ATD3B_HUMAN
ID ATD3B_HUMAN Reviewed; 648 AA.
AC Q5T9A4; A8K3H1; Q6ZRB5; Q9BUK4; Q9ULE7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=ATPase family AAA domain-containing protein 3B;
DE AltName: Full=AAA-TOB3;
GN Name=ATAD3B; Synonyms=KIAA1273, TOB3;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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] (ISOFORMS 1 AND 3).
RC TISSUE=Leiomyosarcoma, and Placenta;
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 OF ISOFORMS 1 AND 3, SUBCELLULAR LOCATION, INDUCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16909202; DOI=10.1007/s00018-006-6200-x;
RA Schaffrik M., Mack B., Matthias C., Rauch J., Gires O.;
RT "Molecular characterization of the tumor-associated antigen AAA-TOB3.";
RL Cell. Mol. Life Sci. 63:2162-2174(2006).
RN [7]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=18063578; DOI=10.1074/jbc.m708444200;
RA Bogenhagen D.F., Rousseau D., Burke S.;
RT "The layered structure of human mitochondrial DNA nucleoids.";
RL J. Biol. Chem. 283:3665-3675(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-427, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
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 [10]
RP FUNCTION, INTERACTION WITH ATAD3A, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND TOPOLOGY.
RX PubMed=22664726; DOI=10.1016/j.mito.2012.05.005;
RA Merle N., Feraud O., Gilquin B., Hubstenberger A., Kieffer-Jacquinot S.,
RA Assard N., Bennaceur-Griscelli A., Honnorat J., Baudier J.;
RT "ATAD3B is a human embryonic stem cell specific mitochondrial protein, re-
RT expressed in cancer cells, that functions as dominant negative for the
RT ubiquitous ATAD3A.";
RL Mitochondrion 12:441-448(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP INTERACTION WITH PROTEINS INVOLVED IN MITOCHONDRIAL TRANSLATION; RNA
RP METABOLISM; ATAD3A AND GADD45GIP1.
RX PubMed=22453275; DOI=10.1093/nar/gks266;
RA He J., Cooper H.M., Reyes A., Di Re M., Sembongi H., Litwin T.R., Gao J.,
RA Neuman K.C., Fearnley I.M., Spinazzola A., Walker J.E., Holt I.J.;
RT "Mitochondrial nucleoid interacting proteins support mitochondrial protein
RT synthesis.";
RL Nucleic Acids Res. 40:6109-6121(2012).
CC -!- FUNCTION: May play a role in a mitochondrial network organization
CC typical for stem cells, characterized by reduced mitochondrial
CC metabolism, low mtDNA copies and fragmentated mitochondrial network.
CC may act by suppressing ATAD3A function, interfering with ATAD3A
CC interaction with matrix nucleoid complexes.
CC {ECO:0000269|PubMed:22664726}.
CC -!- SUBUNIT: Forms heterooligomers with ATAD3A. Interacts with components
CC of the mitochondrial ribosome, including MRPL11 and MRPS18B, and with
CC other proteins involved in mitochondrial RNA metabolism, possibly via
CC interaction with ATAD3A. Interacts with GADD45GIP1.
CC {ECO:0000269|PubMed:22453275, ECO:0000269|PubMed:22664726}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16909202, ECO:0000269|PubMed:18063578}; Peripheral
CC membrane protein {ECO:0000269|PubMed:16909202,
CC ECO:0000269|PubMed:18063578}. Note=Has been found to co-purify with
CC nucleoids (PubMed:22453275). Since it does not face the mitochondrial
CC matrix, the association with nucleoids could be mediated by ATAD3A.
CC {ECO:0000269|PubMed:22453275}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=AAA-TOB3l;
CC IsoId=Q5T9A4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T9A4-2; Sequence=VSP_015637, VSP_015640, VSP_015641,
CC VSP_015642;
CC Name=3; Synonyms=AAA-TOB3s;
CC IsoId=Q5T9A4-3; Sequence=VSP_015638, VSP_015639;
CC -!- TISSUE SPECIFICITY: Tends to be down-regulated in differentiated cells
CC and re-expressed in pluripotent stem cells or cancer cells (at protein
CC level). {ECO:0000269|PubMed:16909202, ECO:0000269|PubMed:22664726}.
CC -!- DEVELOPMENTAL STAGE: Expressed in proliferating embryonic stem cells
CC and down-regulated during differentiation.
CC {ECO:0000269|PubMed:22664726}.
CC -!- INDUCTION: Up-regulated by MYC. {ECO:0000269|PubMed:16909202}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86587.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB033099; BAA86587.1; ALT_INIT; mRNA.
DR EMBL; AK128357; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK290586; BAF83275.1; -; mRNA.
DR EMBL; AL157945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56193.1; -; Genomic_DNA.
DR EMBL; BC002542; AAH02542.1; -; mRNA.
DR EMBL; BC009938; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC018701; AAH18701.1; -; mRNA.
DR CCDS; CCDS30.1; -. [Q5T9A4-1]
DR RefSeq; NP_001304167.1; NM_001317238.1. [Q5T9A4-3]
DR RefSeq; NP_114127.3; NM_031921.5. [Q5T9A4-1]
DR AlphaFoldDB; Q5T9A4; -.
DR SMR; Q5T9A4; -.
DR BioGRID; 123774; 169.
DR IntAct; Q5T9A4; 130.
DR MINT; Q5T9A4; -.
DR STRING; 9606.ENSP00000311766; -.
DR iPTMnet; Q5T9A4; -.
DR PhosphoSitePlus; Q5T9A4; -.
