DAAF1_HUMAN
ID DAAF1_HUMAN Reviewed; 725 AA.
AC Q8NEP3; B4DJA3; Q69YI8; Q69YJ0; Q69YW5; Q96LP3; Q96MB6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 5.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Dynein axonemal assembly factor 1;
DE AltName: Full=Leucine-rich repeat-containing protein 50;
GN Name=DNAAF1; Synonyms=LRRC50;
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] (ISOFORMS 2 AND 3), AND VARIANTS
RP ARG-393; LEU-502; SER-633; PRO-659 AND THR-675.
RC TISSUE=Subthalamic nucleus, and Testis;
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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-393;
RP LEU-502; CYS-545; SER-633; PRO-659 AND THR-675.
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-548 AND 567-725 (ISOFORM 1),
RP AND VARIANTS ARG-393 AND LEU-502.
RC TISSUE=Testis;
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18385425; DOI=10.1681/asn.2007080917;
RA van Rooijen E., Giles R.H., Voest E.E., van Rooijen C., Schulte-Merker S.,
RA van Eeden F.J.;
RT "LRRC50, a conserved ciliary protein implicated in polycystic kidney
RT disease.";
RL J. Am. Soc. Nephrol. 19:1128-1138(2008).
RN [6]
RP FUNCTION, AND INVOLVEMENT IN CILD13.
RX PubMed=19944400; DOI=10.1016/j.ajhg.2009.10.018;
RA Loges N.T., Olbrich H., Becker-Heck A., Haffner K., Heer A., Reinhard C.,
RA Schmidts M., Kispert A., Zariwala M.A., Leigh M.W., Knowles M.R.,
RA Zentgraf H., Seithe H., Nurnberg G., Nurnberg P., Reinhardt R., Omran H.;
RT "Deletions and point mutations of LRRC50 cause primary ciliary dyskinesia
RT due to dynein arm defects.";
RL Am. J. Hum. Genet. 85:883-889(2009).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND VARIANTS CILD13 42-GLU--LYS-117 DEL AND
RP ARG-175.
RX PubMed=19944405; DOI=10.1016/j.ajhg.2009.11.008;
RA Duquesnoy P., Escudier E., Vincensini L., Freshour J., Bridoux A.M.,
RA Coste A., Deschildre A., de Blic J., Legendre M., Montantin G.,
RA Tenreiro H., Vojtek A.M., Loussert C., Clement A., Escalier D., Bastin P.,
RA Mitchell D.R., Amselem S.;
RT "Loss-of-function mutations in the human ortholog of Chlamydomonas
RT reinhardtii ODA7 disrupt dynein arm assembly and cause primary ciliary
RT dyskinesia.";
RL Am. J. Hum. Genet. 85:890-896(2009).
RN [8]
RP INVOLVEMENT IN CILD13.
RX PubMed=25186273; DOI=10.1183/09031936.00052014;
RA Raidt J., Wallmeier J., Hjeij R., Onnebrink J.G., Pennekamp P., Loges N.T.,
RA Olbrich H., Haeffner K., Dougherty G.W., Omran H., Werner C.;
RT "Ciliary beat pattern and frequency in genetic variants of primary ciliary
RT dyskinesia.";
RL Eur. Respir. J. 44:1579-1588(2014).
CC -!- FUNCTION: Cilium-specific protein required for the stability of the
CC ciliary architecture. Plays a role in cytoplasmic preassembly of dynein
CC arms. Involved in regulation of microtubule-based cilia and actin-based
CC brush border microvilli. {ECO:0000269|PubMed:18385425,
CC ECO:0000269|PubMed:19944400, ECO:0000269|PubMed:19944405}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:18385425}. Cytoplasm {ECO:0000269|PubMed:18385425}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18385425}.
CC Note=In HEK293T cells, it is diffusely cytoplasmic and concentrates at
CC the mitotic spindle poles, while in MDCK cells, it localizes in the
CC cilium. In vivo, this protein is probably restricted to the cilium.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NEP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEP3-2; Sequence=VSP_036354, VSP_036355;
CC Name=3;
CC IsoId=Q8NEP3-3; Sequence=VSP_036356;
CC -!- TISSUE SPECIFICITY: Mainly expressed in trachea and testis.
CC {ECO:0000269|PubMed:19944405}.
CC -!- DISEASE: Ciliary dyskinesia, primary, 13 (CILD13) [MIM:613193]: 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. At ultrastructural level, CILD13 is
CC characterized by a marked reduction or absence of both dynein arms from
CC the patients cilia. {ECO:0000269|PubMed:19944400,
CC ECO:0000269|PubMed:19944405, ECO:0000269|PubMed:25186273}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the DNAAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71645.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK057238; BAB71392.1; -; mRNA.
DR EMBL; AK058059; BAB71645.1; ALT_INIT; mRNA.
DR EMBL; AK295990; BAG58765.1; -; mRNA.
DR EMBL; AC009123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC040169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024009; AAH24009.3; -; mRNA.
