IFT88_HUMAN
ID IFT88_HUMAN Reviewed; 824 AA.
AC Q13099; A2A491; B4DUS2; Q5SZJ6; Q8N719;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Intraflagellar transport protein 88 homolog;
DE AltName: Full=Recessive polycystic kidney disease protein Tg737 homolog;
DE AltName: Full=Tetratricopeptide repeat protein 10;
DE Short=TPR repeat protein 10;
GN Name=IFT88; Synonyms=TG737, TTC10;
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 [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT
RP ASN-446.
RC TISSUE=Liver;
RX PubMed=7633404; DOI=10.1093/hmg/4.4.559;
RA Schrick J.J., Onuchic L.F., Reeders S.T., Korenberg J., Chen X.-N.,
RA Moyer J.H., Wilkinson J.E., Woychik R.P.;
RT "Characterization of the human homologue of the mouse Tg737 candidate
RT polycystic kidney disease gene.";
RL Hum. Mol. Genet. 4:559-567(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Neuroepithelioma;
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=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-374.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=28625565; DOI=10.1016/j.devcel.2017.05.016;
RA Kanie T., Abbott K.L., Mooney N.A., Plowey E.D., Demeter J., Jackson P.K.;
RT "The CEP19-RABL2 GTPase complex binds IFT-B to initiate intraflagellar
RT transport at the ciliary base.";
RL Dev. Cell 42:1-15(2017).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=28428259; DOI=10.1091/mbc.e17-01-0017;
RA Nishijima Y., Hagiya Y., Kubo T., Takei R., Katoh Y., Nakayama K.;
RT "RABL2 interacts with the intraflagellar transport-B complex and CEP19 and
RT participates in ciliary assembly.";
RL Mol. Biol. Cell 28:1652-1666(2017).
RN [8]
RP INTERACTION WITH ENTR1, AND SUBCELLULAR LOCATION.
RX PubMed=27767179; DOI=10.1038/srep35399;
RA Yu F., Sharma S., Skowronek A., Erdmann K.S.;
RT "The serologically defined colon cancer antigen-3 (SDCCAG3) is involved in
RT the regulation of ciliogenesis.";
RL Sci. Rep. 6:35399-35399(2016).
RN [9]
RP INTERACTION WITH LRRC56.
RX PubMed=30388400; DOI=10.1016/j.ajhg.2018.10.003;
RG Care4Rare Canada Consortium;
RA Bonnefoy S., Watson C.M., Kernohan K.D., Lemos M., Hutchinson S.,
RA Poulter J.A., Crinnion L.A., Berry I., Simmonds J., Vasudevan P.,
RA O'Callaghan C., Hirst R.A., Rutman A., Huang L., Hartley T., Grynspan D.,
RA Moya E., Li C., Carr I.M., Bonthron D.T., Leroux M., Boycott K.M.,
RA Bastin P., Sheridan E.G.;
RT "Biallelic mutations in LRRC56, encoding a protein associated with
RT intraflagellar transport, cause mucociliary clearance and laterality
RT defects.";
RL Am. J. Hum. Genet. 103:727-739(2018).
CC -!- FUNCTION: Involved in primary cilium biogenesis. Also involved in
CC autophagy since it is required for trafficking of ATG16L and the
CC expansion of the autophagic compartment.
CC {ECO:0000250|UniProtKB:Q61371}.
CC -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC IFT80, IFT81, and IFT88 (By similarity). Interacts with IFT20, IFT22,
CC HSPB11, IFT27, IFT52, TRAF3IP1, IFT74, IFT80 and IFT81 (By similarity).
CC Interacts with IFT172 (By similarity). Interacts with IFT57 (By
CC similarity). Interacts with IFT46 (By similarity). Interacts with
CC TTC30B (By similarity). Interacts with C2CD3 (By similarity). Interacts
CC with ENTR1 (via N-terminus) (PubMed:27767179). Interacts with LRRC56
CC (PubMed:30388400). Interacts with DZIP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q61371, ECO:0000269|PubMed:27767179,
CC ECO:0000269|PubMed:30388400}.
