TRAP1_DICDI
ID TRAP1_DICDI Reviewed; 711 AA.
AC Q86L04; Q550G4; Q8MYB0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=TNF receptor-associated protein 1 homolog, mitochondrial;
DE Short=TNFR-associated protein 1 homolog;
DE Short=Trap1 homolog;
DE Flags: Precursor;
GN Name=trap1; ORFNames=DDB_G0276947;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Morita T., Saitoh K., Amagai A., Maeda Y.;
RT "Novel functions of a Dictyostelium TRAP1 homologue.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12372338; DOI=10.1006/excr.2002.5620;
RA Morita T., Amagai A., Maeda Y.;
RT "Unique behavior of a dictyostelium homologue of TRAP-1, coupling with
RT differentiation of D. discoideum cells.";
RL Exp. Cell Res. 280:45-54(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15507488; DOI=10.1242/jcs.01499;
RA Morita T., Amagai A., Maeda Y.;
RT "Translocation of the Dictyostelium TRAP1 homologue to mitochondria induces
RT a novel prestarvation response.";
RL J. Cell Sci. 117:5759-5770(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15652354; DOI=10.1016/j.yexcr.2004.10.010;
RA Morita T., Yamaguchi H., Amagai A., Maeda Y.;
RT "Involvement of the TRAP-1 homologue, Dd-TRAP1, in spore differentiation
RT during Dictyostelium development.";
RL Exp. Cell Res. 303:425-431(2005).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15652353; DOI=10.1016/j.yexcr.2004.10.005;
RA Yamaguchi H., Morita T., Amagai A., Maeda Y.;
RT "Changes in spatial and temporal localization of Dictyostelium homologues
RT of TRAP1 and GRP94 revealed by immunoelectron microscopy.";
RL Exp. Cell Res. 303:415-424(2005).
CC -!- FUNCTION: Chaperone that expresses an ATPase activity.
CC {ECO:0000305|PubMed:12372338, ECO:0000305|PubMed:15652354}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton.
CC Mitochondrion. Spore, perispore. Nucleus, nucleolus. Note=Localizes to
CC the cortical actin cytoskeleton. Translocates to the mitochondrion
CC during the prestarvation response and in response to differentiation.
CC In prespore cells, colocalizes with grp94 in the prespore-specific
CC vacuole. Found in the outermost layer of spore cell wall.
CC -!- DISRUPTION PHENOTYPE: Defects in prestarvation response, sporulation
CC and in resistance to heat shock. When overexpressed, induces precocious
CC aggregation, however, development arrests before the tight mound stage.
CC {ECO:0000269|PubMed:15652354}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AB061695; BAC07474.1; -; mRNA.
DR EMBL; AAFI02000019; EAL68975.1; -; Genomic_DNA.
DR RefSeq; XP_642968.1; XM_637876.1.
DR AlphaFoldDB; Q86L04; -.
DR SMR; Q86L04; -.
DR STRING; 44689.DDB0185036; -.
DR PaxDb; Q86L04; -.
DR PRIDE; Q86L04; -.
DR EnsemblProtists; EAL68975; EAL68975; DDB_G0276947.
DR GeneID; 8620840; -.
DR KEGG; ddi:DDB_G0276947; -.
DR dictyBase; DDB_G0276947; trap1.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_3_1_1; -.
DR InParanoid; Q86L04; -.
DR OMA; YTRKVLI; -.
DR PhylomeDB; Q86L04; -.
DR PRO; PR:Q86L04; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:dictyBase.
DR GO; GO:0031160; C:spore wall; NAS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Mitochondrion;
KW Nucleotide-binding; Nucleus; Reference proteome; Stress response;
KW Transit peptide.
FT TRANSIT 1..62
FT /note="Mitochondrion"
FT CHAIN 63..711
FT /note="TNF receptor-associated protein 1 homolog,
FT mitochondrial"
FT /id="PRO_0000327691"
FT REGION 303..711
FT /note="Dimerization"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 184
FT /note="E -> V (in Ref. 1; BAC07474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 80179 MW; 6AE818347F799CD7 CRC64;
MQRTLSKVIL NSGKNNLLKS SNLLNSNLLK ATTTNIIGIK TINNNNNVNS IIGFKSLNKR
YFTSNTPKVE EEDDEIAPDE AIKAEEKIKE TERVIGLSEK LSFQTETQKI LHIVAESLYT
EKEVFIRELI SNASDAIEKV RHTQLTNASM IEDASIPFEI KISTDEDNKT LIIQDSGIGM
TKDEMIKNLG KIGYSGSSDF IKKLGENPDK ASIIGQFGVG FYSCFMVGHT IKIYTKSATP
GSKGYLWESD GTGSYSITEA EGVSRGTKII IHLKPSSYEY SKKSIVENII KKYSNFVGFP
IALNGTTVNT IKPLWTLNKN AISEEEHKEF YQFLSKSYDT PSYRVHFSTD TPLSIRSIFY
IPSQHMEKYG MGKMEPGVSL FSRKVLIQQK ANGILPEWMR FVRGVVDSED IPLNVSREHL
QDNGLIQRIS SVLVKRILKH LNDEAKSDPE KFNVFMTEFG GFFKEGIITD FKWKDEISKL
LRFESSNGST ASKTDAVSLE QYVSRMKPEQ KNIYFLSVPN RAVGLSSPYY EPFQLKDIEV
IFLYNAVDEF VLTNVGHFGD KKIVSVESKE AEEFLATNQD KKTETLSQDE IDKFLSWVST
VASDKVTQAK STTRSISSPA IIIDHESANF RRMLKMVEPG KQHETPKQVV EFNMNHPIIL
KLVQQTESNP TIAKLVIDQV VDNAFVSAGL IEDNREMIPR INQLLDSLLT K
