STAR9_HUMAN
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 03-AUG-2022, entry version 156.
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};
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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; 22.
DR IntAct; Q9P2P6; 13.
DR MINT; Q9P2P6; -.
DR STRING; 9606.ENSP00000290607; -.
DR CarbonylDB; Q9P2P6; -.
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; Q9P2P6; -.
DR PeptideAtlas; Q9P2P6; -.
DR PRIDE; Q9P2P6; -.
DR ProteomicsDB; 83876; -. [Q9P2P6-1]
DR ProteomicsDB; 83877; -. [Q9P2P6-2]
DR ProteomicsDB; 83878; -. [Q9P2P6-3]
DR Antibodypedia; 23703; 43 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 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; PLKRQQN; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; Q9P2P6; -.
DR TreeFam; TF332626; -.
DR PathwayCommons; Q9P2P6; -.
DR SignaLink; Q9P2P6; -.
DR BioGRID-ORCS; 57519; 9 hits in 1078 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 144 other tissues.
DR ExpressionAtlas; Q9P2P6; baseline and differential.
DR Genevisible; Q9P2P6; HS.
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; cd00060; FHA; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 3.40.850.10; -; 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; IPR042990; STARD9.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR47117; PTHR47117; 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; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50848; START; 1.
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
