ID HSP7R_ARATH Reviewed; 867 AA. AC F4JMJ1; O23509; Q0WM51; Q949M5; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Heat shock 70 kDa protein 17; DE AltName: Full=Heat shock protein 70-17; DE Short=AtHsp70-17; DE Flags: Precursor; GN Name=HSP70-17; OrderedLocusNames=At4g16660; GN ORFNames=dl4355w, FCAALL.64; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9461215; DOI=10.1038/35140; RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E., RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.; RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis RT thaliana."; RL Nature 391:485-488(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-867. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [6] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:gaoths>2.0.co;2; RA Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.; RT "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana."; RL Cell Stress Chaperones 6:201-208(2001). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE- CC ProRule:PRU10138}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family. CC HSP110/SSE subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB46039.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB78708.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z97341; CAB46039.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161544; CAB78708.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE83781.1; -; Genomic_DNA. DR EMBL; AY051008; AAK93685.1; -; mRNA. DR EMBL; AK229980; BAF01805.1; -; mRNA. DR PIR; E85185; E85185. DR PIR; G71433; G71433. DR RefSeq; NP_567510.1; NM_117767.4. DR AlphaFoldDB; F4JMJ1; -. DR SMR; F4JMJ1; -. DR BioGRID; 12660; 2. DR STRING; 3702.F4JMJ1; -. DR iPTMnet; F4JMJ1; -. DR PaxDb; 3702-AT4G16660-1; -. DR ProMEX; F4JMJ1; -. DR EnsemblPlants; AT4G16660.1; AT4G16660.1; AT4G16660. DR GeneID; 827367; -. DR Gramene; AT4G16660.1; AT4G16660.1; AT4G16660. DR KEGG; ath:AT4G16660; -. DR Araport; AT4G16660; -. DR TAIR; AT4G16660; HSP70. DR eggNOG; KOG0103; Eukaryota. DR eggNOG; KOG0104; Eukaryota. DR HOGENOM; CLU_005965_5_0_1; -. DR InParanoid; F4JMJ1; -. DR OMA; SRTPMIQ; -. DR PRO; PR:F4JMJ1; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; F4JMJ1; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR. DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR. DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0006950; P:response to stress; IEA:UniProt. DR CDD; cd10230; HYOU1-like_NBD; 1. DR Gene3D; 1.20.1270.10; -; 1. DR Gene3D; 3.30.30.30; -; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR018181; Heat_shock_70_CS. DR InterPro; IPR029048; HSP70_C_sf. DR InterPro; IPR029047; HSP70_peptide-bd_sf. DR InterPro; IPR013126; Hsp_70_fam. DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1. DR PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS01036; HSP70_3; 1. DR Genevisible; F4JMJ1; AT. PE 2: Evidence at transcript level; KW ATP-binding; Chaperone; Endoplasmic reticulum; Nucleotide-binding; KW Reference proteome; Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..867 FT /note="Heat shock 70 kDa protein 17" FT /id="PRO_0000415435" FT REGION 560..607 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 829..867 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 865..867 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT COMPBIAS 560..575 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..602 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 413 FT /note="L -> I (in Ref. 5; BAF01805)" FT /evidence="ECO:0000305" FT CONFLICT 741 FT /note="R -> Q (in Ref. 4; AAK93685)" FT /evidence="ECO:0000305" SQ SEQUENCE 867 AA; 96725 MW; B62D427C39CAB87A CRC64; MGKIFSWLVV LLSLISLVPV PSESAVLSVD LGSEWVKVAV VNLKRGQSPI SVAINEMSKR KSPALVAFQS GDRLLGEEAA GITARYPNKV YSQLRDMVGK PFKHVKDFID SVYLPFDIVE DSRGAVGIKI DDGSTVYSVE ELLAMILGYA SNLAEFHAKI PVKDMVVSVP PYFGQAERRG LIQASQLAGV NVLSLVNEHS GAALQYGIDK DFANGSRHVI FYDMGSSSTY AALVYYSAYS EKEYGKTVSV NQFQVKDVRW DLGLGGQSME MRLVEHFADE FNKQLGNGVD VRKFPKAMAK LKKQVKRTKE ILSANTAAPI SVESLHDDRD FRSTITREKF EELCKDLWER SLTPLKDVLK HSGLKIDDIS AVELIGGATR VPKLQSTIQE FIGKQQLDKH LDADEAIVLG SALHAANLSD GIKLKRRLGI VDGSPYGFLV ELEGPNVKKD ESTKQQLVPR MKKLPSKMFR SFVLDKDFDV SLAYESEGIL PPGTTSPVFA QYSVSGLADA SEKYSSRNLS APIKANLHFS LSRSGILSLD RGDAVIEITE WVDVPKKNVT IDSNTTTSTG NATDENSQEN KEDLQTDAEN STASNTTAEE PAVASLGTEK KLKKRTFRIP LKVVEKTVGP GAPFSKESLA EAKIKLEALD KKDRERRRTA ELKNNLESYI YATKEKLETP EFEKISTQEE RKAFVEKLDE VQDWLYMDGE DANATEFEKR LDSLKAIGSP ISFRSEELTA RPVAIEYARK YLTELKEIIK EWETNKTWLP KEKIDEVSKE AEKVKSWLDK NVAEQEKTSL WSKPVFTSTE VYAKVFTLQD KVTKVNKIPK PKPKIEKVTK TENTTKEEEQ SKSSDEAAKE EESHDEL //