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F4JMJ1

- HSP7R_ARATH

UniProt

F4JMJ1 - HSP7R_ARATH

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Protein

Heat shock 70 kDa protein 17

Gene

HSP70-17

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_187630. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 17
Alternative name(s):
Heat shock protein 70-17
Short name:
AtHsp70-17
Gene namesi
Name:HSP70-17
Ordered Locus Names:At4g16660
ORF Names:dl4355w, FCAALL.64
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G16660.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. endoplasmic reticulum Source: TAIR
  3. Golgi apparatus Source: TAIR
  4. vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 867843Heat shock 70 kDa protein 17PRO_0000415435Add
BLAST

Proteomic databases

PRIDEiF4JMJ1.
ProMEXiF4JMJ1.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G16660.1-P.

Structurei

3D structure databases

ProteinModelPortaliF4JMJ1.
SMRiF4JMJ1. Positions 22-734.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi865 – 8673Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
HOGENOMiHOG000239402.
InParanoidiF4JMJ1.
KOiK09486.
OMAiHFADEFN.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

F4JMJ1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKIFSWLVV LLSLISLVPV PSESAVLSVD LGSEWVKVAV VNLKRGQSPI
60 70 80 90 100
SVAINEMSKR KSPALVAFQS GDRLLGEEAA GITARYPNKV YSQLRDMVGK
110 120 130 140 150
PFKHVKDFID SVYLPFDIVE DSRGAVGIKI DDGSTVYSVE ELLAMILGYA
160 170 180 190 200
SNLAEFHAKI PVKDMVVSVP PYFGQAERRG LIQASQLAGV NVLSLVNEHS
210 220 230 240 250
GAALQYGIDK DFANGSRHVI FYDMGSSSTY AALVYYSAYS EKEYGKTVSV
260 270 280 290 300
NQFQVKDVRW DLGLGGQSME MRLVEHFADE FNKQLGNGVD VRKFPKAMAK
310 320 330 340 350
LKKQVKRTKE ILSANTAAPI SVESLHDDRD FRSTITREKF EELCKDLWER
360 370 380 390 400
SLTPLKDVLK HSGLKIDDIS AVELIGGATR VPKLQSTIQE FIGKQQLDKH
410 420 430 440 450
LDADEAIVLG SALHAANLSD GIKLKRRLGI VDGSPYGFLV ELEGPNVKKD
460 470 480 490 500
ESTKQQLVPR MKKLPSKMFR SFVLDKDFDV SLAYESEGIL PPGTTSPVFA
510 520 530 540 550
QYSVSGLADA SEKYSSRNLS APIKANLHFS LSRSGILSLD RGDAVIEITE
560 570 580 590 600
WVDVPKKNVT IDSNTTTSTG NATDENSQEN KEDLQTDAEN STASNTTAEE
610 620 630 640 650
PAVASLGTEK KLKKRTFRIP LKVVEKTVGP GAPFSKESLA EAKIKLEALD
660 670 680 690 700
KKDRERRRTA ELKNNLESYI YATKEKLETP EFEKISTQEE RKAFVEKLDE
710 720 730 740 750
VQDWLYMDGE DANATEFEKR LDSLKAIGSP ISFRSEELTA RPVAIEYARK
760 770 780 790 800
YLTELKEIIK EWETNKTWLP KEKIDEVSKE AEKVKSWLDK NVAEQEKTSL
810 820 830 840 850
WSKPVFTSTE VYAKVFTLQD KVTKVNKIPK PKPKIEKVTK TENTTKEEEQ
860
SKSSDEAAKE EESHDEL
Length:867
Mass (Da):96,725
Last modified:June 28, 2011 - v1
Checksum:iB62D427C39CAB87A
GO

Sequence cautioni

The sequence CAB46039.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78708.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti413 – 4131L → I in BAF01805. 1 PublicationCurated
Sequence conflicti741 – 7411R → Q in AAK93685. (PubMed:14593172)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97341 Genomic DNA. Translation: CAB46039.1. Sequence problems.
AL161544 Genomic DNA. Translation: CAB78708.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83781.1.
AY051008 mRNA. Translation: AAK93685.1.
AK229980 mRNA. Translation: BAF01805.1.
PIRiE85185.
G71433.
RefSeqiNP_567510.1. NM_117767.3.
UniGeneiAt.22039.

Genome annotation databases

EnsemblPlantsiAT4G16660.1; AT4G16660.1; AT4G16660.
GeneIDi827367.
KEGGiath:AT4G16660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97341 Genomic DNA. Translation: CAB46039.1 . Sequence problems.
AL161544 Genomic DNA. Translation: CAB78708.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE83781.1 .
AY051008 mRNA. Translation: AAK93685.1 .
AK229980 mRNA. Translation: BAF01805.1 .
PIRi E85185.
G71433.
RefSeqi NP_567510.1. NM_117767.3.
UniGenei At.22039.

3D structure databases

ProteinModelPortali F4JMJ1.
SMRi F4JMJ1. Positions 22-734.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT4G16660.1-P.

Proteomic databases

PRIDEi F4JMJ1.
ProMEXi F4JMJ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G16660.1 ; AT4G16660.1 ; AT4G16660 .
GeneIDi 827367.
KEGGi ath:AT4G16660.

Organism-specific databases

TAIRi AT4G16660.

Phylogenomic databases

eggNOGi COG0443.
HOGENOMi HOG000239402.
InParanoidi F4JMJ1.
KOi K09486.
OMAi HFADEFN.

Enzyme and pathway databases

Reactomei REACT_187630. XBP1(S) activates chaperone genes.

Miscellaneous databases

PROi F4JMJ1.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100934. SSF100934. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-867.
    Strain: cv. Columbia.
  6. "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana."
    Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.
    Cell Stress Chaperones 6:201-208(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiHSP7R_ARATH
AccessioniPrimary (citable) accession number: F4JMJ1
Secondary accession number(s): O23509, Q0WM51, Q949M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: June 28, 2011
Last modified: November 26, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3