ID DNJA3_MOUSE Reviewed; 480 AA.
AC Q99M87; Q8BSM0; Q99L09; Q99P71; Q99P76; Q9CT11; Q9DBJ7; Q9DC44;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=DnaJ homolog subfamily A member 3, mitochondrial;
DE AltName: Full=DnaJ protein Tid-1;
DE Short=mTid-1;
DE AltName: Full=Tumorous imaginal discs protein Tid56 homolog;
DE Flags: Precursor;
GN Name=Dnaja3; Synonyms=Tid1;
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] (ISOFORMS 1; 2 AND 3), AND INTERACTION WITH
RP RASA1.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=11116152; DOI=10.1074/jbc.m009267200;
RA Trentin G.A., Yin X., Tahir S., Lhotak S., Farhang-Fallah J., Li Y.,
RA Rozakis-Adcock M.;
RT "A mouse homologue of the Drosophila tumor suppressor l(2)tid gene defines
RT a novel Ras GTPase-activating protein (RasGAP)-binding protein.";
RL J. Biol. Chem. 276:13087-13095(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Forelimb, and Lung;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, INTERACTION WITH MUSK, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19038220; DOI=10.1016/j.neuron.2008.09.025;
RA Linnoila J., Wang Y., Yao Y., Wang Z.Z.;
RT "A mammalian homolog of Drosophila tumorous imaginal discs, Tid1, mediates
RT agrin signaling at the neuromuscular junction.";
RL Neuron 60:625-641(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Pancreas;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Modulates apoptotic signal transduction or effector
CC structures within the mitochondrial matrix. Affect cytochrome C release
CC from the mitochondria and caspase 3 activation, but not caspase 8
CC activation. Isoform 1 increases apoptosis triggered by both TNF and the
CC DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses
CC apoptosis. Can modulate IFN-gamma-mediated transcriptional activity (By
CC similarity). Isoform 2 may play a role in neuromuscular junction
CC development as an effector of the MUSK signaling pathway. {ECO:0000250,
CC ECO:0000269|PubMed:19038220}.
CC -!- SUBUNIT: Interacts with JAK2, HSPA9B and IFN-gammaR2 chain. Interacts
CC with Ras GTPase-activating protein 1 (RASA1). Isoform 2 interacts with
CC MUSK (via the cytoplasmic domain). {ECO:0000269|PubMed:11116152,
CC ECO:0000269|PubMed:19038220}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:19038220}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:19038220}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19038220}. Note=Recruited to the postsynaptic cell
CC membrane of the neuromuscular junction through interaction with MUSK.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Tid-1L, TID1L;
CC IsoId=Q99M87-1; Sequence=Displayed;
CC Name=2; Synonyms=Tid-1S, TID1S;
CC IsoId=Q99M87-2; Sequence=VSP_007427, VSP_007428;
CC Name=3;
CC IsoId=Q99M87-3; Sequence=VSP_007440;
CC -!- DOMAIN: Modulation of apoptosis, i.e. proapoptotic activity of isoform
CC 1 and antiapoptotic activity of isoform 2, is J domain-dependent (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated.
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DR EMBL; AY009320; AAG37303.1; -; mRNA.
DR EMBL; AF325535; AAK11222.1; -; mRNA.
DR EMBL; AF326358; AAK11223.1; -; mRNA.
DR EMBL; AK004575; BAB23384.1; -; mRNA.
DR EMBL; AK004910; BAB23661.1; -; mRNA.
DR EMBL; AK011535; BAB27682.2; -; mRNA.
DR EMBL; AK031250; BAC27321.1; -; mRNA.
DR EMBL; BC003920; AAH03920.1; -; mRNA.
DR EMBL; BC027240; AAH27240.1; -; mRNA.
DR CCDS; CCDS27922.1; -. [Q99M87-1]
DR CCDS; CCDS49748.1; -. [Q99M87-2]
DR RefSeq; NP_001128584.1; NM_001135112.1. [Q99M87-2]
DR RefSeq; NP_076135.3; NM_023646.4. [Q99M87-1]
DR AlphaFoldDB; Q99M87; -.
DR SMR; Q99M87; -.
DR BioGRID; 219986; 19.
DR IntAct; Q99M87; 6.
DR MINT; Q99M87; -.
DR STRING; 10090.ENSMUSP00000053842; -.
DR GlyGen; Q99M87; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99M87; -.
DR PhosphoSitePlus; Q99M87; -.
DR SwissPalm; Q99M87; -.
DR EPD; Q99M87; -.
DR jPOST; Q99M87; -.
DR MaxQB; Q99M87; -.
DR PaxDb; 10090-ENSMUSP00000053842; -.
DR PeptideAtlas; Q99M87; -.
