HS12A_MOUSE
ID HS12A_MOUSE Reviewed; 675 AA.
AC Q8K0U4; Q3UQZ8; Q8CHF6;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Heat shock 70 kDa protein 12A;
GN Name=Hspa12a; Synonyms=Kiaa0417;
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 {ECO:0000312|EMBL:AAH30362.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Spinal ganglion;
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 [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina {ECO:0000312|EMBL:AAH30362.1};
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 [4]
RP PROTEIN SEQUENCE OF 99-109; 165-177; 362-372; 398-414; 504-529; 533-544;
RP 571-585 AND 641-654, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5] {ECO:0000305}
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12552099; DOI=10.1073/pnas.252764399;
RA Han Z., Truong Q.A., Park S., Breslow J.L.;
RT "Two Hsp70 family members expressed in atherosclerotic lesions.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1256-1261(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30679749; DOI=10.1038/s41598-018-37336-6;
RA Madsen P., Isaksen T.J., Siupka P., Toth A.E., Nyegaard M., Gustafsen C.,
RA Nielsen M.S.;
RT "HSPA12A targets the cytoplasmic domain and affects the trafficking of the
RT Amyloid Precursor Protein receptor SorLA.";
RL Sci. Rep. 9:611-611(2019).
CC -!- FUNCTION: Adapter protein for SORL1, but not SORT1. Delays SORL1
CC internalization and affects SORL1 subcellular localization.
CC {ECO:0000250|UniProtKB:O43301}.
CC -!- SUBUNIT: Interacts with SORL1 (via cytosolic C-terminus); this
CC interaction affects SORL1 internalization and subcellular localization.
CC {ECO:0000250|UniProtKB:O43301}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30679749}. Nucleus
CC {ECO:0000269|PubMed:30679749}.
CC -!- TISSUE SPECIFICITY: Expressed most strongly in brain, kidney and heart
CC with little or no expression in other tissues (PubMed:12552099). In the
CC brain, expressed in glial cells, including astrocytes (at protein
CC level) (PubMed:30679749). In the aorta, preferentially expressed in
CC lesions (PubMed:12552099). {ECO:0000269|PubMed:12552099,
CC ECO:0000269|PubMed:30679749}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB093239; BAC41423.1; ALT_INIT; mRNA.
DR EMBL; AK038491; BAC30016.1; -; mRNA.
DR EMBL; AK141925; BAE24890.1; -; mRNA.
DR EMBL; BC030362; AAH30362.1; -; mRNA.
DR EMBL; AY196789; AAO37638.1; -; mRNA.
DR CCDS; CCDS38032.1; -.
DR RefSeq; NP_001314927.1; NM_001327998.1.
DR RefSeq; NP_780408.1; NM_175199.3.
DR AlphaFoldDB; Q8K0U4; -.
DR BioGRID; 216020; 18.
DR IntAct; Q8K0U4; 3.
DR STRING; 10090.ENSMUSP00000066860; -.
DR iPTMnet; Q8K0U4; -.
DR PhosphoSitePlus; Q8K0U4; -.
DR SwissPalm; Q8K0U4; -.
DR jPOST; Q8K0U4; -.
DR MaxQB; Q8K0U4; -.
DR PaxDb; Q8K0U4; -.
DR PeptideAtlas; Q8K0U4; -.
DR PRIDE; Q8K0U4; -.
DR ProteomicsDB; 267163; -.
DR Antibodypedia; 2201; 105 antibodies from 22 providers.
DR Ensembl; ENSMUST00000066285; ENSMUSP00000066860; ENSMUSG00000025092.
DR GeneID; 73442; -.
DR KEGG; mmu:73442; -.
DR UCSC; uc008iaw.1; mouse.
DR CTD; 259217; -.
DR MGI; MGI:1920692; Hspa12a.
DR VEuPathDB; HostDB:ENSMUSG00000025092; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000154551; -.
DR HOGENOM; CLU_009958_5_3_1; -.
DR InParanoid; Q8K0U4; -.
DR OMA; TTELCKW; -.
DR OrthoDB; 804087at2759; -.
DR PhylomeDB; Q8K0U4; -.
DR TreeFam; TF329492; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 73442; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Hspa12a; mouse.
DR PRO; PR:Q8K0U4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K0U4; protein.
DR Bgee; ENSMUSG00000025092; Expressed in lateral geniculate body and 207 other tissues.
DR ExpressionAtlas; Q8K0U4; baseline and differential.
DR Genevisible; Q8K0U4; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR026685; HSPA12A.
DR PANTHER; PTHR14187:SF46; PTHR14187:SF46; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43301"
FT CHAIN 2..675
FT /note="Heat shock 70 kDa protein 12A"
FT /id="PRO_0000078293"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43301"
FT CONFLICT 128
FT /note="S -> N (in Ref. 1; BAC41423)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="H -> R (in Ref. 1; BAC41423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 74871 MW; 36FD7ADBF58E3653 CRC64;
MADKEAGGGD AGPRETAPTS TYSSPARSLG DTGITPLSPS HILNDADPVS EQQTFLVVVA
IDFGTTSSGY AYSFTKEPEC IHVMRRWEGG DPGVSNQKTP TTILLTPERK FHSFGYAARD
FYHDLDPSEA KQWLYLEKFK MKLHTTGDLT MDTDLTAANG KKVKALEIFA YALQYFKEQA
LKELSDQAGS DFENSDVRWV ITVPAIWKQP AKQFMREAAY QAGLASPENS EQLIIALEPE
AASIYCRKLR LHQMIELSSK AVVNGYSASD TVGAGFAQAK EHVRRNRQSR TFLVENVIGE
IWSELEEGDK YVVVDSGGGT VDLTVHQIRL PEGHLKELYK ATGGPYGSLG VDYEFEKLLC
KIFGEDFIEQ FKIKRPAAWV DLMIAFESRK RAAAPDRTNP LNITLPFSFI DYYKKFRGHS
VEHALRKSNV DFVKWSSQGM LRMSPDAMNA LFKPTIDSII EHLRDLFQKP EVSTVKFLFL
VGGFAEAPLL QQAVQTAFGD KCRIIIPQDV GLTILKGAVL FGLDPAVIKV RRSPLTYGVG
VLNRYVEGKH PPEKLLVKDG TRWCTDVFDK FISADQSVAL GELVKRSYTP AKPSQLVIII
NIYSSEHDNV SFITDPGVKK CGTLRLDLTG SGGTAVPARR EIQTIMQFGD TEIKATAVDI
TTSKSVKVGI DFLNY
