation of neurotransmitter uptake; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; IDA:RGD.
DR GO; GO:0014010; P:Schwann cell proliferation; IEA:Ensembl.
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 Alternative splicing; Citrullination; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Intermediate filament; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..430
FT /note="Glial fibrillary acidic protein"
FT /id="PRO_0000063807"
FT DOMAIN 67..375
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..70
FT /note="Head"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..102
FT /note="Coil 1A"
FT REGION 103..113
FT /note="Linker 1"
FT REGION 114..212
FT /note="Coil 1B"
FT REGION 213..228
FT /note="Linker 12"
FT REGION 229..250
FT /note="Coil 2A"
FT REGION 251..254
FT /note="Linker 2"
FT REGION 255..375
FT /note="Coil 2B"
FT REGION 376..430
FT /note="Tail"
FT MOD_RES 7
FT /note="Phosphothreonine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P14136"
FT MOD_RES 11
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P03995"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 21
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P03995"
FT MOD_RES 34
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Phosphoserine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P14136"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P03995"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 268
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 404
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 414
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT VAR_SEQ 389..430
FT /note="ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM -> GGKSTK
FT EGEGHKVTRHLKRLTIQVIPIQALARL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017054"
FT VAR_SEQ 389..409
FT /note="ETSLDTKSVSEGHLKRNIVVK -> GQYSGALWERVMNPLPPPPGL (in
FT isoform 3)"
FT /id="VSP_061021"
FT VAR_SEQ 410..430
FT /note="Missing (in isoform 3)"
FT /id="VSP_061022"
FT CONFLICT 273
FT /note="L -> V (in Ref. 1; AAA20540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 49957 MW; 6437A1F784E37D1A CRC64;
MERRRITSAR RSYASSETMV RGHGPTRHLG TIPRLSLSRM TPPLPARVDF SLAGALNAGF
KETRASERAE MMELNDRFAS YIEKVRFLEQ QNKALAAELN QLRAKEPTKL ADVYQAELRE
LRLRLDQLTT NSARLEVERD NLTQDLGTLR QKLQDETNLR LEAENNLAVY RQEADEATLA
RVDLERKVES LEEEIQFLRK IHEEEVRELQ EQLAQQQVHV EMDVAKPDLT AALREIRTQY
EAVATSNMQE TEEWYRSKFA DLTDVASRNA ELLRQAKHEA NDYRRQLQAL TCDLESLRGT
NESLERQMRE QEERHARESA SYQEALARLE EEGQSLKEEM ARHLQEYQDL LNVKLALDIE
IATYRKLLEG EENRITIPVQ TFSNLQIRET SLDTKSVSEG HLKRNIVVKT VEMRDGEVIK
ESKQEHKDVM
