ID STAR9_HUMAN Reviewed; 4700 AA. AC Q9P2P6; Q68DG2; Q6AI01; Q6ZWK0; Q9UF70; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 22-FEB-2012, sequence version 3. DT 27-MAR-2024, entry version 164. DE RecName: Full=StAR-related lipid transfer protein 9; DE AltName: Full=START domain-containing protein 9; DE Short=StARD9; GN Name=STARD9; Synonyms=KIAA1300; 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=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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1975-4700 (ISOFORM 1). RC TISSUE=Cervix, Fetal kidney, and 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2881-4700 (ISOFORM 1), AND RP VARIANT ASP-3383. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [5] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX PubMed=16964419; RA Halama N., Grauling-Halama S.A., Jager D.; RT "Identification and characterization of the human StARD9 gene in the RT LGMD2A-region on chromosome 15q15 by in silico methods."; RL Int. J. Mol. Med. 18:653-656(2006). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-110 AND ARG-223. RX PubMed=22153075; DOI=10.1016/j.cell.2011.11.020; RA Torres J.Z., Summers M.K., Peterson D., Brauer M.J., Lee J., Senese S., RA Gholkar A.A., Lo Y.C., Lei X., Jung K., Anderson D.C., Davis D.P., RA Belmont L., Jackson P.K.; RT "The STARD9/Kif16a kinesin associates with mitotic microtubules and RT regulates spindle pole assembly."; RL Cell 147:1309-1323(2011). RN [7] RP INTERACTION WITH ATAD3A. 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: Microtubule-dependent motor protein required for spindle pole CC assembly during mitosis. Required to stabilize the pericentriolar CC material (PCM). {ECO:0000269|PubMed:22153075}. CC -!- SUBUNIT: Interacts with ATAD3A. {ECO:0000269|PubMed:22453275}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome, centriole {ECO:0000269|PubMed:22153075}. Nucleus CC {ECO:0000269|PubMed:22153075}. Note=Localizes throughout the cytoplasm CC and nucleus during interphase. Localizes to the daughter centriole CC during mitosis. Disappears in cytokinesis. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9P2P6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P2P6-2; Sequence=VSP_029574, VSP_029575; CC Name=3; CC IsoId=Q9P2P6-3; Sequence=VSP_029573, VSP_029576, VSP_029577; CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system, muscle CC cells (heart and skeletal muscle), pancreas, prostate and lung. CC {ECO:0000269|PubMed:16964419}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}. CC -!- SEQUENCE CAUTION: CC Sequence=CAH18258.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAH18258.1; Type=Erroneous termination; Note=Truncated C-terminus.; 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; AK122666; BAC85502.1; -; mRNA. DR EMBL; AL133579; CAB63725.1; -; mRNA. DR EMBL; CR627426; CAH10513.1; -; mRNA. DR EMBL; CR749416; CAH18258.1; ALT_SEQ; mRNA. DR EMBL; AC018362; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090510; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB037721; BAA92538.1; -; mRNA. DR CCDS; CCDS53935.1; -. [Q9P2P6-1] DR PIR; T43486; T43486. DR RefSeq; NP_065810.2; NM_020759.2. [Q9P2P6-1] DR SMR; Q9P2P6; -. DR BioGRID; 121580; 30. DR IntAct; Q9P2P6; 17. DR MINT; Q9P2P6; -. DR STRING; 9606.ENSP00000290607; -. DR CarbonylDB; Q9P2P6; -. DR GlyGen; Q9P2P6; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9P2P6; -. DR