ID HSP7C_MOUSE Reviewed; 646 AA. AC P63017; P08109; P12225; Q3U6R0; Q3U764; Q3U7D7; Q3U7E2; Q3U9B4; Q3U9G0; AC Q3UGM0; Q5FWJ6; Q62373; Q62374; Q62375; Q6NZD0; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=Heat shock cognate 71 kDa protein {ECO:0000305}; DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11142}; DE AltName: Full=Heat shock 70 kDa protein 8; GN Name=Hspa8 {ECO:0000312|MGI:MGI:105384}; GN Synonyms=Hsc70 {ECO:0000303|PubMed:10095055}, Hsc73 GN {ECO:0000303|PubMed:8682318}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3334718; DOI=10.1016/0012-1606(88)90073-5; RA Giebel L.B., Dworniczak B.P., Bautz E.K.F.; RT "Developmental regulation of a constitutively expressed mouse mRNA encoding RT a 72-kDa heat shock-like protein."; RL Dev. Biol. 125:200-207(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129; TISSUE=Mammary gland; RX PubMed=8682318; DOI=10.1016/0378-1119(96)00169-2; RA Soulier S., Vilotte J.-L., L'Huillier P.J., Mercier J.-C.; RT "Developmental regulation of murine integrin beta 1 subunit- and Hsc73- RT encoding genes in mammary gland: sequence of a new mouse Hsc73 cDNA."; RL Gene 172:285-289(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129; RX PubMed=10095055; DOI=10.1016/s0167-4781(98)00285-1; RA Hunt C.R., Parsian A.J., Goswami P.C., Kozak C.A.; RT "Characterization and expression of the mouse Hsc70 gene."; RL Biochim. Biophys. Acta 1444:315-325(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and DBA/2J; RC TISSUE=Amnion, Bone marrow, Heart, Kidney, Liver, Stomach, Thymus, and RC Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; RC TISSUE=Brain, Embryo, Embryonic germ cell, Eye, and Mammary gland; 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 [6] RP PROTEIN SEQUENCE OF 4-49; 57-71; 77-102; 113-155; 160-188; 221-246; RP 300-319; 326-342; 349-357; 362-384; 424-447; 540-550 AND 584-597, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-383; 438-452 AND 580-587. RX PubMed=2251119; DOI=10.1093/nar/18.22.6565; RA Liu J., Maxwell E.S.; RT "Mouse U14 snRNA is encoded in an intron of the mouse cognate hsc70 heat RT shock gene."; RL Nucleic Acids Res. 18:6565-6571(1990). RN [8] RP INTERACTION WITH HSPH1. RX PubMed=9675148; DOI=10.1006/bbrc.1998.8979; RA Hatayama T., Yasuda K., Yasuda K.; RT "Association of HSP105 with HSC70 in high molecular mass complexes in mouse RT FM3A cells."; RL Biochem. Biophys. Res. Commun. 248:395-401(1998). RN [9] RP INTERACTION WITH HSPH1. RX PubMed=15292236; DOI=10.1074/jbc.m407947200; RA Yamagishi N., Ishihara K., Hatayama T.; RT "Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase RT activity."; RL J. Biol. Chem. 279:41727-41733(2004). RN [10] RP ISGYLATION. RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132; RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.; RT "Proteomic identification of proteins conjugated to ISG15 in mouse and RT human cells."; RL Biochem. Biophys. Res. Commun. 336:496-506(2005). RN [11] RP INTERACTION WITH IRAK1BP1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17233114; DOI=10.1089/dna.2006.25.704; RA Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.; RT "The disordered amino-terminus of SIMPL interacts with members of the 70- RT kDa heat-shock protein family."; RL DNA Cell Biol. 25:704-714(2006). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [13] RP INTERACTION WITH GIMAP5; BCL2L1 AND MCL1. RX PubMed=21502331; DOI=10.1084/jem.20101192; RA Chen Y., Yu M., Dai X., Zogg M., Wen R., Weiler H., Wang D.; RT "Critical role for Gimap5 in the survival of mouse hematopoietic stem and RT progenitor cells."; RL J. Exp. Med. 208:923-935(2011). RN [14] RP METHYLATION AT LYS-561. RX PubMed=23921388; DOI=10.1074/jbc.m113.483248; RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., RA Melki R., Falnes P.O.; RT "Identification and characterization of a novel human methyltransferase RT modulating Hsp70 function through lysine methylation."; RL J. Biol. Chem. 288:27752-27763(2013). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246; LYS-319; LYS-328; RP LYS-512; LYS-524 AND LYS-601, SUCCINYLATION [LARGE SCALE ANALYSIS] AT RP LYS-319 AND LYS-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [16] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-469, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Molecular chaperone implicated in a wide variety of cellular CC processes, including protection of the proteome from stress, folding CC and transport of newly synthesized polypeptides, chaperone-mediated CC autophagy, activation of proteolysis of misfolded proteins, formation CC and dissociation of protein complexes, and antigen presentation. Plays CC a pivotal role in the protein quality control system, ensuring the CC correct folding of proteins, the re-folding of misfolded proteins and CC controlling the targeting of proteins for subsequent degradation. This CC is achieved through cycles of ATP binding, ATP hydrolysis and ADP CC release, mediated by co-chaperones. The co-chaperones have been shown CC to not only regulate different steps of the ATPase cycle of HSP70, but CC they also have an individual specificity such that one co-chaperone may CC promote folding of a substrate while another may promote degradation. CC The affinity of HSP70 for polypeptides is regulated by its nucleotide CC bound state. In the ATP-bound form, it has a low affinity for substrate CC proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a CC conformational change that increases its affinity for substrate CC proteins. HSP70 goes through repeated cycles of ATP hydrolysis and CC nucleotide exchange, which permits cycles of substrate binding and CC release. The HSP70-associated co-chaperones are of three types: J- CC domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the CC nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate CC conversion of HSP70 from the ADP-bound to the ATP-bound state thereby CC promoting substrate release), and the TPR domain chaperones such as CC HOPX and STUB1. Plays a critical role in mitochondrial import, delivers CC preproteins to the mitochondrial import receptor TOMM70. Acts as a CC repressor of transcriptional activation. Inhibits the transcriptional CC coactivator activity of CITED1 on Smad-mediated transcription. CC Component of the PRP19-CDC5L complex that forms an integral part of the CC spliceosome and is required for activating pre-mRNA splicing. May have CC a scaffolding role in the spliceosome assembly as it contacts all other CC components of the core complex. Binds bacterial lipopolysaccharide CC (LPS) and mediates LPS-induced inflammatory response, including TNF CC secretion by monocytes. Substrate recognition component in chaperone- CC mediated autophagy (CMA), a selective protein degradation process that CC mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 CC specifically recognizes and binds cytosolic proteins bearing a -KFERQ CC motif and promotes their recruitment to the surface of the lysosome CC where they bind to lysosomal protein LAMP2. KFERQ motif-containing CC proteins are eventually transported into the lysosomal lumen where they CC are degraded. In conjunction with LAMP2, facilitates MHC class II CC presentation of cytoplasmic antigens by guiding antigens to the CC lysosomal membrane for interaction with LAMP2 which then elicits MHC CC class II presentation of peptides to the cell membrane. Participates in CC the ER-associated degradation (ERAD) quality control pathway in CC conjunction with J domain-containing co-chaperones and the E3 ligase CC STUB1. It is recruited to clathrin-coated vesicles through its CC interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase CC activity and therefore uncoating of clathrin-coated vesicles (By CC similarity). {ECO:0000250|UniProtKB:P11142, CC ECO:0000250|UniProtKB:P19120}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; CC Evidence={ECO:0000250|UniProtKB:P11142}; CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex CC containing untranslated mRNAs (By similarity). Interacts with PACRG (By CC similarity). Interacts with DNAJC7 (By similarity). Interacts with CC DNAJB12 (via J domain) (By similarity). Interacts with DNAJB14 (via J CC domain) (By similarity). Interacts (via C-terminus) with the E3 ligase CC STUB1 forming a 210 kDa complex of one STUB1 and