CC -!- INTERACTION:
CC Q13099; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-347427, EBI-1765641;
CC Q13099; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-347427, EBI-744556;
CC Q13099; Q96G04: EEF2KMT; NbExp=3; IntAct=EBI-347427, EBI-747840;
CC Q13099; A0A0C4DGQ7: EML2; NbExp=3; IntAct=EBI-347427, EBI-12112376;
CC Q13099; P27987: ITPKB; NbExp=3; IntAct=EBI-347427, EBI-751388;
CC Q13099; Q9NZV6: MSRB1; NbExp=3; IntAct=EBI-347427, EBI-12330065;
CC Q13099; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-347427, EBI-455078;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q61371}. Cell
CC projection, cilium {ECO:0000269|PubMed:28428259}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:27767179,
CC ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:27767179}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q61371}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q61371}. Note=Colocalizes with ENTR1 and gamma-
CC tubulin at the basal body of primary cilia. Colocalizes with ENTR1 and
CC pericentrin at the centrosome. {ECO:0000269|PubMed:27767179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=Q13099-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q13099-1; Sequence=VSP_060641;
CC Name=3;
CC IsoId=Q13099-3; Sequence=VSP_060641, VSP_060642;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, brain, liver, lung, kidney,
CC skeletal muscle and pancreas. {ECO:0000269|PubMed:7633404}.
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DR EMBL; U20362; AAA86720.1; -; mRNA.
DR EMBL; AK300769; BAG62434.1; -; mRNA.
DR EMBL; AL161772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08272.1; -; Genomic_DNA.
DR EMBL; BC030776; AAH30776.2; -; mRNA.
DR CCDS; CCDS31944.1; -. [Q13099-1]
DR CCDS; CCDS31945.1; -. [Q13099-2]
DR RefSeq; NP_001305420.1; NM_001318491.1.
DR RefSeq; NP_006522.2; NM_006531.4. [Q13099-2]
DR RefSeq; NP_783195.2; NM_175605.4. [Q13099-1]
DR RefSeq; XP_005266610.1; XM_005266553.2.
DR RefSeq; XP_006719933.1; XM_006719870.3. [Q13099-2]
DR RefSeq; XP_011533543.1; XM_011535241.2.
DR RefSeq; XP_011533544.1; XM_011535242.1.
DR RefSeq; XP_011533545.1; XM_011535243.1. [Q13099-2]
DR RefSeq; XP_016876246.1; XM_017020757.1. [Q13099-2]
DR RefSeq; XP_016876247.1; XM_017020758.1. [Q13099-3]
DR AlphaFoldDB; Q13099; -.
DR SMR; Q13099; -.
DR BioGRID; 113771; 51.
DR ComplexPortal; CPX-5022; IFT-B complex.
DR CORUM; Q13099; -.
DR IntAct; Q13099; 54.
DR MINT; Q13099; -.
DR STRING; 9606.ENSP00000323580; -.
DR iPTMnet; Q13099; -.
DR PhosphoSitePlus; Q13099; -.
DR BioMuta; IFT88; -.
DR DMDM; 206729873; -.
DR EPD; Q13099; -.
DR jPOST; Q13099; -.
DR MassIVE; Q13099; -.
DR MaxQB; Q13099; -.
DR PaxDb; Q13099; -.
DR PeptideAtlas; Q13099; -.
DR PRIDE; Q13099; -.
DR ProteomicsDB; 59151; -. [Q13099-1]
DR ProteomicsDB; 59152; -. [Q13099-2]
DR ProteomicsDB; 59153; -. [Q13099-3]
DR Antibodypedia; 22319; 268 antibodies from 29 providers.
DR DNASU; 8100; -.
DR Ensembl; ENST00000319980.10; ENSP00000323580.6; ENSG00000032742.18. [Q13099-1]
DR Ensembl; ENST00000351808.10; ENSP00000261632.5; ENSG00000032742.18. [Q13099-2]
DR GeneID; 8100; -.
DR KEGG; hsa:8100; -.
DR MANE-Select; ENST00000351808.10; ENSP00000261632.5; NM_006531.5; NP_006522.2.
DR UCSC; uc001unh.4; human. [Q13099-2]
DR CTD; 8100; -.
DR DisGeNET; 8100; -.
DR GeneCards; IFT88; -.
DR HGNC; HGNC:20606; IFT88.
DR HPA; ENSG00000032742; Tissue enhanced (testis).
DR MalaCards; IFT88; -.
DR MIM; 600595; gene.
DR neXtProt; NX_Q13099; -.
DR OpenTargets; ENSG00000032742; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA134991804; -.
DR VEuPathDB; HostDB:ENSG00000032742; -.
DR eggNOG; KOG2003; Eukaryota.
DR GeneTree; ENSGT00390000015473; -.
DR HOGENOM; CLU_010738_1_0_1; -.
DR InParanoid; Q13099; -.
DR OMA; RIKIMHN; -.
DR OrthoDB; 259837at2759; -.
DR PhylomeDB; Q13099; -.
DR TreeFam; TF313218; -.
DR PathwayCommons; Q13099; -.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR SignaLink; Q13099; -.
DR SIGNOR; Q13099; -.
DR BioGRID-ORCS; 8100; 12 hits in 1079 CRISPR screens.
DR ChiTaRS; IFT88; human.
