DNJA2_HUMAN
ID DNJA2_HUMAN Reviewed; 412 AA.
AC O60884; B2R7L7; O14711;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=DnaJ homolog subfamily A member 2;
DE AltName: Full=Cell cycle progression restoration gene 3 protein;
DE AltName: Full=Dnj3;
DE Short=Dj3;
DE AltName: Full=HIRA-interacting protein 4;
DE AltName: Full=Renal carcinoma antigen NY-REN-14;
DE Flags: Precursor;
GN Name=DNAJA2; Synonyms=CPR3, HIRIP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lorain S., Brendel C., Scamps C., Lecluse Y., Lipinski M.;
RT "HIRIP4, a new human DnaJ, is a nuclear protein that interacts with the
RT product of the DiGeorge syndrome gene candidate HIRA.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9383053; DOI=10.1093/genetics/147.3.1063;
RA Edwards M.C., Liegeois N., Horecka J., DePinho R.A., Sprague G.F. Jr.,
RA Tyers M., Elledge S.J.;
RT "Human CPR (cell cycle progression restoration) genes impart a Far-
RT phenotype on yeast cells.";
RL Genetics 147:1063-1076(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
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 IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10816573; DOI=10.1074/jbc.m002021200;
RA Terada K., Mori M.;
RT "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of
RT hsc70.";
RL J. Biol. Chem. 275:24728-24734(2000).
RN [8]
RP ISOPRENYLATION AT CYS-409.
RX PubMed=15308774; DOI=10.1073/pnas.0403413101;
RA Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J., Jaunbergs J.,
RA Weinbaum C., Tamanoi F., Falck J., Zhao Y.;
RT "A tagging-via-substrate technology for detection and proteomics of
RT farnesylated proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION.
RX PubMed=24318877; DOI=10.1074/jbc.m113.521997;
RA Rauch J.N., Gestwicki J.E.;
RT "Binding of human nucleotide exchange factors to heat shock protein 70
RT (Hsp70) generates functionally distinct complexes in vitro.";
RL J. Biol. Chem. 289:1402-1414(2014).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-391; SER-394 AND SER-395, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the
CC folding of unfolded proteins mediated by HSPA1A/B (in vitro)
CC (PubMed:24318877). {ECO:0000269|PubMed:24318877}.
CC -!- INTERACTION:
CC O60884; Q9GZX7: AICDA; NbExp=3; IntAct=EBI-352957, EBI-3834328;
CC O60884; Q8WW22: DNAJA4; NbExp=2; IntAct=EBI-352957, EBI-2555157;
CC O60884; P63172: DYNLT1; NbExp=3; IntAct=EBI-352957, EBI-1176455;
CC O60884; Q9Y266: NUDC; NbExp=2; IntAct=EBI-352957, EBI-357298;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
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DR EMBL; AJ001309; CAA04669.1; -; mRNA.
DR EMBL; Y13350; CAA73791.1; -; mRNA.
DR EMBL; AF011793; AAB69313.1; -; mRNA.
DR EMBL; AK313031; BAG35864.1; -; mRNA.
DR EMBL; CH471092; EAW82693.1; -; Genomic_DNA.
DR EMBL; BC013044; AAH13044.1; -; mRNA.
DR EMBL; BC015809; AAH15809.1; -; mRNA.
DR CCDS; CCDS10726.1; -.
DR RefSeq; NP_005871.1; NM_005880.3.
DR AlphaFoldDB; O60884; -.
DR SMR; O60884; -.
DR BioGRID; 115582; 500.
DR CORUM; O60884; -.
DR DIP; DIP-33143N; -.
DR IntAct; O60884; 114.
DR MINT; O60884; -.
DR STRING; 9606.ENSP00000314030; -.
DR ChEMBL; CHEMBL4295671; -.
DR GlyGen; O60884; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60884; -.
DR MetOSite; O60884; -.
DR PhosphoSitePlus; O60884; -.