DR EMBL; AL137334; CAH10706.1; -; mRNA.
DR EMBL; AL833328; CAH10390.1; -; mRNA.
DR EMBL; AL833336; CAH10394.1; -; mRNA.
DR CCDS; CCDS10943.2; -. [Q8NEP3-1]
DR RefSeq; NP_001305685.1; NM_001318756.1. [Q8NEP3-2]
DR RefSeq; NP_848547.4; NM_178452.5. [Q8NEP3-1]
DR AlphaFoldDB; Q8NEP3; -.
DR SMR; Q8NEP3; -.
DR BioGRID; 125839; 9.
DR IntAct; Q8NEP3; 6.
DR STRING; 9606.ENSP00000367815; -.
DR iPTMnet; Q8NEP3; -.
DR PhosphoSitePlus; Q8NEP3; -.
DR BioMuta; DNAAF1; -.
DR DMDM; 215274261; -.
DR MassIVE; Q8NEP3; -.
DR PaxDb; Q8NEP3; -.
DR PeptideAtlas; Q8NEP3; -.
DR PRIDE; Q8NEP3; -.
DR ProteomicsDB; 73190; -. [Q8NEP3-1]
DR ProteomicsDB; 73191; -. [Q8NEP3-2]
DR ProteomicsDB; 73192; -. [Q8NEP3-3]
DR Antibodypedia; 30549; 190 antibodies from 15 providers.
DR DNASU; 123872; -.
DR Ensembl; ENST00000378553.10; ENSP00000367815.5; ENSG00000154099.18. [Q8NEP3-1]
DR Ensembl; ENST00000563093.5; ENSP00000457373.1; ENSG00000154099.18. [Q8NEP3-3]
DR GeneID; 123872; -.
DR KEGG; hsa:123872; -.
DR MANE-Select; ENST00000378553.10; ENSP00000367815.5; NM_178452.6; NP_848547.4.
DR UCSC; uc002fhl.5; human. [Q8NEP3-1]
DR CTD; 123872; -.
DR DisGeNET; 123872; -.
DR GeneCards; DNAAF1; -.
DR GeneReviews; DNAAF1; -.
DR HGNC; HGNC:30539; DNAAF1.
DR HPA; ENSG00000154099; Group enriched (fallopian tube, testis).
DR MalaCards; DNAAF1; -.
DR MIM; 613190; gene.
DR MIM; 613193; phenotype.
DR neXtProt; NX_Q8NEP3; -.
DR OpenTargets; ENSG00000154099; -.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR PharmGKB; PA142671510; -.
DR VEuPathDB; HostDB:ENSG00000154099; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000158494; -.
DR HOGENOM; CLU_035292_0_0_1; -.
DR InParanoid; Q8NEP3; -.
DR OMA; IAHNHLE; -.
DR OrthoDB; 891307at2759; -.
DR PhylomeDB; Q8NEP3; -.
DR TreeFam; TF315818; -.
DR PathwayCommons; Q8NEP3; -.
DR SignaLink; Q8NEP3; -.
DR BioGRID-ORCS; 123872; 6 hits in 1063 CRISPR screens.
DR ChiTaRS; DNAAF1; human.
DR GeneWiki; LRRC50; -.
DR GenomeRNAi; 123872; -.
DR Pharos; Q8NEP3; Tbio.
DR PRO; PR:Q8NEP3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NEP3; protein.
DR Bgee; ENSG00000154099; Expressed in right uterine tube and 153 other tissues.
DR ExpressionAtlas; Q8NEP3; baseline and differential.
DR Genevisible; Q8NEP3; HS.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; NAS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IMP:UniProtKB.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IMP:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0003341; P:cilium movement; IMP:BHF-UCL.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:BHF-UCL.
DR GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:BHF-UCL.
DR GO; GO:0035469; P:determination of pancreatic left/right asymmetry; IMP:BHF-UCL.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IC:BHF-UCL.
DR GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
DR GO; GO:0036159; P:inner dynein arm assembly; IMP:BHF-UCL.
DR GO; GO:0060972; P:left/right pattern formation; IMP:BHF-UCL.
DR GO; GO:0030324; P:lung development; IMP:BHF-UCL.
DR GO; GO:0044458; P:motile cilium assembly; IMP:BHF-UCL.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:BHF-UCL.
DR GO; GO:0003356; P:regulation of cilium beat frequency; IMP:BHF-UCL.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR027734; DNAAF1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR45973:SF19; PTHR45973:SF19; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Ciliopathy; Cilium; Cytoplasm;
KW Cytoskeleton; Disease variant; Kartagener syndrome; Leucine-rich repeat;
KW Phosphoprotein; Primary ciliary dyskinesia; Reference proteome; Repeat.
