ID   DAAF5_HUMAN             Reviewed;         855 AA.
AC   Q86Y56; Q69YL1; Q96FI9; Q9NX75;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 4.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Dynein axonemal assembly factor 5 {ECO:0000303|PubMed:25232951, ECO:0000312|HGNC:HGNC:26013};
DE   AltName: Full=HEAT repeat-containing protein 2 {ECO:0000305};
GN   Name=DNAAF5 {ECO:0000303|PubMed:25232951,
GN   ECO:0000312|HGNC:HGNC:26013};
GN   Synonyms=HEATR2 {ECO:0000312|HGNC:HGNC:26013};
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), AND VARIANT LYS-743.
RC   TISSUE=Colon carcinoma;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 422-855 (ISOFORM 2), AND VARIANT LYS-743.
RC   TISSUE=Hippocampus, and Pancreas;
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 94-105; 423-438; 625-655 AND 804-814, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 662-855 (ISOFORMS 1/3), AND
RP   VARIANT LYS-743.
RC   TISSUE=Melanoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   INVOLVEMENT IN CILD18, FUNCTION, INTERACTION WITH DNAI2, SUBCELLULAR
RP   LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=25232951; DOI=10.1371/journal.pgen.1004577;
RA   Diggle C.P., Moore D.J., Mali G., zur Lage P., Ait-Lounis A., Schmidts M.,
RA   Shoemark A., Garcia Munoz A., Halachev M.R., Gautier P., Yeyati P.L.,
RA   Bonthron D.T., Carr I.M., Hayward B., Markham A.F., Hope J.E.,
RA   von Kriegsheim A., Mitchison H.M., Jackson I.J., Durand B., Reith W.,
RA   Sheridan E., Jarman A.P., Mill P.;
RT   "HEATR2 plays a conserved role in assembly of the ciliary motile
RT   apparatus.";
RL   PLoS Genet. 10:E1004577-E1004577(2014).
RN   [11]
RP   VARIANT CILD18 PRO-795, CHARACTERIZATION OF VARIANT CILD18 PRO-795,
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=23040496; DOI=10.1016/j.ajhg.2012.08.022;
RA   Horani A., Druley T.E., Zariwala M.A., Patel A.C., Levinson B.T.,
RA   Van Arendonk L.G., Thornton K.C., Giacalone J.C., Albee A.J., Wilson K.S.,
RA   Turner E.H., Nickerson D.A., Shendure J., Bayly P.V., Leigh M.W.,
RA   Knowles M.R., Brody S.L., Dutcher S.K., Ferkol T.W.;
RT   "Whole-exome capture and sequencing identifies HEATR2 mutation as a cause
RT   of primary ciliary dyskinesia.";
RL   Am. J. Hum. Genet. 91:685-693(2012).
CC   -!- FUNCTION: Cytoplasmic protein involved in the delivery of the dynein
CC       machinery to the motile cilium. It is required for the assembly of the
CC       axonemal dynein inner and outer arms, two structures attached to the
CC       peripheral outer doublet A microtubule of the axoneme, that play a
CC       crucial role in cilium motility. {ECO:0000269|PubMed:23040496,
CC       ECO:0000269|PubMed:25232951}.
CC   -!- SUBUNIT: Interacts with DNAI2; probably involved in outer arm dynein
CC       assembly. {ECO:0000269|PubMed:25232951}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23040496,
CC       ECO:0000269|PubMed:25232951}. Dynein axonemal particle
CC       {ECO:0000269|PubMed:23040496, ECO:0000269|PubMed:25232951}.
CC       Note=Observed only in the cytoplasm of ciliated cells and absent from
CC       cilia. {ECO:0000269|PubMed:23040496, ECO:0000269|PubMed:25232951}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q86Y56-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86Y56-2; Sequence=VSP_016110;
CC       Name=3;
CC         IsoId=Q86Y56-3; Sequence=VSP_016109;
CC   -!- TISSUE SPECIFICITY: Expressed in nasal epithelium and lung epithelium
CC       by ciliated cells (at protein level). {ECO:0000269|PubMed:23040496}.
CC   -!- DEVELOPMENTAL STAGE: Expressed by immature cells in the process of
CC       extending cilia. {ECO:0000269|PubMed:25232951}.
CC   -!- DISEASE: Ciliary dyskinesia, primary, 18 (CILD18) [MIM:614874]: A
CC       disorder characterized by abnormalities of motile cilia. Respiratory
CC       infections leading to chronic inflammation and bronchiectasis are
CC       recurrent, due to defects in the respiratory cilia; reduced fertility
CC       is often observed in male patients due to abnormalities of sperm tails.
CC       Half of the patients exhibit randomization of left-right body asymmetry
CC       and situs inversus, due to dysfunction of monocilia at the embryonic
CC       node. Primary ciliary dyskinesia associated with situs inversus is
CC       referred to as Kartagener syndrome. {ECO:0000269|PubMed:23040496,
CC       ECO:0000269|PubMed:25232951}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the DNAAF5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH10850.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK000404; BAA91142.1; -; mRNA.
DR   EMBL; AC144411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010850; AAH10850.1; ALT_INIT; mRNA.
DR   EMBL; BC047240; AAH47240.1; -; mRNA.
DR   EMBL; AL832914; CAH10624.2; -; mRNA.
DR   CCDS; CCDS34580.1; -. [Q86Y56-1]
DR   RefSeq; NP_060272.3; NM_017802.3. [Q86Y56-1]
DR   AlphaFoldDB; Q86Y56; -.
DR   BioGRID; 120260; 189.
DR   CORUM; Q86Y56; -.
DR   IntAct; Q86Y56; 34.
DR   MINT; Q86Y56; -.
DR   STRING; 9606.ENSP00000297440; -.
DR   GlyGen; Q86Y56; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q86Y56; -.
DR   PhosphoSitePlus; Q86Y56; -.
DR   SwissPalm; Q86Y56; -.
DR   BioMuta; DNAAF5; -.
DR   DMDM; 317373567; -.
DR   EPD; Q86Y56; -.
DR   jPOST; Q86Y56; -.
DR   MassIVE; Q86Y56; -.
DR   MaxQB; Q86Y56; -.
DR   PaxDb; 9606-ENSP00000297440; -.
DR   PeptideAtlas; Q86Y56; -.
DR   ProteomicsDB; 70375; -. [Q86Y56-1]
DR   ProteomicsDB; 70376; -. [Q86Y56-2]
DR   ProteomicsDB; 70377; -. [Q86Y56-3]
DR   Pumba; Q86Y56; -.
DR   Antibodypedia; 10790; 107 antibodies from 18 providers.
DR   DNASU; 54919; -.
DR   Ensembl; ENST00000297440.11; ENSP00000297440.6; ENSG00000164818.16. [Q86Y56-1]
DR   GeneID; 54919; -.
DR   KEGG; hsa:54919; -.
DR   MANE-Select; ENST00000297440.11; ENSP00000297440.6; NM_017802.4; NP_060272.3.
DR   UCSC; uc010krz.2; human. [Q86Y56-1]
DR   AGR; HGNC:26013; -.
DR   CTD; 54919; -.
DR   DisGeNET; 54919; -.
DR   GeneCards; DNAAF5; -.
DR   GeneReviews; DNAAF5; -.
DR   HGNC; HGNC:26013; DNAAF5.
DR   HPA; ENSG00000164818; Low tissue specificity.
DR   MalaCards; DNAAF5; -.
DR   MIM; 614864; gene.
DR   MIM; 614874; phenotype.
DR   neXtProt; NX_Q86Y56; -.
DR   OpenTargets; ENSG00000164818; -.
DR   Orphanet; 244; Primary ciliary dyskinesia.
DR   PharmGKB; PA145008229; -.
DR   VEuPathDB; HostDB:ENSG00000164818; -.
DR   eggNOG; ENOG502QRXT; Eukaryota.
DR   GeneTree; ENSGT00390000005666; -.
DR   HOGENOM; CLU_010823_1_0_1; -.
DR   InParanoid; Q86Y56; -.
DR   OMA; WTCYSPE; -.
DR   OrthoDB; 177908at2759; -.
DR   PhylomeDB; Q86Y56; -.
DR   TreeFam; TF326738; -.
DR   PathwayCommons; Q86Y56; -.
DR   SignaLink; Q86Y56; -.
DR   BioGRID-ORCS; 54919; 66 hits in 1151 CRISPR screens.
DR   ChiTaRS; DNAAF5; human.
DR   GenomeRNAi; 54919; -.
DR   Pharos; Q86Y56; Tbio.
DR   PRO; PR:Q86Y56; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q86Y56; Protein.
DR   Bgee; ENSG00000164818; Expressed in bronchial epithelial cell and 200 other cell types or tissues.
DR   ExpressionAtlas; Q86Y56; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IPI:UniProtKB.
DR   GO; GO:0003341; P:cilium movement; IMP:UniProtKB.
DR   GO; GO:0036159; P:inner dynein arm assembly; IMP:UniProtKB.
DR   GO; GO:0036158; P:outer dynein arm assembly; IMP:UniProtKB.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR034085; TOG.
DR   PANTHER; PTHR16216; DYNEIN ASSEMBLY FACTOR 5, AXONEMAL; 1.
DR   PANTHER; PTHR16216:SF2; DYNEIN AXONEMAL ASSEMBLY FACTOR 5; 1.
DR   Pfam; PF02985; HEAT; 2.
DR   SMART; SM01349; TOG; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
DR   Genevisible; Q86Y56; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Ciliopathy;
KW   Cilium biogenesis/degradation; Cytoplasm; Direct protein sequencing;
KW   Disease variant; Kartagener syndrome; Primary ciliary dyskinesia;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..855
FT                   /note="Dynein axonemal assembly factor 5"
FT                   /id="PRO_0000050820"
FT   REPEAT          71..109
FT                   /note="HEAT 1"
FT   REPEAT          202..240
FT                   /note="HEAT 2"
FT   REPEAT          241..278
FT                   /note="HEAT 3"
FT   REPEAT          280..318
FT                   /note="HEAT 4"
FT   REPEAT          354..376
FT                   /note="HEAT 5"
FT   REPEAT          377..414
FT                   /note="HEAT 6"
FT   REPEAT          599..638
FT                   /note="HEAT 7"
FT   REPEAT          696..734
FT                   /note="HEAT 8"
FT   REPEAT          738..776
FT                   /note="HEAT 9"
FT   REPEAT          784..822
FT                   /note="HEAT 10"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   VAR_SEQ         1..620
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_016109"
FT   VAR_SEQ         811..855
FT                   /note="EVLKEGSGLFPDLLVRETEAVIHKHRSATYCEQLLQHVQAVPATQ -> DVP
FT                   GSPSPSAMIGSFLRPPHPWRTVSQLNLFSS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016110"
FT   VARIANT         560
FT                   /note="R -> C (in dbSNP:rs73258248)"
FT                   /id="VAR_060463"
FT   VARIANT         632
FT                   /note="V -> A (in dbSNP:rs4720951)"
FT                   /id="VAR_056911"
FT   VARIANT         743
FT                   /note="R -> K (in dbSNP:rs3922641)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT                   /id="VAR_060464"
FT   VARIANT         795
FT                   /note="L -> P (in CILD18; decreased protein abundance;
FT                   dbSNP:rs397514561)"
FT                   /evidence="ECO:0000269|PubMed:23040496"
FT                   /id="VAR_068969"
FT   CONFLICT        128
FT                   /note="P -> H (in Ref. 3; AAH47240)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419..421
FT                   /note="SCT -> TSS (in Ref. 3; AAH10850)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="L -> M (in Ref. 3; AAH47240)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   855 AA;  93521 MW;  D1ED73FAEAC8F54C CRC64;
     MAALGVAEAV AAPHPAEGAE TAEAVELSRA LSRLLPGLEA DSKPGRRRAL EALRRALEEP
     GPAADPTAFQ GPWARLLLPR LLRCLSDPAE GCRALAVHLL DLGLRRAARP RDALPRLLPA
     LAARLAGPVP ARRPPEACEE LRLALVQLLG LAVDLCGAAL APHLDDALRA LRCSLLDPFA
     AVRRESCSCA AALAQATPDH FHMQSESLIG PLMQTISHQH WKVRVAAIEA TGAVIHFGNG
     KSVDDVLSHF AQRLFDDVPQ VRRAVASVVG GWLLCLRDRY SFFHKLIPLL LSSLNDEVPE
     VRQLAASLWE DVGLQWQKEN EEDLKDKLDF APPTPPHYPP HERRPVLGCR ELVFRNLSKI
     LPALCHDITD WVVGTRVKSA QLLPVLLLHA EDHATQHLEV VLRTLFQACT DEEAAVVQSC
     TRSAELVGTF VSPEVFLKLI LSTLKKTPSA SGLLVLASAM RGCPREALQP HLAAIATELA
     QAHICQASEN DLYLERLLLC VQALVSVCHE DCGVASLQLL DVLLTIVALA GATGLRDKAQ
     ETMDSLAMVE GVSSCQDLYR KHIGPLLERV TASHLDWTAH SPELLQFSVI VAQSGPALGE
     ALPHVVPTLR ACLQPSQDPQ MRLKLFSILS TVLLRATDTI NSQGQFPSYL ETVTKDILAP
     NLQWHAGRTA AAIRTAAVSC LWALTSSEVL SAEQIRDVQE TLMPQVLTTL EEDSKMTRLI
     SCRIINTFLK TSGGMTDPEK LIRIYPELLK RLDDVSNDVR MAAASTLVTW LQCVKGANAK
     SYYQSSVQYL YRELLVHLDD PERAIQDAIL EVLKEGSGLF PDLLVRETEA VIHKHRSATY
     CEQLLQHVQA VPATQ
//