HSP7C_MOUSE
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 03-AUG-2022, entry version 179.
DE RecName: Full=Heat shock cognate 71 kDa protein;
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}; Synonyms=Hsc70, Hsc73;
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, Pancreas,
RC 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, activation of
CC proteolysis of misfolded proteins and the formation and dissociation of
CC protein complexes. Plays a pivotal role in the protein quality control
CC system, ensuring the correct folding of proteins, the re-folding of
CC misfolded proteins and controlling the targeting of proteins for
CC subsequent degradation. This is achieved through cycles of ATP binding,
CC ATP hydrolysis and ADP release, mediated by co-chaperones. The co-
CC chaperones have been shown to not only regulate different steps of the
CC ATPase cycle of HSP70, but they also have an individual specificity
CC such that one co-chaperone may promote folding of a substrate while
CC another may promote degradation. The affinity of HSP70 for polypeptides
CC is regulated by its nucleotide bound state. In the ATP-bound form, it
CC has a low affinity for substrate proteins. However, upon hydrolysis of
CC the ATP to ADP, it undergoes a conformational change that increases its
CC affinity for substrate proteins. HSP70 goes through repeated cycles of
CC ATP hydrolysis and nucleotide exchange, which permits cycles of
CC substrate binding and release. The HSP70-associated co-chaperones are
CC of three types: J-domain co-chaperones HSP40s (stimulate ATPase
CC hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as
CC BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-
CC bound state thereby promoting substrate release), and the TPR domain
CC chaperones such as HOPX and STUB1. Plays a critical role in
CC mitochondrial import, delivers preproteins to the mitochondrial import
CC receptor TOMM70. Acts as a repressor of transcriptional activation.
CC Inhibits the transcriptional coactivator activity of CITED1 on Smad-
CC mediated transcription. Component of the PRP19-CDC5L complex that forms
CC an integral part of the spliceosome and is required for activating pre-
CC mRNA splicing. May have a scaffolding role in the spliceosome assembly
CC as it contacts all other components of the core complex. Binds
CC bacterial lipopolysaccharide (LPS) and mediates LPS-induced
CC inflammatory response, including TNF secretion by monocytes.
CC Participates in the ER-associated degradation (ERAD) quality control
CC pathway in conjunction with J domain-containing co-chaperones and the
CC E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21.
CC {ECO:0000250|UniProtKB:P11142}.
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 ASCL2, 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). {ECO:0000250|UniProtKB:P11142,
CC ECO:0000250|UniProtKB:P63018, ECO:0000269|PubMed:15292236,
CC ECO:0000269|PubMed:17233114, ECO:0000269|PubMed:21502331,
CC 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}. Melanosome
CC {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs. Translocates rapidly from the cytoplasm to the
CC nuclei, and especially to the nucleoli, upon heat shock (By
CC similarity). {ECO:0000250}.
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};
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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; 168.
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 CarbonylDB; P63017; -.
DR iPTMnet; P63017; -.
DR PhosphoSitePlus; P63017; -.
DR SwissPalm; P63017; -.
DR COMPLUYEAST-2DPAGE; P63017; -.
DR REPRODUCTION-2DPAGE; IPI00323357; -.
DR REPRODUCTION-2DPAGE; P63017; -.
DR REPRODUCTION-2DPAGE; Q6NZD0; -.
DR SWISS-2DPAGE; P63017; -.
DR UCD-2DPAGE; P63017; -.
DR CPTAC; non-CPTAC-3713; -.
DR EPD; P63017; -.
DR jPOST; P63017; -.
DR MaxQB; P63017; -.
DR PaxDb; P63017; -.
DR PeptideAtlas; P63017; -.
DR PRIDE; P63017; -.
DR ProteomicsDB; 273196; -.
DR Antibodypedia; 3675; 1192 antibodies from 44 providers.
DR DNASU; 15481; -.
DR Ensembl; ENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656.
DR GeneID; 15481; -.
DR KEGG; mmu:15481; -.
DR UCSC; uc009ozx.3; mouse.
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; 288077at2759; -.
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 BioGRID-ORCS; 15481; 31 hits in 73 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 121 other tissues.
DR ExpressionAtlas; P63017; baseline and differential.
DR Genevisible; P63017; MM.
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:0101031; C:chaperone complex; 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:ParkinsonsUK-UCL.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
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:0043005; C:neuron projection; ISO:MGI.
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: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:0051087; F:chaperone 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:0051787; F:misfolded protein binding; IBA:GO_Central.
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:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
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:0007568; P:aging; IEA:Ensembl.
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:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
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; IGI:MGI.
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; ISO:MGI.
DR GO; GO:0044788; P:modulation by host of viral process; IMP:AgBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IEA:Ensembl.
DR GO; GO:1902904; P:negative regulation of supramolecular fiber organization; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0097214; P:positive regulation of lysosomal membrane permeability; ISO:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:1904592; P:positive regulation of protein refolding; ISO:MGI.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IDA:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0042026; P:protein refolding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; ISO:MGI.
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:0007608; P:sensory perception of smell; 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:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
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; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Isopeptide bond; Membrane;
KW Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Spliceosome;
KW Stress response; Transcription; 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 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 268..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 339..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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
