HS74L_MOUSE
ID HS74L_MOUSE Reviewed; 838 AA.
AC P48722; P97854; Q3TQN2; Q3UNG4; Q8BQD0; Q8CC45; Q91X29;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Heat shock 70 kDa protein 4L;
DE AltName: Full=Heat shock 70-related protein APG-1;
DE AltName: Full=Osmotic stress protein 94;
GN Name=Hspa4l; Synonyms=Apg1, Hsp4l, Osp94;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8647834; DOI=10.1074/jbc.271.21.12327;
RA Kojima R., Randall J., Brenner B.M., Gullans S.R.;
RT "Osmotic stress protein 94 (Osp94). A new member of the Hsp110/SSE gene
RT subfamily.";
RL J. Biol. Chem. 271:12327-12332(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC STRAIN=DDY/STD; TISSUE=Testis;
RX PubMed=9006898; DOI=10.1074/jbc.272.5.2640;
RA Kaneko Y., Nishiyama H., Nonoguchi K., Higashitsuji H., Kishishita M.,
RA Fujita J.;
RT "A novel hsp110-related gene, apg-1, that is abundantly expressed in the
RT testis responds to a low temperature heat shock rather than the traditional
RT elevated temperatures.";
RL J. Biol. Chem. 272:2640-2645(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ddY; TISSUE=Testis;
RA Kaneko Y., Fujita J.;
RT "Apg-1b, an alternative form of apg-1 transcript.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Brain, and Salivary 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 135-153; 484-500 AND 622-632, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; THR-545 AND SER-579, AND
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).
CC -!- FUNCTION: Possesses chaperone activity in vitro where it inhibits
CC aggregation of citrate synthase. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P48722; Q99P72: Rtn4; NbExp=4; IntAct=EBI-8314699, EBI-3869532;
CC P48722; Q9JK11-1: Rtn4; Xeno; NbExp=6; IntAct=EBI-8314699, EBI-919989;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=May translocate to the nucleus after heat shock. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48722-1; Sequence=Displayed;
CC Name=2; Synonyms=Apg-1b;
CC IsoId=P48722-2; Sequence=VSP_007500;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in renal
CC medulla of water-restricted animals. {ECO:0000269|PubMed:8647834}.
CC -!- INDUCTION: By hyperosmolar salt stress and heat shock.
CC {ECO:0000269|PubMed:9006898}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U23921; AAC52610.1; -; mRNA.
DR EMBL; D49482; BAA08446.1; -; mRNA.
DR EMBL; AB001926; BAA19468.1; -; mRNA.
DR EMBL; AK033950; BAC28524.1; -; mRNA.
DR EMBL; AK050997; BAC34491.1; -; mRNA.
DR EMBL; AK144225; BAE25783.1; -; mRNA.
DR EMBL; AK163459; BAE37350.1; -; mRNA.
DR EMBL; BC012712; AAH12712.1; -; mRNA.
DR EMBL; BC057002; AAH57002.1; -; mRNA.
DR EMBL; BC110662; AAI10663.1; -; mRNA.
DR CCDS; CCDS17327.1; -. [P48722-1]
DR RefSeq; NP_035150.3; NM_011020.3. [P48722-1]
DR RefSeq; XP_006500829.2; XM_006500766.3. [P48722-1]
DR RefSeq; XP_006500830.1; XM_006500767.3. [P48722-1]
DR AlphaFoldDB; P48722; -.
DR SMR; P48722; -.
DR BioGRID; 201985; 22.
DR IntAct; P48722; 4.
DR MINT; P48722; -.
DR STRING; 10090.ENSMUSP00000076336; -.
DR iPTMnet; P48722; -.
DR PhosphoSitePlus; P48722; -.
DR SwissPalm; P48722; -.
DR REPRODUCTION-2DPAGE; IPI00317710; -.
DR REPRODUCTION-2DPAGE; P48722; -.
DR EPD; P48722; -.
DR jPOST; P48722; -.
DR MaxQB; P48722; -.
DR PaxDb; P48722; -.
DR PeptideAtlas; P48722; -.