two HSPA8 molecules CC (By similarity). Interacts with CITED1 (via N-terminus); the CC interaction suppresses the association of CITED1 to p300/CBP and Smad- CC mediated transcription transactivation (By similarity). Component of CC the PRP19-CDC5L splicing complex composed of a core complex comprising CC a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three CC less stably associated proteins CTNNBL1, CWC15 and HSPA8 (By CC similarity). Interacts with IRAK1BP1 and HSPH1/HSP105 (PubMed:9675148, CC PubMed:15292236, PubMed:17233114). Interacts with TRIM5 (By CC similarity). Part of a complex composed at least of ASH2L, EMSY, HCFC1, CC HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this CC complex may have a histone H3-specific methyltransferase activity (By CC similarity). Following LPS binding, may form a complex with CXCR4, GDF5 CC and HSP90AA1 (By similarity). Interacts with PRKN (By similarity). CC Interacts with FOXP3 (By similarity). Interacts with DNAJC9 (via J CC domain) (By similarity). Interacts with MLLT11 (By similarity). CC Interacts with RNF207 (By similarity). Interacts with DNAJC21 (By CC similarity). Interacts with DNAJB2 (By similarity). Interacts with TTC1 CC (via TPR repeats) (By similarity). Interacts with SGTA (via TPR CC repeats) (By similarity). Interacts with HSF1 (via transactivation CC domain) (By similarity). Interacts with HOPX, STUB1, HSP40, HSP90, BAG2 CC and BAG3 (By similarity). Interacts with DNAJC12 (By similarity). CC Interacts with HSPC138 (By similarity). Interacts with ZMYND10 (By CC similarity). Interacts with VGF-derived peptide TLQP-21 (By CC similarity). Interacts with BCL2L1, GIMAP5 and MCL1; the interaction CC with BCL2L1 or MCL1 is impaired in the absence of GIMAP5 CC (PubMed:21502331). Interacts with NLPR12 (By similarity). Interacts CC with TTC4 (By similarity). Interacts with TOMM70; the interaction is CC required for preprotein mitochondrial import (By similarity). May CC interact with DNJC9; the interaction seems to be histone-dependent (By CC similarity). Interacts with BAG5 and JPH2; the interaction with JPH2 is CC increased in the presence of BAG5 (By similarity). Interacts with VGF- CC derived peptide TLQP-21 (By similarity). Interacts with DNAJC6 (via J CC domain) in an ATP-dependent manner; this interaction stimulates the CC HSPA8's ATPase activity. Forms a complex composed of HSPA8, CLTC and CC DNAJC6 (By similarity). {ECO:0000250|UniProtKB:P11142, CC ECO:0000250|UniProtKB:P19120, ECO:0000250|UniProtKB:P63018, CC ECO:0000269|PubMed:15292236, ECO:0000269|PubMed:17233114, CC ECO:0000269|PubMed:21502331, ECO:0000269|PubMed:9675148}. CC -!- INTERACTION: CC P63017; O88447: Klc1; NbExp=3; IntAct=EBI-433443, EBI-301550; CC P63017; P43883: Plin2; NbExp=3; IntAct=EBI-433443, EBI-16156700; CC P63017; Q9DBG5: Plin3; NbExp=2; IntAct=EBI-433443, EBI-643495; CC P63017; O41974: GAMMAHV.ORF73; Xeno; NbExp=3; IntAct=EBI-433443, EBI-6933128; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11142}. CC Melanosome {ECO:0000250|UniProtKB:P11142}. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P11142}. Cell membrane CC {ECO:0000250|UniProtKB:P11142}. Lysosome membrane CC {ECO:0000250|UniProtKB:P11142}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P11142}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P11142}. Note=Localized in cytoplasmic mRNP CC granules containing untranslated mRNAs. Translocates rapidly from the CC cytoplasm to the nuclei, and especially to the nucleoli, upon heat CC shock. {ECO:0000250|UniProtKB:P11142}. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- INDUCTION: Constitutively synthesized. CC -!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as CC the ATPase domain) is responsible for binding and hydrolyzing ATP. The CC C-terminal substrate-binding domain (SBD) (also known as peptide- CC binding domain) binds to the client/substrate proteins. The two domains CC are allosterically coupled so that, when ATP is bound to the NBD, the CC SBD binds relatively weakly to clients. When ADP is bound in the NBD, a CC conformational change enhances the affinity of the SBD for client CC proteins. {ECO:0000250|UniProtKB:P11142}. CC -!- PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}. CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}. CC -!- PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding. CC {ECO:0000250|UniProtKB:P11142}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE31508.1; Type=Frameshift; 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; M19141; AAA37869.1; -; mRNA. DR EMBL; U27129; AAC52836.1; -; mRNA. DR EMBL; U73744; AAB18391.1; -; Genomic_DNA. DR EMBL; AK035286; BAC29016.1; -; mRNA. DR EMBL; AK075935; BAC36065.1; -; mRNA. DR EMBL; AK145579; BAE26523.1; -; mRNA. DR EMBL; AK146708; BAE27374.1; -; mRNA. DR EMBL; AK146985; BAE27588.1; -; mRNA. DR EMBL; AK147864; BAE28187.1; -; mRNA. DR EMBL; AK150474; BAE29591.1; -; mRNA. DR EMBL; AK150498; BAE29612.1; -; mRNA. DR EMBL; AK150701; BAE29780.1; -; mRNA. DR EMBL; AK150958; BAE29990.1; -; mRNA. DR EMBL; AK151065; BAE30081.1; -; mRNA. DR EMBL; AK151127; BAE30135.1; -; mRNA. DR EMBL; AK151287; BAE30272.1; -; mRNA. DR EMBL; AK151435; BAE30398.1; -; mRNA. DR EMBL; AK151516; BAE30465.1; -; mRNA. DR EMBL; AK151537; BAE30484.1; -; mRNA. DR EMBL; AK151775; BAE30681.1; -; mRNA. DR EMBL; AK151808; BAE30707.1; -; mRNA. DR EMBL; AK151865; BAE30753.1; -; mRNA. DR EMBL; AK151892; BAE30776.1; -; mRNA. DR EMBL; AK151948; BAE30822.1; -; mRNA. DR EMBL; AK151997; BAE30861.1; -; mRNA. DR EMBL; AK152598; BAE31346.1; -; mRNA. DR EMBL; AK152697; BAE31427.1; -; mRNA. DR EMBL; AK152703; BAE31432.1; -; mRNA. DR EMBL; AK152803; BAE31508.1; ALT_FRAME; mRNA. DR EMBL; AK153032; BAE31664.1; -; mRNA. DR EMBL; AK153834; BAE32204.1; -; mRNA. DR EMBL; AK159479; BAE35116.1; -; mRNA. DR EMBL; AK164000; BAE37581.1; -; mRNA. DR EMBL; AK166643; BAE38912.1; -; mRNA. DR EMBL; AK166721; BAE38970.1; -; mRNA. DR EMBL; AK166767; BAE39005.1; -; mRNA. DR EMBL; AK166776; BAE39012.1; -; mRNA. DR EMBL; AK166808; BAE39036.1; -; mRNA. DR EMBL; AK166830; BAE39053.1; -; mRNA. DR EMBL; AK166846; BAE39065.1; -; mRNA. DR EMBL; AK166861; BAE39076.1; -; mRNA. DR EMBL; AK166873; BAE39084.1; -; mRNA. DR EMBL; AK166908; BAE39109.1; -; mRNA. DR EMBL; AK166910; BAE39111.1; -; mRNA. DR EMBL; AK166913; BAE39113.1; -; mRNA. DR EMBL; AK166933; BAE39127.1; -; mRNA. DR EMBL; AK167043; BAE39211.1; -; mRNA. DR EMBL; AK167121; BAE39269.1; -; mRNA. DR EMBL; AK167122; BAE39270.1; -; mRNA. DR EMBL; AK167134; BAE39280.1; -; mRNA. DR EMBL; AK167163; BAE39304.1; -; mRNA. DR EMBL; AK167218; BAE39344.1; -; mRNA. DR EMBL; AK167229; BAE39353.1; -; mRNA. DR EMBL; AK167845; BAE39865.1; -; mRNA. DR EMBL; AK167910; BAE39917.1; -; mRNA. DR EMBL; AK168492; BAE40379.1; -; mRNA. DR EMBL; AK168519; BAE40398.1; -; mRNA. DR EMBL; AK168542; BAE40419.1; -; mRNA. DR EMBL; AK168711; BAE40553.1; -; mRNA. DR EMBL; AK168750; BAE40590.1; -; mRNA. DR EMBL; AK168776; BAE40612.1; -; mRNA. DR EMBL; AK168887; BAE40704.1; -; mRNA. DR EMBL; AK168934; BAE40745.1; -; mRNA. DR EMBL; AK169093; BAE40876.1; -; mRNA. DR EMBL; AK169179; BAE40957.1; -; mRNA. DR EMBL; AK169236; BAE41004.1; -; mRNA. DR EMBL; AK169293; BAE41049.1; -; mRNA. DR EMBL; BC006722; AAH06722.1; -; mRNA. DR EMBL; BC066191; AAH66191.1; -; mRNA. DR EMBL; BC085486; AAH85486.1; -; mRNA. DR EMBL; BC089322; AAH89322.1; -; mRNA. DR EMBL; BC089457; AAH89457.1; -; mRNA. DR EMBL; BC106193; AAI06194.1; -; mRNA. DR EMBL; X54401; CAA38267.1; -; Genomic_DNA. DR EMBL; X54402; CAA38268.1; -; Genomic_DNA. DR EMBL; X54403; CAA38269.1; -; Genomic_DNA. DR CCDS; CCDS23083.1; -. DR PIR; A45935; A45935. DR PIR; JC4853; JC4853. DR RefSeq; NP_112442.2; NM_031165.4. DR PDB; 3CQX; X-ray; 2.30 A; A/B=1-381. DR PDBsum; 3CQX; -. DR AlphaFoldDB; P63017; -. DR SMR; P63017; -. DR BioGRID; 200428; 176. DR ComplexPortal; CPX-5825; PRP19-CDC5L complex. DR CORUM; P63017; -. DR DIP; DIP-32353N; -. DR IntAct; P63017; 50. DR MINT; P63017; -. DR STRING; 10090.ENSMUSP00000015800; -. DR ChEMBL; CHEMBL5169139; -. DR CarbonylDB; P63017; -. DR GlyGen; P63017; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P63017; -. DR MetOSite; P63017; -. DR PhosphoSitePlus; P63017; -. DR SwissPalm; P63017; -. DR REPRODUCTION-2DPAGE; IPI00323357; -. DR REPRODUCTION-2DPAGE; P63017; -. DR REPRODUCTION-2DPAGE; Q6NZD0; -. DR CPTAC; non-CPTAC-3713; -. DR EPD; P63017; -. DR jPOST; P63017; -. DR MaxQB; P63017; -. DR PaxDb; 10090-ENSMUSP00000015800; -. DR PeptideAtlas; P63017; -. DR ProteomicsDB; 273196; -. DR Pumba; P63017; -. DR Antibodypedia; 3675; 1343 antibodies from 44 providers. DR DNASU; 15481; -. DR Ensembl; ENSMUST00000015800.16; ENSMUSP00000015800.10; ENSMUSG00000015656.18. DR GeneID; 15481; -. DR KEGG; mmu:15481; -. DR UCSC; uc009ozx.3; mouse. DR AGR; MGI:105384; -. DR CTD; 3312; -. DR MGI; MGI:105384; Hspa8. DR VEuPathDB; HostDB:ENSMUSG00000015656; -. DR eggNOG; KOG0101; Eukaryota. DR GeneTree; ENSGT00950000183206; -. DR HOGENOM; CLU_005965_3_0_1; -. DR InParanoid; P63017; -. DR OMA; KANPIMM; -. DR OrthoDB; 143at2759; -. DR PhylomeDB; P63017; -. DR TreeFam; TF105042; -. DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-MMU-3371568; Attenuation phase. DR Reactome; R-MMU-3371571; HSF1-dependent transactivation. DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR Reactome; R-MMU-8876725; Protein methylation. DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation. DR Reactome; R-MMU-9833482; PKR-mediated signaling. DR BioGRID-ORCS; 15481; 32 hits in 78 CRISPR screens. DR ChiTaRS; Hspa8; mouse. DR EvolutionaryTrace; P63017; -. DR PRO; PR:P63017; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; P63017; Protein. DR Bgee; ENSMUSG00000015656; Expressed in embryonic post-anal tail and 124 other cell types or tissues. DR ExpressionAtlas; P63017; baseline and differential. DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI. DR GO; GO:0005776; C:autophagosome; ISO:MGI. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:AgBase. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0043198; C:dendritic shaft; ISO:MGI. DR GO; GO:0043197; C:dendritic spine; ISO:MGI. DR GO; GO:0070062; C:extracellular exosome; IDA:MGI. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO. DR GO; GO:0005882; C:intermediate filament; ISO:MGI. DR GO; GO:0005770; C:late endosome; IDA:ParkinsonsUK-UCL. DR GO; GO:0031906; C:late endosome lumen; TAS:Reactome. DR GO; GO:1990836; C:lysosomal matrix; ISO:MGI. DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB. DR GO; GO:0005764; C:lysosome; IBA:GO_Central. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:MGI. DR GO; GO:0005874; C:microtubule; ISO:MGI. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0044309; C:neuron spine; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI. DR GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI. DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0098794; C:postsynapse; ISO:MGI. DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; ISO:MGI. DR GO; GO:0099634; C:postsynaptic specialization membrane; IDA:SynGO. DR GO; GO:0098793; C:presynapse; IDA:SynGO. DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI. DR GO; GO:0101031; C:protein folding chaperone complex; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI. DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI. DR GO; GO:0043195; C:terminal bouton; ISO:MGI. DR GO; GO:0031686; F:A1 adenosine receptor binding; ISO:MGI. DR GO; GO:0043531; F:ADP binding; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI. DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; ISO:MGI. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:MGI. DR GO; GO:1990833; F:clathrin-uncoating ATPase activity; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI. DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI. DR GO; GO:0042277; F:peptide binding; ISO:MGI. DR GO; GO:0001786; F:phosphatidylserine binding; IDA:ParkinsonsUK-UCL. DR GO; GO:1904593; F:prostaglandin binding; ISO:MGI. DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central. DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; ISO:MGI. DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0051082; F:unfolded protein binding; IPI:MGI. DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI. DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl. DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IGI:MGI. DR GO; GO:0061684; P:chaperone-mediated autophagy; ISS:ParkinsonsUK-UCL. DR GO; GO:1904764; P:chaperone-mediated autophagy translocation complex disassembly; ISS:ParkinsonsUK-UCL. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:SynGO. DR GO; GO:0072318; P:clathrin coat disassembly; IDA:UniProtKB. DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl. DR GO; GO:0030900; P:forebrain development; IEA:Ensembl. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0061738; P:late endosomal microautophagy; IMP:ParkinsonsUK-UCL. DR GO; GO:0098880; P:maintenance of postsynaptic specialization structure; IEA:Ensembl. DR GO; GO:0044788; P:modulation by host of viral process; IMP:AgBase. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:ComplexPortal. DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; ISO:MGI. DR GO; GO:1902904; P:negative regulation of supramolecular fiber organization; ISO:MGI. DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase. DR GO; GO:0097214; P:positive regulation of lysosomal membrane permeability; IEA:Ensembl. DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI. DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl. DR GO; GO:1904592; P:positive regulation of protein refolding; IEA:Ensembl. DR GO; GO:0045862; P:positive regulation of proteolysis; IEA:Ensembl. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl. DR GO; GO:0006457; P:protein folding; IDA:MGI. DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl. DR GO; GO:0042026; P:protein refolding; ISS:ParkinsonsUK-UCL. DR GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; ISS:UniProtKB. DR GO; GO:0044743; P:protein transmembrane import into intracellular organelle; IEA:Ensembl. DR GO; GO:0032984; P:protein-containing complex disassembly; ISO:MGI. DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI. DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO. DR GO; GO:0061635; P:regulation of protein complex stability; ISS:ParkinsonsUK-UCL. DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0010045; P:response to nickel cation; IEA:Ensembl. DR GO; GO:1990834; P:response to odorant; IEA:Ensembl. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0042594; P:response to starvation; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl. DR GO; GO:1990832; P:slow axonal transport; IBA:GO_Central. DR GO; GO:0016191; P:synaptic vesicle uncoating; IEA:Ensembl. DR CDD; cd10233; HSPA1-2_6-8-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; PTHR19375:SF379; HEAT SHOCK COGNATE 71 KDA PROTEIN; 1. DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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 SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. DR COMPLUYEAST-2DPAGE; P63017; -. DR SWISS-2DPAGE; P63017; -. DR UCD-2DPAGE; P63017; -. DR Genevisible; P63017; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Autophagy; Cell membrane; KW Chaperone; Cytoplasm; Direct protein sequencing; Hydrolase; KW Isopeptide bond; Lysosome; Membrane; Methylation; mRNA processing; KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; Spliceosome; Stress response; Transcription; KW Transcription regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P11142" FT CHAIN 2..646 FT /note="Heat shock cognate 71 kDa protein" FT /id="PRO_0000078271" FT REGION 2..386 FT /note="Nucleotide-binding domain (NBD)" FT /evidence="ECO:0000250|UniProtKB:P11142" FT REGION 186..377 FT /note="Interaction with BAG1" FT /evidence="ECO:0000250" FT REGION 394..509 FT /note="Substrate-binding domain (SBD)" FT /evidence="ECO:0000250|UniProtKB:P11142" FT REGION 614..646 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 12..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 14 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P19120" FT BINDING 15 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P19120" FT BINDING 71 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 202..204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 202 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P19120" FT BINDING 268..275 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 268 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P19120" FT BINDING 271 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P19120" FT BINDING 275 