DR SwissPalm; Q5T9A4; -.
DR BioMuta; ATAD3B; -.
DR DMDM; 74745646; -.
DR EPD; Q5T9A4; -.
DR jPOST; Q5T9A4; -.
DR MassIVE; Q5T9A4; -.
DR MaxQB; Q5T9A4; -.
DR PaxDb; Q5T9A4; -.
DR PeptideAtlas; Q5T9A4; -.
DR PRIDE; Q5T9A4; -.
DR ProteomicsDB; 64783; -. [Q5T9A4-1]
DR ProteomicsDB; 64784; -. [Q5T9A4-2]
DR ProteomicsDB; 64785; -. [Q5T9A4-3]
DR Antibodypedia; 26380; 84 antibodies from 25 providers.
DR DNASU; 83858; -.
DR Ensembl; ENST00000673477.1; ENSP00000500094.1; ENSG00000160072.20. [Q5T9A4-1]
DR GeneID; 83858; -.
DR KEGG; hsa:83858; -.
DR MANE-Select; ENST00000673477.1; ENSP00000500094.1; NM_031921.6; NP_114127.3.
DR UCSC; uc001afv.4; human. [Q5T9A4-1]
DR CTD; 83858; -.
DR DisGeNET; 83858; -.
DR GeneCards; ATAD3B; -.
DR HGNC; HGNC:24007; ATAD3B.
DR HPA; ENSG00000160072; Low tissue specificity.
DR MIM; 612317; gene.
DR neXtProt; NX_Q5T9A4; -.
DR OpenTargets; ENSG00000160072; -.
DR PharmGKB; PA134993325; -.
DR VEuPathDB; HostDB:ENSG00000160072; -.
DR eggNOG; KOG0742; Eukaryota.
DR GeneTree; ENSGT00940000167742; -.
DR HOGENOM; CLU_011488_2_0_1; -.
DR InParanoid; Q5T9A4; -.
DR OMA; RSKLIMT; -.
DR OrthoDB; 357201at2759; -.
DR PhylomeDB; Q5T9A4; -.
DR TreeFam; TF313922; -.
DR PathwayCommons; Q5T9A4; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q5T9A4; -.
DR BioGRID-ORCS; 83858; 26 hits in 1067 CRISPR screens.
DR ChiTaRS; ATAD3B; human.
DR GenomeRNAi; 83858; -.
DR Pharos; Q5T9A4; Tbio.
DR PRO; PR:Q5T9A4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T9A4; protein.
DR Bgee; ENSG00000160072; Expressed in adenohypophysis and 171 other tissues.
DR ExpressionAtlas; Q5T9A4; baseline and differential.
DR Genevisible; Q5T9A4; HS.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR039188; ATAD3.
DR InterPro; IPR021911; ATAD3_N.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23075; PTHR23075; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF12037; DUF3523; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Coiled coil; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..648
FT /note="ATPase family AAA domain-containing protein 3B"
FT /id="PRO_0000084800"
FT TOPO_DOM 2..246
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT INTRAMEM 247..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..648
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..214
FT /evidence="ECO:0000255"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 427
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 495
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q925I1"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015637"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015638"
FT VAR_SEQ 47..94
FT /note="WSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLK ->
FT MQLEALNLLHTLVWARSLCRAGAVQTQERLSGSASPEQVPAGECCALQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015639"
FT VAR_SEQ 119..128
FT /note="LSEETRQHQA -> MCLCRPLLPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015640"
FT VAR_SEQ 252..284
FT /note="AGLTLLAVGVYSAKNATAVTGRFIEARLGKPSL -> NIFIKQGWQVAERQH
FT VGASWSPRSCPCRLCTAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015641"
FT VAR_SEQ 285..648
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015642"
FT VARIANT 7
FT /note="V -> I (in dbSNP:rs1240504)"
FT /id="VAR_048120"
FT CONFLICT 149
FT /note="Q -> R (in Ref. 5; AAH02542/AAH18701)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="E -> V (in Ref. 2; AK128357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 72573 MW; 5133DB55E3415707 CRC64;
MSWLFGVNKG PKGEGAGPPP PLPPAQPGAE GGGDRGLGDR PAPKDKWSNF DPTGLERAAK
AARELEHSRY AKEALNLAQM QEQTLQLEQQ SKLKEYEAAV EQLKSEQIRA QAEERRKTLS
EETRQHQARA QYQDKLARQR YEDQLKQQQL LNEENLRKQE ESVQKQEAMR RATVEREMEL
RHKNEMLRVE TEARARAKAE RENADIIREQ IRLKASEHRQ TVLESIRTAG TLFGEGFRAF
VTDRDKVTAT VAGLTLLAVG VYSAKNATAV TGRFIEARLG KPSLVRETSR ITVLEALRHP
IQVSRRLLSR PQDVLEGVVL SPSLEARVRD IAIATRNTKK NRGLYRHILL YGPPGTGKTL
FAKKLALHSG MDYAIMTGGD VAPMGREGVT AMHKLFDWAN TSRRGLLLFM DEADAFLRKR
ATEEISKDLR ATLNAFLYHM GQHSNKFMLV LASNLPEQFD CAINSRIDVM VHFDLPQQEE
RERLVRLHFD NCVLKPATEG KRRLKLAQFD YGRKCSEVAR LTEGMSGREI AQLAVSWQAT
AYASKDGVLT EAMMDACVQD AVQQYRQKMR WLKAEGPGRG VEHPLSGVQG ETLTSWSLAT
DPSYPCLAGP CTFRICSWMG TGLCPGPLSP RMSCGGGRPF CPPGHPLL
