STAR9_MOUSE
ID STAR9_MOUSE Reviewed; 4561 AA.
AC Q80TF6; O35058; Q8C121; Q8CFL0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=StAR-related lipid transfer protein 9;
DE AltName: Full=Kinesin-like protein Kif16a;
DE AltName: Full=START domain-containing protein 9;
DE Short=StARD9;
GN Name=Stard9; Synonyms=Kiaa1300, Kif16a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-258.
RC STRAIN=ICR;
RX PubMed=9275178; DOI=10.1073/pnas.94.18.9654;
RA Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y.,
RA Hirokawa N.;
RT "Identification and classification of 16 new kinesin superfamily (KIF)
RT proteins in mouse genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3094-4561.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3922-4561.
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4191-4561.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Microtubule-dependent motor protein required for spindle pole
CC assembly during mitosis. Required to stabilize the pericentriolar
CC material (PCM) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ATAD3A. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Localizes throughout the cytoplasm and nucleus during interphase.
CC Localizes to the daughter centriole during mitosis. Disappears in
CC cytokinesis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AL772299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB001425; BAA22385.1; -; mRNA.
DR EMBL; AK122489; BAC65771.1; -; mRNA.
DR EMBL; AK029170; BAC26335.1; -; mRNA.
DR EMBL; BC032885; AAH32885.1; -; mRNA.
DR SMR; Q80TF6; -.
DR iPTMnet; Q80TF6; -.
DR PhosphoSitePlus; Q80TF6; -.
DR MaxQB; Q80TF6; -.
DR PaxDb; Q80TF6; -.
DR PeptideAtlas; Q80TF6; -.
DR PRIDE; Q80TF6; -.
DR ProteomicsDB; 257367; -.
DR Ensembl; ENSMUST00000180041; ENSMUSP00000136055; ENSMUSG00000033705.
DR MGI; MGI:3045258; Stard9.
DR VEuPathDB; HostDB:ENSMUSG00000033705; -.
DR GeneTree; ENSGT00940000163117; -.
DR HOGENOM; CLU_223684_0_0_1; -.
DR InParanoid; Q80TF6; -.
DR TreeFam; TF332626; -.
DR ChiTaRS; Stard9; mouse.
DR PRO; PR:Q80TF6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80TF6; protein.
DR Bgee; ENSMUSG00000033705; Expressed in humerus cartilage element and 185 other tissues.
DR ExpressionAtlas; Q80TF6; baseline and differential.
DR Genevisible; Q80TF6; MM.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; ISS: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 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; PS50006; FHA_DOMAIN; 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 ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..4561
FT /note="StAR-related lipid transfer protein 9"
FT /id="PRO_0000415577"
FT DOMAIN 3..384
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 482..533
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 4344..4561
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 307..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..1980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2077..2120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2320..2356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2384..2427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2439..2467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2622..2656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2712..2735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2777..2800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3002..3067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3185..3207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3246..3286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3645..3703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3790..3847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3863..3913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2414..2463
FT /evidence="ECO:0000255"
FT COILED 4185..4224
FT /evidence="ECO:0000255"
FT COMPBIAS 307..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2077..2099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2320..2354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2398..2412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2445..2459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2635..2649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3010..3067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3185..3201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3813..3828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3832..3847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3880..3894
FT /note="Basic and acidic 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 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 99
FT /note="L -> I (in Ref. 2; BAA22385)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="Q -> R (in Ref. 2; BAA22385)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="N -> K (in Ref. 2; BAA22385)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="Q -> H (in Ref. 2; BAA22385)"
FT /evidence="ECO:0000305"
FT CONFLICT 3164
FT /note="Y -> C (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3275
FT /note="Y -> H (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3281
FT /note="I -> V (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3336
FT /note="G -> D (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3364
FT /note="E -> K (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3386
FT /note="L -> P (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3422
FT /note="I -> M (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3426
FT /note="L -> I (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3451..3453
FT /note="SDV -> CDI (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3465
FT /note="V -> A (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3471
FT /note="A -> T (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3484
FT /note="M -> T (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3512
FT /note="T -> S (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3586
FT /note="S -> L (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3620
FT /note="M -> V (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3636
FT /note="P -> T (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3741
FT /note="R -> S (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3798
FT /note="R -> G (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3805
FT /note="Q -> K (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3838
FT /note="N -> T (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3841
FT /note="S -> P (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3847
FT /note="S -> N (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3857
FT /note="I -> T (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3896
FT /note="T -> A (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3900
FT /note="H -> Y (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 3964..3966
FT /note="HPV -> RPM (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 4007
FT /note="R -> G (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 4011
FT /note="E -> V (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 4030
FT /note="P -> L (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 4149
FT /note="E -> G (in Ref. 4; BAC26335)"
FT /evidence="ECO:0000305"
FT CONFLICT 4175
FT /note="E -> G (in Ref. 4; BAC26335)"
FT /evidence="ECO:0000305"
FT CONFLICT 4296
FT /note="Q -> R (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
FT CONFLICT 4454
FT /note="N -> D (in Ref. 3; BAC65771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4561 AA; 500243 MW; 3C56213EF0DAAF4A CRC64;
MANVQVAVRV RPLSKRETKE GGRIIVEVDD KVAKIRNVKV DSRPESFGDT REKVVAFGFD
YCYWSVNPED PHYASQEVVF RDLGTEVLSG AAKGYNICLF AYGQTGSGKT YTMLGTPASV
GLTPRICEGL FIREDDCASQ PCSRSIKVSF LEIYNERVRD LLKQSNQNKS YTLRVREHPE
MGPYVQGLSQ HVVTNYQQVI QLLEAGIANR ITAATHVHEA SSRSHAIFTI HCTQAILQNN
LPSETASKIN LVDLAGSERA DPSYCKDRIT EGANINKSLV TLGIVISTLA QNSQVFSSCQ
SLSSAASSGG DSGVPSTTSG ASSGGGPARR QSYIPYRDSV LTWLLKESLG GNSKTIMVAT
VSPAHTSYSE TMSTMRYASN AKNIINKPRV NEDANVKLIR ELREEIERLK AVLLNFELID
TLTQHWTEKR NDRQALMEHY GVDINRKRAR VVIDSSLPHL MALEDDVLST GVVLYHLKEG
TTKIGRIDSD QEQDIVLQGQ WIERDHCTIT STCGVVILRP TQGARCTVNG REVTASCRLT
QGAVITLGKA QKFRFNHPAE AAVLRHQRLK VGEALGSSGS LEWLDLDGDV SASRLGLCPV
LRKERRVLEE QCDRDQQPSR HSEIPYRAQP EQQQCHVEAL KQQAKEGQSR VQKELELDHT
HISQQIKDNQ QWLLTEETWL ASLRETQQEG NCGEEKELEA SVAPDAWLPT VPQTPPSPLV
QSQKRVVQPQ CSPRHTTRAT VWNIRQKKVS FQLERIIKKR RLLEAQRRLE QLSTFFWIQD
DGASRAPSWA SSSNTSGPGS QRRSRWTTCS SLSLQRLGCR RLPQLHSDFM NWDPSAMSPP
VPELTHQMPE KTLSTDCIPP KAGRLGRNSF HSSRWRKFSP ARRASTQGTH LTVSHKSVSS
QEIESLGKQP CQMSSQGQST KKQKARDGSR TFIPAAQTRW ASVNTKTGWQ KEGTCGTYKD
PKETTSQSTD LSGLEPAAGH RKVVKTFQAE SKPSPSSRAS KKHQRVLAAR ARDIVKTFSR
LPHGGPLKNQ PRAGDPGTPA SFTDSRPIKD PVREEDRDLS DTESSYSVDS LSYIYAKVPK
KLLKPEDLQG KWNLPDSENS ESDNSQISED SLAGKGHKSL PENSRGEYSM KDHGHSRART
SASVRGLPMP SDSSLCTQKY RSFSLDSLID PENRQGEPFL GSADEMPTET FWHLQNATPS
SVDQEAMDRP SPTNHRMGVG VNVLLPKSNS FYLDPQFQPP CEQLESEMEA SYSEHTNPLR
GLQLARESPL LSVDSWFSCD SKVSPSSPSG DIHSLCPSPD IHEIQPHDEK PKHWLSIEEP
KPPGTCKLPQ SSTEPPCSSD LYATSASDTS KPSVCESQGL LQPGDGGFFQ GREMPDMTNQ
GISEESHNSD MSSVLAPSAT SFTQVCSVNK DWAALHQEYL LELSDSGFEA VGEPRPAFPF
LEEDSSSLAE ASDKVDTQLP TGPGLPRNLD FSSFPVHISK IGHLRAEKDH DSLSAKVESA
SDLLSTVERM SSNGTYPADI ESLTSGSINA QPYTAGNVIP SSMTEAWEVH RASLEGCLQG
DRHSVLITSS GQKRAYHNDD TLATEGDCLP QDGALLGKNT KVQPGLLSHN SYQQPLLEEK
AASQQCTDGE VAGTRIDACC AFPSGPELFL HSTPWSSSPS SLQPPPLETF YVTKSRDALT
ETALEIPACR EAWVPSPPPR EAWGFDHSHQ VSQKAHWKNN LPKLSQSQNS KIDSPQQTTT
KRPTDLDTGE GTEELGKHSR NMREEENHDS AYSFVAQNRQ HLPSTRLKVC ECGNQLGILN
KEYSLSVHQD EEGASAWHHG SVAFNGSEPK TLLFICDSKA SGEEQSLLLP QIQSCGMHSQ
SPGARSDFIG KIANLDPEKV IPEEAAVSLK SRSLHCLSSP VIVAGGRSPT RRREGRNETG
LLREVISKDI QEEFSLPGTQ YICERCHLLL CSRERKPTEC KAHGQSQEVQ SKEEPLEEKQ
NKRVNNIDEM ARLMRSVMQL ETGILEIESK HNKHLHASHM PSTELMLQDL EDQEKADHVP
TPESSGEHLC FEDQPSFPIQ IKDDIFEDSK AREIEVTNAT SNNNTQIQKL TGSPFRSREY
VQTRESESEH SYPPPGADRL ARDTCDSLGK GTALRKPSNI SLHSRTMRGL ARALPLQPSI
ERPKKDNELL KASAKFQGQT WALESLEELE SMERFQESQI VVVPSGSELE DAKTQGGVEE
MTVDRRGSLQ EKEDMVSSTQ KVPTPSQHWK GTFFSQEAVS PFYYQTGFSA ALPHGELSGT
QPVHSLSFPR SGLHGSDTKG VSSFEYILEP VMLKTNRNSL ATGVGDQDHS GETRSSSPQE
RASGDVSTTH TPLGGSVMPV VVRASGQAVT SDSTLLNTED WITVSTSSQE DQEGDFRDTS
TGSTTQEALG SEAEATVQKE RKNSSLDRIS RQAEKRVSFL LQEDSNQGEE ERQKAEETSE
DQQLPNSAYL TPISELKGPD AEPLLLPDSS INASICLGIL AEIRQAKTQR KQLTDLVAEG
TVLPYETLQE AEWFSEAAGK PQTQKVKLGW GSTRNDAKAQ RLHEASPSAV SADLLADERK
AQVSAGSFHH LPNPETDRGP QHHLLASPHI VSELEKRYCT GKPRQFCGAS GRSDSSEVIE
KRKEASRTKS SVDPLPSDRL LSIPAVEQDG GLGSEKVSVL PSQTSYAPGR ILHGQGQLTA
RETVKGLSFG GKDSILGHQE PRSLDSTHGG GSEKISVTTQ KENAVFSECP SVICTVDNAV
DLSQSKQDHV QGLDASTGLE ETKASPKSGA VHPEAPGNVG AEANIRHPVK WKNVDSGLAC
GGDSKNPWST PFLDQRPSLH PSGVREEAPG PCPKECLVFE RNTGGSRPLG SSYEEAENRT
IPCPHLSGSQ PTTAVHACCS HSSTLLCCRD GVLRKGTPWA AAPPDHSLCI VPSTVCEVDG
TGECLSRVSL AHDLKHKCGP VDNSIPNPPT TTPVSSPAQN CSCLSTSEMR ARCLTHTFAR
GRSVEGSGEE TTGKKVTTAP EDTFPSSPAG MSSEPLRTLK NNSVDENGQA SQTMPEPPAV
TQGPGTLNSN ECVDSKLVIA AQFGHLENTK CCSEKMQPST KVRGHSCLAP QARFVDMLKP
TCHPKIETSW EEEEQQRDQV SGDGKDHAQV RNLVPSNVGG FDGYQTRDGE TKSSVPQTFF
SDFEAQTEPS QPAAQTHSQH CSDREQLPRS HRHLLPVIAI FSGPKHARYS PRPQFTVVSS
SRSLQELNLS VEPPSPTDED AQRPDSSWRP HLRGYSSEKP ISTSLKTQDC SQKALCNLNN
SSSNHRPLNP VIPPYPTSST VSCMPTPEFM TTWMPGALEQ AHQGKTDKLS VQGMPENWHS
QTDEEMLHFG SSELSPSVLS SCPQGLVHIG WKQYVFGSAV DVSCSQKPQC LIQSNMAQCS
SIDNVLEDKK SPFHSHPKTD AQTQDLPNIH SDVENDQSSN ELPLVGGSAT AQVDEILLLC
PPEMGCAGGE ASVNTFEQGT QALGSRRHWC CTDVSLQPEA RTMSDSELAS WTSMHNLSVH
LSQLLHSTSE LLGSLSHPGV VIKEQNVKRD SLDEAQQALR MDGSASTTVD EGIQTDLALP
PLAFQGPEVK SEEVSVILDM MDSGITTVAQ EKGDVPVVFQ KREAEGAAET PGLHEESTHN
KLQSPPLPSP HLRVQKADLG QNFTFMSPPA SPDGSPPPSL RPEESCMVVN MPRFSPHSGL
SLGAFESTQE PRTQKRLCGS RAVLVDRASS PILTFSASIQ ELSNPLACVT LSAPSVHPLE
DFQKLDDINS DLAVGDPRPP VDNSQATDES GDSQRAESLD REGKSPLGKS SERLLLDNSS
SCSPQQSSSL QVSFLGIAPQ QLQPKTTTGD QSKLPSPPPR HKNPKLDDSC VSEKVTSVEH
GPLRPSQWQG RTTNKDWGSE FMVEPQPNLD QPSSRRGLQP LSPCQISDTT GLQSPAVDPP
QACHPVGLLC SGSHMHVAPG PQHYNLRDLP VHNNFNNLYG VQGGPGRGLH EGESLGVRCD
SSSVGTHRPP QLSDKYSQNL EWLRLEHIPL QAGVQKLALS VELTEAKLHH GFGETDALLK
VLQSGTGEVL APQEPAVPSS EEFYTRQKKT IETLRRQRAE RLHNFRRTRS LSPQKQLGLL
PSKDLPTWEL DLPSRRQEYL QQLRKHIVDT TRIPEPAPGL ARPPSDIELM LQEYRRAREE
AKVEIAQARD RLKERTEQEK MRIRQQIISQ LLKEEEKLQT LANFSSLYTS SNGSISSGVT
SGYNSSPAFS GHLQSLEVSG DSQVPDSQDT WIGDWQDQST VRNSYLYLTG SSWKSLAHSR
RASMGSGCCS ASSLSSLGAC FSFPYQDLAK HIVSTSMADV MAACSDNLHN LFIRQATDGW
NYQGEEQEVQ LYYKEFSSTR HGFLGASVVS QPLSQVWAAV SDPTLWPLYH KPIQTARLHQ
RVTNSISLVY LVCNTTLCEL KQLRDFCCVC VEAKEGCLSI MAAQSVYDAS MPRPSRKMVR
GEILPSAWVL QPVIIEGKEI TRVISLVQVE LGAPGFPPHL LNSCIKQQPL VVAKLASFLR
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