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P19120" FT BINDING 339..342 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 339 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P19120" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P11142" FT MOD_RES 108 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11142" FT MOD_RES 246 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 319 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 319 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 328 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 329 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11142" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11142" FT MOD_RES 469 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 512 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 512 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 524 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 541 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11142" FT MOD_RES 561 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:23921388" FT MOD_RES 561 FT /note="N6,N6,N6-trimethyllysine; by METTL21A; alternate" FT /evidence="ECO:0000250" FT MOD_RES 561 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11142" FT MOD_RES 589 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11142" FT MOD_RES 597 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11142" FT MOD_RES 601 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT CROSSLNK 512 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P11142" FT CROSSLNK 512 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P11142" FT CONFLICT 9 FT /note="I -> V (in Ref. 4; BAE28187)" FT /evidence="ECO:0000305" FT CONFLICT 35 FT /note="N -> K (in Ref. 4; BAE30081/BAE30861/BAE30753)" FT /evidence="ECO:0000305" FT CONFLICT 268 FT /note="E -> G (in Ref. 4; BAE31432/BAE31346)" FT /evidence="ECO:0000305" FT CONFLICT 269 FT /note="R -> G (in Ref. 4; BAE31508)" FT /evidence="ECO:0000305" FT CONFLICT 353 FT /note="F -> C (in Ref. 4; BAE31664)" FT /evidence="ECO:0000305" FT CONFLICT 428 FT /note="F -> L (in Ref. 1; AAA37869 and 3; AAB18391)" FT /evidence="ECO:0000305" FT CONFLICT 432 FT /note="S -> Y (in Ref. 4; BAE30707)" FT /evidence="ECO:0000305" FT CONFLICT 589 FT /note="K -> E (in Ref. 5; AAH66191)" FT /evidence="ECO:0000305" FT CONFLICT 645 FT /note="V -> M (in Ref. 4; BAE30272/BAE31427)" FT /evidence="ECO:0000305" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 13..22 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 53..57 FT /evidence="ECO:0007829|PDB:3CQX" FT TURN 58..61 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:3CQX" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 81..86 FT /evidence="ECO:0007829|PDB:3CQX" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 91..97 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 100..107 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 116..135 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 152..164 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 175..182 FT /evidence="ECO:0007829|PDB:3CQX" FT TURN 183..186 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 187..200 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 205..213 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 216..225 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 230..249 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 257..273 FT /evidence="ECO:0007829|PDB:3CQX" FT TURN 274..276 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 278..288 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 291..298 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 299..312 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 314..324 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:3CQX" FT STRAND 333..338 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 344..353 FT /evidence="ECO:0007829|PDB:3CQX" FT TURN 354..356 FT /evidence="ECO:0007829|PDB:3CQX" FT TURN 365..367 FT /evidence="ECO:0007829|PDB:3CQX" FT HELIX 368..380 FT /evidence="ECO:0007829|PDB:3CQX" SQ SEQUENCE 646 AA; 70871 MW; 03A27B30E6C076ED CRC64; MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD //