ID DNAI1_HUMAN Reviewed; 699 AA. AC Q9UI46; B7Z7U1; Q5T8G7; Q8NHQ7; Q9UEZ8; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 183. DE RecName: Full=Dynein axonemal intermediate chain 1; DE AltName: Full=Axonemal dynein intermediate chain 1; GN Name=DNAI1; 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 [GENOMIC DNA / MRNA] (ISOFORM 1). RC TISSUE=Testis, and Trachea; RX PubMed=10577904; DOI=10.1086/302683; RA Pennarun G., Escudier E., Chapelin C., Bridoux A.-M., Cacheux V., Roger G., RA Clement A., Goossens M., Amselem S., Duriez B.; RT "Loss-of-function mutations in a human gene related to Chlamydomonas RT reinhardtii dynein IC78 result in primary ciliary dyskinesia."; RL Am. J. Hum. Genet. 65:1508-1519(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-8. 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-134, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Sperm; RX PubMed=12509440; DOI=10.1074/jbc.m202325200; RA Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F., Kalab P., RA Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F., Visconti P.E.; RT "Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine RT phosphorylation of a kinase-anchoring protein 3 and valosin-containing RT protein/p97 during capacitation."; RL J. Biol. Chem. 278:11579-11589(2003). RN [6] RP INTERACTION WITH BICD2. RX PubMed=23664119; DOI=10.1016/j.ajhg.2013.04.013; RA Peeters K., Litvinenko I., Asselbergh B., Almeida-Souza L., Chamova T., RA Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E., De Winter V., RA Ooms T., Timmerman V., Tournev I., Jordanova A.; RT "Molecular defects in the motor adaptor BICD2 cause proximal spinal RT muscular atrophy with autosomal-dominant inheritance."; RL Am. J. Hum. Genet. 92:955-964(2013). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=27120127; DOI=10.1002/humu.23005; RA Jeanson L., Thomas L., Copin B., Coste A., Sermet-Gaudelus I., RA Dastot-Le Moal F., Duquesnoy P., Montantin G., Collot N., Tissier S., RA Papon J.F., Clement A., Louis B., Escudier E., Amselem S., Legendre M.; RT "Mutations in GAS8, a gene encoding a nexin-dynein regulatory complex RT subunit, cause primary ciliary dyskinesia with axonemal disorganization."; RL Hum. Mutat. 37:776-785(2016). RN [8] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=33263282; DOI=10.7554/elife.58662; RA Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L., RA Marcotte E.M., Wallingford J.B.; RT "Functional partitioning of a liquid-like organelle during assembly of RT axonemal dyneins."; RL Elife 9:0-0(2020). RN [9] RP INTERACTION WITH CFAP45 AND CFAP52. RX PubMed=33139725; DOI=10.1038/s41467-020-19113-0; RA Dougherty G.W., Mizuno K., Noethe-Menchen T., Ikawa Y., Boldt K., RA Ta-Shma A., Aprea I., Minegishi K., Pang Y.P., Pennekamp P., Loges N.T., RA Raidt J., Hjeij R., Wallmeier J., Mussaffi H., Perles Z., Elpeleg O., RA Rabert F., Shiratori H., Letteboer S.J., Horn N., Young S., Struenker T., RA Stumme F., Werner C., Olbrich H., Takaoka K., Ide T., Twan W.K., RA Biebach L., Grosse-Onnebrink J., Klinkenbusch J.A., Praveen K., RA Bracht D.C., Hoeben I.M., Junger K., Guetzlaff J., Cindric S., Aviram M., RA Kaiser T., Memari Y., Dzeja P.P., Dworniczak B., Ueffing M., Roepman R., RA Bartscherer K., Katsanis N., Davis E.E., Amirav I., Hamada H., Omran H.; RT "CFAP45 deficiency causes situs abnormalities and asthenospermia by RT disrupting an axonemal adenine nucleotide homeostasis module."; RL Nat. Commun. 11:5520-5520(2020). RN [10] RP VARIANT SER-8, AND VARIANT KTGS SER-515. RX PubMed=11231901; DOI=10.1086/319511; RA Guichard C., Harricane M.-C., Lafitte J.-J., Godard P., Zaegel M., Tack V., RA Lalau G., Bouvagnet P.; RT "Axonemal dynein intermediate-chain gene (DNAI1) mutations result in situs RT inversus and primary ciliary dyskinesia (Kartagener syndrome)."; RL Am. J. Hum. Genet. 68:1030-1035(2001). RN [11] RP INVOLVEMENT IN CILD1. 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: Part of the dynein complex of respiratory cilia. CC -!- SUBUNIT: Consists of at least two heavy chains and a number of CC intermediate and light chains. Interacts with BICD2 (PubMed:23664119). CC Interacts with CFAP45 and CFAP52 (PubMed:33139725). CC {ECO:0000269|PubMed:23664119, ECO:0000269|PubMed:33139725}. CC -!- SUBCELLULAR LOCATION: Dynein axonemal particle CC {ECO:0000269|PubMed:33263282}. Cytoplasm, cytoskeleton, cilium axoneme CC {ECO:0000269|PubMed:27120127}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UI46-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UI46-2; Sequence=VSP_056963, VSP_056964; CC -!- TISSUE SPECIFICITY: Expressed in respiratory ciliated cells (at protein CC level). {ECO:0000269|PubMed:33263282}. CC -!- DISEASE: Ciliary dyskinesia, primary, 1 (CILD1) [MIM:244400]: 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:25186273}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Kartagener syndrome (KTGS) [MIM:244400]: An autosomal CC recessive disorder characterized by the association of primary ciliary CC dyskinesia with situs inversus. Clinical features include recurrent CC respiratory infections, bronchiectasis, infertility, and lateral CC transposition of the viscera of the thorax and abdomen. The situs CC inversus is most often total, although it can be partial in some cases CC (isolated dextrocardia or isolated transposition of abdominal viscera). CC {ECO:0000269|PubMed:11231901}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the dynein intermediate chain family. CC {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; AF091619; AAF18570.1; -; mRNA. DR EMBL; AF190496; AAF19816.1; -; Genomic_DNA. DR EMBL; AF190477; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190478; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190479; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190480; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190481; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190482; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190483; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190484; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190485; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190486; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190487; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190488; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190489; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190490; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190491; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190492; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190493; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190494; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AF190495; AAF19816.1; JOINED; Genomic_DNA. DR EMBL; AK302499; BAH13727.1; -; mRNA. DR EMBL; AL160270; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC030583; AAH30583.1; -; mRNA. DR CCDS; CCDS6557.1; -. [Q9UI46-1] DR RefSeq; NP_001268357.1; NM_001281428.1. DR RefSeq; NP_036276.1; NM_012144.3. [Q9UI46-1] DR PDB; 8J07; EM; 4.10 A; m1/o1/q1/s1=1-699. DR PDBsum; 8J07; -. DR AlphaFoldDB; Q9UI46; -. DR EMDB; EMD-35888; -. DR SMR; Q9UI46; -. DR BioGRID; 117957; 9. DR STRING; 9606.ENSP00000480538; -. DR iPTMnet; Q9UI46; -. DR PhosphoSitePlus; Q9UI46; -. DR BioMuta; DNAI1; -. DR DMDM; 12643888; -. DR MassIVE; Q9UI46; -. DR PaxDb; 9606-ENSP00000480538; -. DR PeptideAtlas; Q9UI46; -. DR ProteomicsDB; 6899; -. DR ProteomicsDB; 84474; -. [Q9UI46-1] DR Antibodypedia; 11255; 255 antibodies from 34 providers. DR DNASU; 27019; -. DR Ensembl; ENST00000242317.9; ENSP00000242317.4; ENSG00000122735.16. [Q9UI46-1] DR GeneID; 27019; -. DR KEGG; hsa:27019; -. DR MANE-Select; ENST00000242317.9; ENSP00000242317.4; NM_012144.4; NP_036276.1. DR UCSC; uc003zum.5; human. [Q9UI46-1] DR AGR; HGNC:2954; -. DR CTD; 27019; -. DR DisGeNET; 27019; -. DR GeneCards; DNAI1; -. DR GeneReviews; DNAI1; -. DR HGNC; HGNC:2954; DNAI1. DR HPA; ENSG00000122735; Group enriched (choroid plexus, fallopian tube, testis). DR MalaCards; DNAI1; -. DR MIM; 244400; phenotype. DR MIM; 604366; gene. DR neXtProt; NX_Q9UI46; -. DR OpenTargets; ENSG00000122735; -. DR Orphanet; 244; Primary ciliary dyskinesia. DR PharmGKB; PA27407; -. DR VEuPathDB; HostDB:ENSG00000122735; -. DR eggNOG; KOG1587; Eukaryota. DR GeneTree; ENSGT00940000156436; -. DR HOGENOM; CLU_015820_2_0_1; -. DR InParanoid; Q9UI46; -. DR OMA; FNYCERA; -. DR OrthoDB; 3088529at2759; -. DR PhylomeDB; Q9UI46; -. DR TreeFam; TF300553; -. DR PathwayCommons; Q9UI46; -. DR SignaLink; Q9UI46; -. DR SIGNOR; Q9UI46; -. DR BioGRID-ORCS; 27019; 10 hits in 1145 CRISPR screens. DR ChiTaRS; DNAI1; human. DR GeneWiki; DNAI1; -. DR GenomeRNAi; 27019; -. DR Pharos; Q9UI46; Tbio. DR PRO; PR:Q9UI46; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9UI46; Protein. DR Bgee; ENSG00000122735; Expressed in right uterine tube and 114 other cell types or tissues. DR ExpressionAtlas; Q9UI46; baseline and differential. DR GO; GO:0097729; C:9+2 motile cilium; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IEA:Ensembl. DR GO; GO:0005929; C:cilium; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0120293; C:dynein axonemal particle; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:GOC. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0036157; C:outer dynein arm; IMP:SYSCILIA_CCNET. DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:ProtInc. DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central. DR GO; GO:0045503; F:dynein light chain binding; IBA:GO_Central. DR GO; GO:0003341; P:cilium movement; IMP:SYSCILIA_CCNET. DR GO; GO:0007368; P:determination of left/right symmetry; IMP:SYSCILIA_CCNET. DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IEA:Ensembl. DR GO; GO:0030317; P:flagellated sperm motility; IMP:SYSCILIA_CCNET. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0036158; P:outer dynein arm assembly; IMP:SYSCILIA_CCNET. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR12442:SF11; DYNEIN AXONEMAL INTERMEDIATE CHAIN 1; 1. DR PANTHER; PTHR12442; DYNEIN INTERMEDIATE CHAIN; 1. DR Pfam; PF00400; WD40; 2. DR SMART; SM00320; WD40; 4. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q9UI46; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; Cilium; KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant; KW Dynein; Kartagener syndrome; Microtubule; Motor protein; Phosphoprotein; KW Primary ciliary dyskinesia; Reference proteome; Repeat; WD repeat. FT CHAIN 1..699 FT /note="Dynein axonemal intermediate chain 1" FT /id="PRO_0000114658" FT REPEAT 320..370 FT /note="WD 1" FT REPEAT 375..413 FT /note="WD 2" FT REPEAT 422..465 FT /note="WD 3" FT REPEAT 474..526 FT /note="WD 4" FT REPEAT 531..570 FT /note="WD 5" FT REPEAT 574..612 FT /note="WD 6" FT REPEAT 618..658 FT /note="WD 7" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 140..170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 131 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:12509440" FT MOD_RES 134 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:12509440" FT VAR_SEQ 88..168 FT /note="EGTYKPIGFVNQLAVHYTQVGNLIPKDSDEGRRQHYRDELVAGSQESVKVIS FT ETGNLEEDEEPKELETEPGSQTDVPAAGA -> KQWSLGFIPKLKRKIPVNYWGQDEGE FT ISNETVRVIYSLGIFIMKIVTILLNINIEHLLCVRHCVNRLFLLFLILIIIMQIR (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056963" FT VAR_SEQ 169..699 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056964" FT VARIANT 8 FT /note="A -> S (in dbSNP:rs11547035)" FT /evidence="ECO:0000269|PubMed:11231901, FT ECO:0000269|PubMed:15489334" FT /id="VAR_016774" FT VARIANT 60 FT /note="A -> V (in dbSNP:rs16931549)" FT /id="VAR_033876" FT VARIANT 326 FT /note="Q -> H (in dbSNP:rs16931555)" FT /id="VAR_033877" FT VARIANT 335 FT /note="V -> I (in dbSNP:rs11793196)" FT /id="VAR_033878" FT VARIANT 487 FT /note="V -> G (in dbSNP:rs11999454)" FT /id="VAR_033879" FT VARIANT 515 FT /note="G -> S (in KTGS; dbSNP:rs79833450)" FT /evidence="ECO:0000269|PubMed:11231901" FT /id="VAR_016775" FT CONFLICT 202 FT /note="Y -> C (in Ref. 4; AAH30583)" FT /evidence="ECO:0000305" FT CONFLICT 495 FT /note="P -> Q (in Ref. 4; AAH30583)" FT /evidence="ECO:0000305" SQ SEQUENCE 699 AA; 79283 MW; F7E2CF9D09A1F8BD CRC64; MIPASAKAPH KQPHKQSISI GRGTRKRDED SGTEVGEGTD EWAQSKATVR PPDQLELTDA ELKEEFTRIL TANNPHAPQN IVRYSFKEGT YKPIGFVNQL AVHYTQVGNL IPKDSDEGRR QHYRDELVAG SQESVKVISE TGNLEEDEEP KELETEPGSQ TDVPAAGAAE KVTEEELMTP KQPKERKLTN QFNFSERASQ TYNNPVRDRE CQTEPPPRTN FSATANQWEI YDAYVEELEK QEKTKEKEKA KTPVAKKSGK MAMRKLTSME SQTDDLIKLS QAAKIMERMV NQNTYDDIAQ DFKYYDDAAD EYRDQVGTLL PLWKFQNDKA KRLSVTALCW NPKYRDLFAV GYGSYDFMKQ SRGMLLLYSL KNPSFPEYMF SSNSGVMCLD IHVDHPYLVA VGHYDGNVAI YNLKKPHSQP SFCSSAKSGK HSDPVWQVKW QKDDMDQNLN FFSVSSDGRI VSWTLVKRKL VHIDVIKLKV EGSTTEVPEG LQLHPVGCGT AFDFHKEIDY MFLVGTEEGK IYKCSKSYSS QFLDTYDAHN MSVDTVSWNP YHTKVFMSCS SDWTVKIWDH TIKTPMFIYD LNSAVGDVAW APYSSTVFAA VTTDGKAHIF DLAINKYEAI CNQPVAAKKN RLTHVQFNLI HPIIIVGDDR GHIISLKLSP NLRKMPKEKK GQEVQKGPAV EIAKLDKLLN LVREVKIKT //