DR PRIDE; P48722; -.
DR ProteomicsDB; 273384; -. [P48722-1]
DR ProteomicsDB; 273385; -. [P48722-2]
DR Antibodypedia; 26922; 153 antibodies from 28 providers.
DR DNASU; 18415; -.
DR Ensembl; ENSMUST00000108086; ENSMUSP00000103721; ENSMUSG00000025757. [P48722-2]
DR Ensembl; ENSMUST00000204702; ENSMUSP00000145468; ENSMUSG00000025757. [P48722-1]
DR GeneID; 18415; -.
DR KEGG; mmu:18415; -.
DR UCSC; uc008pbk.1; mouse. [P48722-1]
DR CTD; 22824; -.
DR MGI; MGI:107422; Hspa4l.
DR VEuPathDB; HostDB:ENSMUSG00000025757; -.
DR eggNOG; KOG0103; Eukaryota.
DR GeneTree; ENSGT00940000158736; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; P48722; -.
DR OMA; AYDRHFG; -.
DR OrthoDB; 406172at2759; -.
DR PhylomeDB; P48722; -.
DR TreeFam; TF105043; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 18415; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Hspa4l; mouse.
DR PRO; PR:P48722; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P48722; protein.
DR Bgee; ENSMUSG00000025757; Expressed in spermatid and 162 other tissues.
DR ExpressionAtlas; P48722; baseline and differential.
DR Genevisible; P48722; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
DR CDD; cd11738; HSPA4L_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 2.
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 InterPro; IPR042708; HSPA4L_NBD.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..838
FT /note="Heat shock 70 kDa protein 4L"
FT /id="PRO_0000078281"
FT REGION 506..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 545
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 761
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 1..36
FT /note="MSVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTP -> MGGPPRHGVLDR
FT EER (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_007500"
FT CONFLICT 175..176
FT /note="TA -> HS (in Ref. 2; BAA08446 and 3; BAA19468)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="K -> E (in Ref. 2; BAA08446 and 3; BAA19468)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="A -> P (in Ref. 2; BAA08446 and 3; BAA19468)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="Q -> R (in Ref. 2; BAA08446 and 3; BAA19468)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="R -> S (in Ref. 4; BAE37350)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="T -> A (in Ref. 4; BAE37350)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="K -> M (in Ref. 1; AAC52610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 838 AA; 94382 MW; B2C5847DA7EAF6B7 CRC64;
MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN AAKSQIVTNV
RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSTG VKVRYLEEER PFAIEQVTGM
LLAKLKETSE NALKKPVADC VISIPSFFTD AERRSVMAAA QVAGLNCLRL MNETTAVALA
YGIYKQDLPS LDEKPRNVVF IDMGHSAYQV SVCAFNKGKL KVLATTFDPY LGGRNFDEAL
VDYFCDEFKT KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK
MNRAQFEQLC ASLLARVEPP LKSVMDQANL QREDINSIEI VGGATRIPAV KEQVTRFFLK
DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY SVTLRWKTSF EEGTGECEVF
SKNHPAPFSK VITFHKKEPF ELEAFYTNLH EVPYPDPRIG NFTIQNVFPQ SDGDSSKVKV
KVRINIHGIF SVASASVIEK QNLEGDHNDA AMETEAPKSE GKEDVDKMQV DQEEGGHQKC
HAEHTPEEEI DHTGAKAKAP PSDKQDRINQ TIKKGKIKSI DLPIQSSLYR QLTQDLLNSY
IENEGKMIMQ DKLEKERNDA KNAVEEYVYD FRDKLGTVYE KFITPEDMNK LSAMLEDTEN
WLYEEGEDQP KQVYVDRLQE LKKYGQPIQM KYVEHEERPK ALNDLGKKIQ LVLKVIEAHR
NKDERYDHLD PAEMERVEKY ISDSMNWLNS KMNAQNKLSL TQDPVVKVSE IVTKSKELDN
FCNPIVYKPK PKVEAPEDKA KTGSEHNGPM DGQSGSETSP DPPKGSSQHT DSGEMEVD