DR ProteomicsDB; 277475; -. [Q99M87-1]
DR ProteomicsDB; 277476; -. [Q99M87-2]
DR ProteomicsDB; 277477; -. [Q99M87-3]
DR Pumba; Q99M87; -.
DR Antibodypedia; 24319; 312 antibodies from 33 providers.
DR DNASU; 83945; -.
DR Ensembl; ENSMUST00000060067.12; ENSMUSP00000053842.6; ENSMUSG00000004069.18. [Q99M87-1]
DR Ensembl; ENSMUST00000115854.4; ENSMUSP00000111520.4; ENSMUSG00000004069.18. [Q99M87-2]
DR Ensembl; ENSMUST00000229529.2; ENSMUSP00000155588.2; ENSMUSG00000004069.18. [Q99M87-3]
DR GeneID; 83945; -.
DR KEGG; mmu:83945; -.
DR UCSC; uc007yac.2; mouse. [Q99M87-1]
DR UCSC; uc012aat.1; mouse. [Q99M87-3]
DR AGR; MGI:1933786; -.
DR CTD; 9093; -.
DR MGI; MGI:1933786; Dnaja3.
DR VEuPathDB; HostDB:ENSMUSG00000004069; -.
DR eggNOG; KOG0715; Eukaryota.
DR GeneTree; ENSGT00940000155280; -.
DR HOGENOM; CLU_017633_0_5_1; -.
DR InParanoid; Q99M87; -.
DR OMA; CPECAGD; -.
DR OrthoDB; 276132at2759; -.
DR PhylomeDB; Q99M87; -.
DR TreeFam; TF105152; -.
DR BioGRID-ORCS; 83945; 23 hits in 78 CRISPR screens.
DR ChiTaRS; Dnaja3; mouse.
DR PRO; PR:Q99M87; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q99M87; Protein.
DR Bgee; ENSMUSG00000004069; Expressed in interventricular septum and 258 other cell types or tissues.
DR ExpressionAtlas; Q99M87; baseline and differential.
DR Genevisible; Q99M87; MM.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0030695; F:GTPase regulator activity; IDA:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0106137; F:IkappaB kinase complex binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0005133; F:type II interferon receptor binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IPI:MGI.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0090398; P:cellular senescence; IDA:MGI.
DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060336; P:negative regulation of type II interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR GO; GO:0034341; P:response to type II interferon; ISO:MGI.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR44145; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR44145:SF3; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Cell membrane; Chaperone;
KW Cytoplasm; Membrane; Metal-binding; Methylation; Mitochondrion;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..480
FT /note="DnaJ homolog subfamily A member 3, mitochondrial"
FT /id="PRO_0000007257"
FT DOMAIN 93..158
FT /note="J"
FT REPEAT 236..243
FT /note="CXXCXGXG motif"
FT REPEAT 253..260
FT /note="CXXCXGXG motif"
FT REPEAT 275..282
FT /note="CXXCXGXG motif"
FT REPEAT 289..296
FT /note="CXXCXGXG motif"
FT ZN_FING 223..301
FT /note="CR-type"
FT REGION 437..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="Omega-N-methylarginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT MOD_RES 134
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 238
FT /note="Omega-N-methylarginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT MOD_RES 293
FT /note="Omega-N-methylarginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT VAR_SEQ 211..261
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11116152"
FT /id="VSP_007440"
FT VAR_SEQ 448..453
FT /note="GRTMDS -> KRSTGN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11116152,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_007427"
FT VAR_SEQ 454..480
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11116152,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_007428"
FT CONFLICT 403
FT /note="D -> H (in Ref. 2; BAB23661)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="G -> E (in Ref. 2; BAB23384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 52443 MW; 30AA5557C18665A8 CRC64;
MAAWCSPRWL RVAVGTPRLP AAAGRGVQQP QGGVVATSLC RKLCVSAFGL SMGAHGPRAL
LTLRPGVRLT GTKSFPFVCT TSFHTSASLA KDDYYQILGV PRNASQKDIK KAYYQLAKKY
HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK RKQYDAYGSA GFDPGTSSSG QGYWRGGPSV
DPEELFRKIF GEFSSSPFGD FQNVFDQPQE YIMELTFNQA AKGVNKEFTV NIMDTCERCD
GKGNEPGTKV QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIITNPCV VCRGAGQAKQ
KKRVTIPVPA GVEDGQTVRM PVGKREIFVT FRVQKSPVFR RDGADIHSDL FISIAQAILG
GTAKAQGLYE TINVTIPAGI QTDQKIRLTG KGIPRINSYG YGDHYIHIKI RVPKRLSSRQ
QNLILSYAED ETDVEGTVNG VTHTSTGGRT MDSSAGSKDR REAGEDNEGF LSKLKKIFTS
//
