DAAF5_HUMAN
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 03-AUG-2022, entry version 170.
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, 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; 175.
DR CORUM; Q86Y56; -.
DR IntAct; Q86Y56; 32.
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; Q86Y56; -.
DR PeptideAtlas; Q86Y56; -.
DR PRIDE; Q86Y56; -.
DR ProteomicsDB; 70375; -. [Q86Y56-1]
DR ProteomicsDB; 70376; -. [Q86Y56-2]
DR ProteomicsDB; 70377; -. [Q86Y56-3]
DR Antibodypedia; 10790; 90 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 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; RKHMGPL; -.
DR PhylomeDB; Q86Y56; -.
DR TreeFam; TF326738; -.
DR PathwayCommons; Q86Y56; -.
DR SignaLink; Q86Y56; -.
DR BioGRID-ORCS; 54919; 60 hits in 1073 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 198 other tissues.
DR ExpressionAtlas; Q86Y56; baseline and differential.
DR Genevisible; Q86Y56; HS.
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; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
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
