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TNF receptor-associated protein 1 homolog, mitochondrial (TNFR-associated protein 1 homolog) (Trap1 homolog)

 TRAP1_DICDI             Reviewed;         711 AA.
Q86L04; Q550G4; Q8MYB0;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
28-MAR-2018, entry version 110.
RecName: Full=TNF receptor-associated protein 1 homolog, mitochondrial;
Short=TNFR-associated protein 1 homolog;
Short=Trap1 homolog;
Flags: Precursor;
Name=trap1; ORFNames=DDB_G0276947;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Morita T., Saitoh K., Amagai A., Maeda Y.;
"Novel functions of a Dictyostelium TRAP1 homologue.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12372338; DOI=10.1006/excr.2002.5620;
Morita T., Amagai A., Maeda Y.;
"Unique behavior of a dictyostelium homologue of TRAP-1, coupling with
differentiation of D. discoideum cells.";
Exp. Cell Res. 280:45-54(2002).
[5]
SUBCELLULAR LOCATION.
PubMed=15507488; DOI=10.1242/jcs.01499;
Morita T., Amagai A., Maeda Y.;
"Translocation of the Dictyostelium TRAP1 homologue to mitochondria
induces a novel prestarvation response.";
J. Cell Sci. 117:5759-5770(2004).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15652354; DOI=10.1016/j.yexcr.2004.10.010;
Morita T., Yamaguchi H., Amagai A., Maeda Y.;
"Involvement of the TRAP-1 homologue, Dd-TRAP1, in spore
differentiation during Dictyostelium development.";
Exp. Cell Res. 303:425-431(2005).
[7]
SUBCELLULAR LOCATION.
PubMed=15652353; DOI=10.1016/j.yexcr.2004.10.005;
Yamaguchi H., Morita T., Amagai A., Maeda Y.;
"Changes in spatial and temporal localization of Dictyostelium
homologues of TRAP1 and GRP94 revealed by immunoelectron microscopy.";
Exp. Cell Res. 303:415-424(2005).
-!- FUNCTION: Chaperone that expresses an ATPase activity.
{ECO:0000305|PubMed:12372338, ECO:0000305|PubMed:15652354}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm,
cytoskeleton. Mitochondrion. Spore wall, perispore. Nucleus,
nucleolus. Note=Localizes to the cortical actin cytoskeleton.
Translocates to the mitochondrion during the prestarvation
response and in response to differentiation. In prespore cells,
colocalizes with grp94 in the prespore-specific vacuole. Found in
the outermost layer of spore cell wall.
-!- DISRUPTION PHENOTYPE: Defects in prestarvation response,
sporulation and in resistance to heat shock. When overexpressed,
induces precocious aggregation, however, development arrests
before the tight mound stage. {ECO:0000269|PubMed:15652354}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB061695; BAC07474.1; -; mRNA.
EMBL; AAFI02000019; EAL68975.1; -; Genomic_DNA.
RefSeq; XP_642968.1; XM_637876.1.
ProteinModelPortal; Q86L04; -.
SMR; Q86L04; -.
STRING; 44689.DDB0185036; -.
PaxDb; Q86L04; -.
PRIDE; Q86L04; -.
EnsemblProtists; EAL68975; EAL68975; DDB_G0276947.
GeneID; 8620840; -.
KEGG; ddi:DDB_G0276947; -.
dictyBase; DDB_G0276947; trap1.
eggNOG; KOG0019; Eukaryota.
eggNOG; COG0326; LUCA.
InParanoid; Q86L04; -.
KO; K09488; -.
OMA; ALYTRKV; -.
PhylomeDB; Q86L04; -.
PRO; PR:Q86L04; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:dictyBase.
GO; GO:0031160; C:spore wall; NAS:dictyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
GO; GO:0007275; P:multicellular organism development; IMP:dictyBase.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0006950; P:response to stress; IEA:InterPro.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
CDD; cd00075; HATPase_c; 1.
Gene3D; 1.20.120.790; -; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
2: Evidence at transcript level;
ATP-binding; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton;
Mitochondrion; Nucleotide-binding; Nucleus; Reference proteome;
Stress response; Transit peptide.
TRANSIT 1 62 Mitochondrion.
CHAIN 63 711 TNF receptor-associated protein 1
homolog, mitochondrial.
/FTId=PRO_0000327691.
REGION 303 711 Dimerization.
COMPBIAS 43 49 Poly-Asn.
BINDING 132 132 ATP. {ECO:0000250}.
BINDING 175 175 ATP. {ECO:0000250}.
BINDING 188 188 ATP. {ECO:0000250}.
BINDING 221 221 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 417 417 ATP. {ECO:0000250}.
CONFLICT 184 184 E -> V (in Ref. 1; BAC07474).
{ECO:0000305}.
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


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