PhosphoSitePlus; Q9P2P6; -. DR BioMuta; STARD9; -. DR DMDM; 378405232; -. DR EPD; Q9P2P6; -. DR jPOST; Q9P2P6; -. DR MassIVE; Q9P2P6; -. DR MaxQB; Q9P2P6; -. DR PaxDb; 9606-ENSP00000290607; -. DR PeptideAtlas; Q9P2P6; -. DR ProteomicsDB; 83876; -. [Q9P2P6-1] DR ProteomicsDB; 83877; -. [Q9P2P6-2] DR ProteomicsDB; 83878; -. [Q9P2P6-3] DR Antibodypedia; 23703; 44 antibodies from 12 providers. DR Ensembl; ENST00000290607.12; ENSP00000290607.7; ENSG00000159433.12. [Q9P2P6-1] DR GeneID; 57519; -. DR KEGG; hsa:57519; -. DR MANE-Select; ENST00000290607.12; ENSP00000290607.7; NM_020759.3; NP_065810.2. DR UCSC; uc010udj.3; human. [Q9P2P6-1] DR AGR; HGNC:19162; -. DR CTD; 57519; -. DR DisGeNET; 57519; -. DR GeneCards; STARD9; -. DR HGNC; HGNC:19162; STARD9. DR HPA; ENSG00000159433; Low tissue specificity. DR MIM; 614642; gene. DR neXtProt; NX_Q9P2P6; -. DR OpenTargets; ENSG00000159433; -. DR VEuPathDB; HostDB:ENSG00000159433; -. DR eggNOG; KOG0245; Eukaryota. DR GeneTree; ENSGT00940000164290; -. DR HOGENOM; CLU_223684_0_0_1; -. DR InParanoid; Q9P2P6; -. DR OMA; QPHCELQ; -. DR OrthoDB; 126886at2759; -. DR PhylomeDB; Q9P2P6; -. DR TreeFam; TF332626; -. DR PathwayCommons; Q9P2P6; -. DR SignaLink; Q9P2P6; -. DR BioGRID-ORCS; 57519; 9 hits in 1156 CRISPR screens. DR ChiTaRS; STARD9; human. DR GenomeRNAi; 57519; -. DR Pharos; Q9P2P6; Tbio. DR PRO; PR:Q9P2P6; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q9P2P6; Protein. DR Bgee; ENSG00000159433; Expressed in sural nerve and 146 other cell types or tissues. DR ExpressionAtlas; Q9P2P6; baseline and differential. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008289; F:lipid binding; IEA:InterPro. DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB. DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro. DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB. DR CDD; cd22731; FHA_KIF16A_STARD9; 1. DR CDD; cd01365; KISc_KIF1A_KIF1B; 1. DR CDD; cd08874; START_STARD9-like; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 3.30.530.20; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR019821; Kinesin_motor_CS. DR InterPro; IPR001752; Kinesin_motor_dom. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR InterPro; IPR023393; START-like_dom_sf. DR InterPro; IPR002913; START_lipid-bd_dom. DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1. DR PANTHER; PTHR47117:SF1; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1. DR Pfam; PF00498; FHA; 1. DR Pfam; PF00225; Kinesin; 1. DR Pfam; PF01852; START; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00240; FHA; 1. DR SMART; SM00129; KISc; 1. DR SUPFAM; SSF55961; Bet v1-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR PROSITE; PS50848; START; 1. DR Genevisible; Q9P2P6; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; KW Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..4700 FT /note="StAR-related lipid transfer protein 9" FT /id="PRO_0000220678" FT DOMAIN 3..384 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT DOMAIN 498..569 FT /note="FHA" FT DOMAIN 4483..4700 FT /note="START" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197" FT REGION 310..331 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 631..652 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 851..880 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1057..1104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1128..1188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1939..1976 