FT CHAIN 1..725
FT /note="Dynein axonemal assembly factor 1"
FT /id="PRO_0000232889"
FT REPEAT 107..129
FT /note="LRR 1"
FT REPEAT 130..151
FT /note="LRR 2"
FT REPEAT 152..173
FT /note="LRR 3"
FT REPEAT 174..195
FT /note="LRR 4"
FT REPEAT 196..217
FT /note="LRR 5"
FT REPEAT 221..242
FT /note="LRR 6"
FT DOMAIN 256..294
FT /note="LRRCT"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYH9"
FT MOD_RES 559
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2H9"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2H9"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2H9"
FT VAR_SEQ 1..252
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036354"
FT VAR_SEQ 343
FT /note="R -> RGMRSAEDNSPRVPLRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036355"
FT VAR_SEQ 409..725
FT /note="GPEPEGTLPAETLLLSSPVEVKGEDGDGEPEGTLPAEAPPPPPPVEVKGEDG
FT DQEPEGTLPAETLLLSPPVKVKGEDGDREPEGTLPAEAPPPPPLGAAREEPTPQAVATE
FT GVFVTELDGTRTEDLETIRLETKETFCIDDLPDLEDDDETGKSLEDQNMCFPKIEVISS
FT LSDDSDPELDYTSLPVLENLPTDTLSNIFAVSKDTSKAARVPFTDIFKKEAKRDLEIRK
FT QDTKSPRPLIQELSDEDPSGQLLMPPTCQRDAAPLTSSGDRDSDFLAASSPVPTESAAT
FT PPETCVGVAQPSQALPTWDLTAFPAPKAS -> DPATVTACEG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036356"
FT VARIANT 42..117
FT /note="Missing (in CILD13)"
FT /evidence="ECO:0000269|PubMed:19944405"
FT /id="VAR_063097"
FT VARIANT 175
FT /note="L -> R (in CILD13; dbSNP:rs267607227)"
FT /evidence="ECO:0000269|PubMed:19944405"
FT /id="VAR_063098"
FT VARIANT 387
FT /note="D -> E (in dbSNP:rs36062234)"
FT /id="VAR_047662"
FT VARIANT 393
FT /note="K -> R (in dbSNP:rs17856705)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_047663"
FT VARIANT 432
FT /note="E -> D (in dbSNP:rs9972733)"
FT /id="VAR_047664"
FT VARIANT 502
FT /note="P -> L (in dbSNP:rs11644164)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_047665"
FT VARIANT 545
FT /note="F -> C (in dbSNP:rs17856706)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047666"
FT VARIANT 633
FT /note="L -> S (in dbSNP:rs2288020)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047667"
FT VARIANT 659
FT /note="L -> P (in dbSNP:rs2288022)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047668"
FT VARIANT 659
FT /note="L -> V (in dbSNP:rs2288021)"
FT /id="VAR_047669"
FT VARIANT 675
FT /note="S -> T (in dbSNP:rs2288023)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047670"
FT VARIANT 703
FT /note="G -> R (in dbSNP:rs4150188)"
FT /id="VAR_047671"
FT VARIANT 712
FT /note="P -> A (in dbSNP:rs4150187)"
FT /id="VAR_047672"
FT CONFLICT 307
FT /note="Q -> E (in Ref. 4; CAH10390)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="P -> L (in Ref. 4; CAH10394)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="G -> R (in Ref. 2; BAG58765)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="D -> G (in Ref. 4; CAH10394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 80026 MW; CFDBF86796FA61B0 CRC64;
MHPEPSEPAT GGAAELDCAQ EPGVEESAGD HGSAGRGGCK EEINDPKEIC VGSSDTSYHS
QQKQSGDNGS GGHFAHPRED REDRGPRMTK SSLQKLCKQH KLYITPALND TLYLHFKGFD
RIENLEEYTG LRCLWLQSNG IQKIENLEAQ TELRCLFLQM NLLRKIENLE PLQKLDALNL
SNNYIKTIEN LSCLPVLNTL QMAHNHLETV EDIQHLQECL RLCVLDLSHN KLSDPEILSI
LESMPDLRVL NLMGNPVIRQ IPNYRRTVTV RLKHLTYLDD RPVFPKDRAC AEAWARGGYA
AEKEERQQWE SRERKKITDS IEALAMIKQR AEERKRQRES QERGEMTSSD DGENVPASAE
GKEEPPGDRE TRQKMELFVK ESFEAKDELC PEKPSGEEPP VEAKREDGGP EPEGTLPAET
LLLSSPVEVK GEDGDGEPEG TLPAEAPPPP PPVEVKGEDG DQEPEGTLPA ETLLLSPPVK
VKGEDGDREP EGTLPAEAPP PPPLGAAREE PTPQAVATEG VFVTELDGTR TEDLETIRLE
TKETFCIDDL PDLEDDDETG KSLEDQNMCF PKIEVISSLS DDSDPELDYT SLPVLENLPT
DTLSNIFAVS KDTSKAARVP FTDIFKKEAK RDLEIRKQDT KSPRPLIQEL SDEDPSGQLL
MPPTCQRDAA PLTSSGDRDS DFLAASSPVP TESAATPPET CVGVAQPSQA LPTWDLTAFP
APKAS