DR SwissPalm; O60884; -.
DR BioMuta; DNAJA2; -.
DR CPTAC; CPTAC-496; -.
DR CPTAC; CPTAC-497; -.
DR EPD; O60884; -.
DR jPOST; O60884; -.
DR MassIVE; O60884; -.
DR MaxQB; O60884; -.
DR PaxDb; O60884; -.
DR PeptideAtlas; O60884; -.
DR PRIDE; O60884; -.
DR ProteomicsDB; 49650; -.
DR Antibodypedia; 28078; 408 antibodies from 31 providers.
DR DNASU; 10294; -.
DR Ensembl; ENST00000317089.10; ENSP00000314030.5; ENSG00000069345.12.
DR GeneID; 10294; -.
DR KEGG; hsa:10294; -.
DR MANE-Select; ENST00000317089.10; ENSP00000314030.5; NM_005880.4; NP_005871.1.
DR UCSC; uc002eeo.3; human.
DR CTD; 10294; -.
DR DisGeNET; 10294; -.
DR GeneCards; DNAJA2; -.
DR HGNC; HGNC:14884; DNAJA2.
DR HPA; ENSG00000069345; Low tissue specificity.
DR MIM; 611322; gene.
DR neXtProt; NX_O60884; -.
DR OpenTargets; ENSG00000069345; -.
DR PharmGKB; PA27409; -.
DR VEuPathDB; HostDB:ENSG00000069345; -.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000154688; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; O60884; -.
DR OMA; RVCPTCV; -.
DR OrthoDB; 1012379at2759; -.
DR PhylomeDB; O60884; -.
DR TreeFam; TF105141; -.
DR PathwayCommons; O60884; -.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR SignaLink; O60884; -.
DR BioGRID-ORCS; 10294; 29 hits in 1079 CRISPR screens.
DR ChiTaRS; DNAJA2; human.
DR GeneWiki; DNAJA2; -.
DR GenomeRNAi; 10294; -.
DR Pharos; O60884; Tbio.
DR PRO; PR:O60884; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O60884; protein.
DR Bgee; ENSG00000069345; Expressed in calcaneal tendon and 206 other tissues.
DR ExpressionAtlas; O60884; baseline and differential.
DR Genevisible; O60884; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
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; IPR044713; DNJA1/2-like.
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; PTHR43888; PTHR43888; 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; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
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; Chaperone; Isopeptide bond; Lipoprotein; Membrane;
KW Metal-binding; Methylation; Phosphoprotein; Prenylation;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..409
FT /note="DnaJ homolog subfamily A member 2"
FT /id="PRO_0000071011"
FT PROPEP 410..412
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000393942"
FT DOMAIN 8..70
FT /note="J"
FT REPEAT 143..150
FT /note="CXXCXGXG motif"
FT REPEAT 159..166
FT /note="CXXCXGXG motif"
FT REPEAT 186..193
FT /note="CXXCXGXG motif"
FT REPEAT 202..209
FT /note="CXXCXGXG motif"
FT ZN_FING 130..214
FT /note="CR-type"
FT REGION 365..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYJ0"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35824"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYJ0"
FT MOD_RES 391
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 409
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 409
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:15308774"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 17
FT /note="P -> A (in Ref. 2; AAB69313)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..46
FT /note="NAGDK -> QMQETN (in Ref. 2; AAB69313)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..93
FT /note="GMDDIFSHIFG -> WHGLIFSLTVFC (in Ref. 2; AAB69313)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..257
FT /note="GVEPGDIVLLLQEKEH -> EWNPETLFFLLPGEKNM (in Ref. 2;
FT AAB69313)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="FK -> LS (in Ref. 2; AAB69313)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="D -> G (in Ref. 2; AAB69313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 45746 MW; 8F1BC367425CB428 CRC64;
MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP
EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL
KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ
QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA
PGVEPGDIVL LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD GRQIVVKYPP
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE
VPNIIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ