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2014..2043 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2088..2179 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2254..2290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2377..2403 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2416..2444 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2479..2539 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2589..2613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2642..2678 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2696..2731 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2765..2789 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2821..2852 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2892..2955 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3124..3144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3199..3241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3274..3412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3564..3611 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3766..3790 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3830..3884 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3906..3991 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4033..4086 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4153..4193 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4397..4419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 4334..4387 FT /evidence="ECO:0000255" FT COMPBIAS 310..329 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1057..1080 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1089..1103 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1162..1188 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2016..2032 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2106..2121 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2153..2179 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2255..2269 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2383..2397 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2490..2514 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2594..2610 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2765..2782 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2934..2955 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3205..3219 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3303..3355 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3369..3384 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3385..3399 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3830..3870 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3906..3926 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3947..3991 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4047..4079 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4169..4186 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 103..110 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT MOD_RES 1203 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80TF6" FT VAR_SEQ 1..84 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029573" FT VAR_SEQ 290..292 FT /note="AQN -> GIF (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_029574" FT VAR_SEQ 293..4700 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_029575" FT VAR_SEQ 360..435 FT /note="TVSPAHTSYSETMSTLRYASSAKNIINKPRVNEDANLKLIRELREEIERLKA FT LLLSFELRNFSSLSDENLKELVLQ -> SEWDARAGPVLGLVLYLRERAMAPVSGMPEL FT DLCWDWYSISEKGPWPQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029576" FT VAR_SEQ 436..4700 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029577" FT VARIANT 835 FT /note="R -> C (in dbSNP:rs12594837)" FT /id="VAR_059811" FT VARIANT 1172 FT /note="R -> C (in dbSNP:rs12594837)" FT /id="VAR_037257" FT VARIANT 1720 FT /note="P -> L (in dbSNP:rs7161810)" FT /id="VAR_037258" FT VARIANT 2205 FT /note="A -> V (in dbSNP:rs16957055)" FT /id="VAR_037259" FT VARIANT 2677 FT /note="R -> H (in dbSNP:rs8030587)" FT /id="VAR_037260" FT VARIANT 2855 FT /note="T -> I (in dbSNP:rs8031218)" FT /id="VAR_037261" FT VARIANT 2869 FT /note="P -> S (in dbSNP:rs11857283)" FT /id="VAR_037262" FT VARIANT 3015 FT /note="R -> G (in dbSNP:rs3742995)" FT /id="VAR_037263" FT VARIANT 3383 FT /note="N -> D (in dbSNP:rs3742993)" FT /evidence="ECO:0000269|PubMed:10718198" FT /id="VAR_037264" FT VARIANT 3469 FT /note="Y -> C (in dbSNP:rs16957061)" FT /id="VAR_037266" FT MUTAGEN 110 FT /note="T->N: Reduced ATPase activity." FT /evidence="ECO:0000269|PubMed:22153075" FT MUTAGEN 223 FT /note="R->A: Reduced ability to bind microtubules." FT /evidence="ECO:0000269|PubMed:22153075" FT CONFLICT 2602 FT /note="S -> L (in Ref. 2; CAH18258)" FT /evidence="ECO:0000305" FT CONFLICT 2818 FT /note="T -> I (in Ref. 2; CAH18258)" FT /evidence="ECO:0000305" FT CONFLICT 3633 FT /note="T -> A (in Ref. 2; CAH18258)" FT /evidence="ECO:0000305" FT CONFLICT 4433..4438 FT /note="LPDSRD -> IPGIRQ (in Ref. 2; CAB63725)" FT /evidence="ECO:0000305" FT CONFLICT 4639 FT /note="R -> H (in Ref. 4; BAA92538)" FT /evidence="ECO:0000305" SQ SEQUENCE 4700 AA; 516343 MW; D422BEE9E5612036 CRC64; MANVQVAVRV RPLSKRETKE GGRIIVEVDG KVAKIRNLKV DNRPDGFGDS REKVMAFGFD YCYWSVNPED PQYASQDVVF QDLGMEVLSG VAKGYNICLF AYGQTGSGKT YTMLGTPASV GLTPRICEGL FVREKDCASL PSSCRIKVSF LEIYNERVRD LLKQSGQKKS YTLRVREHPE MGPYVQGLSQ HVVTNYKQVI QLLEEGIANR ITAATHVHEA SSRSHAIFTI HYTQAILENN LPSEMASKIN LVDLAGSERA DPSYCKDRIA EGANINKSLV TLGIVISTLA QNSQVFSSCQ SLNSSVSNGG DSGILSSPSG TSSGGAPSRR QSYIPYRDSV LTWLLKDSLG GNSKTIMVAT VSPAHTSYSE TMSTLRYASS AKNIINKPRV NEDANLKLIR ELREEIERLK ALLLSFELRN FSSLSDENLK ELVLQNELKI DQLTKDWTQK WNDWQALMEH YSVDINRRRA GVVIDSSLPH LMALEDDVLS TGVVLYHLKE GTTKIGRIDS DQEQDIVLQG QWIERDHCTI TSACGVVVLR PARGARCTVN GREVTASCRL TQGAVITLGK AQKFRFNHPA EAAVLRQRRQ VGEAAAGRGS LEWLDLDGDL AASRLGLSPL LWKERRALEE QCDEDHQTPR DGETSHRAQI QQQQSYVEDL RHQILAEEIR AAKELEFDQA WISQQIKENQ QCLLREETWL ASLQQQQQED QVAEKELEAS VALDAWLQTD PEIQPSPFVQ SQKRVVHLQL LRRHTLRAAE RNVRRKKVSF QLERIIKKQR LLEAQKRLEK LTTLCWLQDD STQEPPYQVL SPDATVPRPP CRSKLTSCSS LSPQRLCSKH MPQLHSIFLS WDPSTTLPPR PDPTHQTSEK TSSEEHLPQA ASYPARTGCL RKNGLHSSGH GQPCTARAAL ARKGASAPDA CLTMSPNSVG IQEMEMGVKQ PHQMVSQGLA SLRKSANKLK PRHEPKIFTS TTQTRGAKGL ADPSHTQAGW RKEGNLGTHK AAKGASCNSL YPHGPRQTAG HGKAVKTFWT EYKPPSPSRA SKRHQRVLAT RVRNITKKSS HLPLGSPLKR QQNTRDPDTM VPLTDFSPVM DHSREKDNDL SDTDSNYSLD SLSCVYAKAL IEPLKPEERK WDFPEPENSE SDDSQLSEDS LAEKRYQSPK NRLGGNRPTN NRGQPRTRTR ASVRGFTAAS DSDLLAQTHR SFSLDSLIDA EEELGEDQQE EPFPGSADEI PTETFWHLED SSLPVMDQEA ICRLGPINYR TAARLDAVLP MSSSFYLDPQ FQPHCELQPH CELQPHCELQ PHCEQAESQV EPSYSEQADS LQGMQLSRES PLMSMDSWFS CDSKINPSSP PGIVGSLCPS PDMQEFHSCK GERPGYWPNT EELKPSDAET VLPYSSKLHQ GSTELLCSAR DEHTASAADT SRLSLWGIQR LIQPGADGTF QGRCIPDMTQ QGSSEASHNS SVSNVLAASA TTLTHVGSTH ERDWSALQQK YLLELSCPVL EAIGAPKPAY PYLEEDSGSL AQASSKGGDT LLPVGPRVSS NLNLNNFPVH LSRIRRLRAE KEQDSLNAKL EGVSDFFSTS EKEASYDETY SADLESLSAS RSTNAQVFAT ENAIPDSMTE ACEVKQNNLE ECLQSCRKPG LMTSSDEDFF QKNACHSNVT TATKADHWSQ GWAPLRKNSA VQPGQLSPDS HYPLEEEKTD CQESSKEAVR RHINVSFALP SGPELYLHSA PWNPLSSSLQ PPLLETFYVT KSRDALTETA LEIPACREVR VPSPPPREAW GFGHNHQALQ GAYLKNNLPV LLQNQNSKIA SSQQVTAEIP VDLNTREVIR ESGKCPGNIT EESHDSVYSS VTQNRHFLPS TSTKVCEFEN QVVILNKKHS FPALEGGEVT AQSCCGASSD STESGKSLLF RESEAREEEE LDQNTVLRQT INVSLEKDMP GESAVSLKSR SVDRRVSSPV MVAQGGGPTP KWEGKNETGL LEKGLRPKDS SEEFKLPGTK PAYERFQLVA CPQERNPSEC KSQEMLNPNR EPSGKKQNKR VNNTDEMARL IRSVMQLENG ILEIESKQNK QVHASHTPGT DKELVFQDQK EQEKTDHAFR PDSSGNPLPS KDQPSSPRQT DDTVFRDSEA GAMEVNSIGN HPQVQKITPN PFRSREGVRE SEPVREHTHP AGSDRPARDI CDSLGKHTTC REFTNTSLHP QRMKALARAL PLQPRLERSS KNNGQFVKAS ASLKGQPWGL GSLEELETVK GFQESQVAEH VSSSNQEEPK AQGKVEEMPM QRGGSLQEEN KVTQKFPSLS QLCRDTFFRQ ETVSPLLSRT EFCTAPLHQD LSNTLPLNSP RWPRRCLHVP VALGISSLDC VLDLTMLKIH NSPLVTGVEH QDQSTETRSH SPEGNVRGRS SEAHTAWCGS VRSMAMGSHS QSGVPESIPL GTEDRISAST SPQDHGKDLR ITLLGFSTSE DFASEAEVAV QKEIRVSSLN KVSSQPEKRV SFSLEEDSDQ ASKPRQKAEK ETEDVGLTSG VSLAPVSLPR VPSPEPRLLE PSDHASMCLA ILEEIRQAKA QRKQLHDFVA RGTVLSYCET LLEPECSSRV AGRPQCKQID QSSSDQTRNE GEAPGFHVAS LSAEAGQIDL LPDERKVQAT SLSADSFESL PNTETDREPW DPVQAFSHAA PAQDRKRRTG ELRQFAGASE PFICHSSSSE IIEKKKDATR TPSSADPLAP DSPRSSAPVE EVRRVVSKKV VAALPSQAPY DDPRVTLHEL SQSVPQETAE GIPPGSQDSS PEHQEPRTLD TTYGEVSDNL LVTAQGEKTA HFESQSVTCD VQNSTSASGP KQDHVQCPEA STGFEEGRAS PKQDTILPGA LTRVALEAPT QQCVQCKESV GSGLTEVCRA GSKHSRPIPL PDQRPSANPG GIGEEAPCRH PREALDGPVF SRNPEGSRTL SPSRGKESRT LPCRQPCSSQ PVATHAYSSH SSTLLCFRDG DLGKEPFKAA PHTIHPPCVV PSRAYEMDET GEISRGPDVH LTHGLEPKDV NREFRLTESS TCEPSTVAAV LSRAQGCRSP SAPDVRTGSF SHSATDGSVG LIGVPEKKVA EKQASTELEA ASFPAGMYSE PLRQFRDSSV GDQNAQVCQT NPEPPATTQG PHTLDLSEGS AESKLVVEPQ HECLENTTRC FLEKPQFSTE LRDHNRLDSQ AKFVARLKHT CSPQEDSPWQ EEEQHRDQAS GGGEGFAQGV NPLPDEDGLD GCQILDAGRE EVAVAKPPVS KILSQGFKDP ATVSLRQNET PQPAAQRSGH LYTGREQPAP NHRGSLPVTT IFSGPKHSRS SPTPQFSVVG SSRSLQELNL SVEPPSPTDE DTQGPNRLWN PHLRGYSSGK SVARTSLQAE DSNQKASSRL DDGTTDHRHL KPATPPYPMP STLSHMPTPD FTTSWMSGTL EQAQQGKREK LGVQVRPENW CSQMDKGMLH FGSSDISPYA LPWRPEEPAR ISWKQYMSGS AVDVSCSQKP QGLTLSNVAR CSSMDNGLED QNSPFHSHLS TYANICDLST THSSTENAQG SNEAWEVFRG SSSIALGDPH IPTSPEGVAP TSGHDRRPQF RGPSGEADCL RSKPPLAKGS AAGPVDEIML LYPSEAGCPV GQTRTNTFEQ GTQTLGSRRH WSSTDISFAQ PEASAVSAFD LASWTSMHNL SLHLSQLLHS TSELLGSLSQ PDVARREQNT KRDIPDKAPQ ALMMDGSTQT TVDEGSQTDL TLPTLCLQTS EAEPQGANVI LEGLGSDTST VSQEEGDVPG VPQKREAEET AQKMAQLLYL QEESTPYKPQ SPSIPSSHLR FQKAPVGQHL PSVSPSVSDA FLPPSSQPEE SYCLVVSSPS PSSPHSPGLF PSTSEYPGDS RVQKKLGPTS ALFVDRASSP ILTLSASTQE PGLSPGSLTL SAPSTHPVEG HQKLDSSPDP VDAPRTPMDN YSQTTDELGG SQRGRSSLQR SNGRSFLELH SPHSPQQSPK LQFSFLGQHP QQLQPRTTIG VQSRLLPPPL RHRSQRLGNS FVPEKVASPE HCPLSGREPS QWQSRTENGG ESSASPGEPQ RTLDRPSSWG GLQHLSPCPV SELTDTAGLR GSALGLPQAC QPEELLCFSC QMCMAPEHQH HSLRDLPVHN KFSNWCGVQK GSPGGLDMTE EELGASGDLS SEKQEQSPPQ PPNDHSQDSE WSKREQIPLQ VGAQNLSLSV ELTEAKLHHG FGEADALLQV LQSGTGEALA ADEPVTSTWK ELYARQKKAI ETLRRERAER LGNFCRTRSL SPQKQLSLLP NKDLFIWDLD LPSRRREYLQ QLRKDVVETT RSPESVSRSA HTPSDIELML QDYQQAHEEA KVEIARARDQ LRERTEQEKL RIHQKIISQL LKEEDKLHTL ANSSSLCTSS NGSLSSGMTS GYNSSPALSG QLQFPENMGH TNLPDSRDVW IGDERGGHSA VRKNSAYSHR ASLGSCCCSP SSLSSLGTCF SSSYQDLAKH VVDTSMADVM AACSDNLHNL FSCQATAGWN YQGEEQAVQL YYKVFSPTRH GFLGAGVVSQ PLSRVWAAVS DPTVWPLYYK PIQTARLHQR VTNSISLVYL VCNTTLCALK QPRDFCCVCV EAKEGHLSVM AAQSVYDTSM PRPSRKMVRG EILPSAWILQ PITVEGKEVT RVIYLAQVEL GAPGFPPQLL SSFIKRQPLV IARLASFLGR //