DR GeneWiki; IFT88; -.
DR GenomeRNAi; 8100; -.
DR Pharos; Q13099; Tbio.
DR PRO; PR:Q13099; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q13099; protein.
DR Bgee; ENSG00000032742; Expressed in bronchial epithelial cell and 200 other tissues.
DR ExpressionAtlas; Q13099; baseline and differential.
DR Genevisible; Q13099; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IBA:GO_Central.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal.
DR GO; GO:0031514; C:motile cilium; ISS:BHF-UCL.
DR GO; GO:0097730; C:non-motile cilium; IBA:GO_Central.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IBA:GO_Central.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IBA:GO_Central.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:2000785; P:regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00671; SEL1; 4.
DR SMART; SM00028; TPR; 11.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 9.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Flagellum;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..824
FT /note="Intraflagellar transport protein 88 homolog"
FT /id="PRO_0000106391"
FT REPEAT 197..230
FT /note="TPR 1"
FT REPEAT 233..266
FT /note="TPR 2"
FT REPEAT 272..305
FT /note="TPR 3"
FT REPEAT 307..338
FT /note="TPR 4"
FT REPEAT 415..448
FT /note="TPR 5"
FT REPEAT 450..483
FT /note="TPR 6"
FT REPEAT 484..517
FT /note="TPR 7"
FT REPEAT 518..551
FT /note="TPR 8"
FT REPEAT 552..585
FT /note="TPR 9"
FT REPEAT 586..619
FT /note="TPR 10"
FT REPEAT 620..653
FT /note="TPR 11"
FT REPEAT 654..687
FT /note="TPR 12"
FT REGION 113..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1
FT /note="M -> MKFTNTKVQM (in isoform 1 and isoform 3)"
FT /id="VSP_060641"
FT VAR_SEQ 52..70
FT /note="Missing (in isoform 3)"
FT /id="VSP_060642"
FT VARIANT 374
FT /note="M -> I (in dbSNP:rs2442455)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_046464"
FT VARIANT 446
FT /note="S -> N (in dbSNP:rs9509307)"
FT /evidence="ECO:0000269|PubMed:7633404"
FT /id="VAR_046465"
FT VARIANT 662
FT /note="S -> G (in dbSNP:rs9552254)"
FT /id="VAR_046466"
FT CONFLICT 201
FT /note="F -> S (in Ref. 1; AAA86720)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="K -> E (in Ref. 5; AAH30776)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="I -> V (in Ref. 5; AAH30776)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="M -> T (in Ref. 1; AAA86720)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="Y -> C (in Ref. 1; AAA86720)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="E -> G (in Ref. 5; AAH30776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 824 AA; 93192 MW; 12E30169CFC5476B CRC64;
MMQNVHLAPE TDEDDLYSGY NDYNPIYDIE ELENDAAFQQ AVRTSHGRRP PITAKISSTA
VTRPIATGYG SKTSLASSIG RPMTGAIQDG VTRPMTAVRA AGFTKAALRG SAFDPLSQSR
GPASPLEAKK KDSPEEKIKQ LEKEVNELVE ESCIANSCGD LKLALEKAKD AGRKERVLVR
QREQVTTPEN INLDLTYSVL FNLASQYSVN EMYAEALNTY QVIVKNKMFS NAGILKMNMG
NIYLKQRNYS KAIKFYRMAL DQVPSVNKQM RIKIMQNIGV TFIQAGQYSD AINSYEHIMS
MAPNLKAGYN LTICYFAIGD REKMKKAFQK LITVPLEIDE DKYISPSDDP HTNLVTEAIK
NDHLRQMERE RKAMAEKYIM TSAKLIAPVI ETSFAAGYDW CVEVVKASQY VELANDLEIN
KAVTYLRQKD YNQAVEILKV LEKKDSRVKS AAATNLSALY YMGKDFAQAS SYADIAVNSD
RYNPAALTNK GNTVFANGDY EKAAEFYKEA LRNDSSCTEA LYNIGLTYEK LNRLDEALDC
FLKLHAILRN SAEVLYQIAN IYELMENPSQ AIEWLMQVVS VIPTDPQVLS KLGELYDREG
DKSQAFQYYY ESYRYFPCNI EVIEWLGAYY IDTQFWEKAI QYFERASLIQ PTQVKWQLMV
ASCFRRSGNY QKALDTYKDT HRKFPENVEC LRFLVRLCTD LGLKDAQEYA RKLKRLEKMK
EIREQRIKSG RDGSGGSRGK REGSASGDSG QNYSASSKGE RLSARLRALP GTNEPYESSS
NKEIDASYVD PLGPQIERPK TAAKKRIDED DFADEELGDD LLPE
