CEP78_HUMAN
ID CEP78_HUMAN Reviewed; 689 AA.
AC Q5JTW2; A1A4S8; E9PHX5; Q5BJE3; Q5JTW0; Q5JTW1; Q9H9N3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Centrosomal protein of 78 kDa;
DE Short=Cep78;
GN Name=CEP78; Synonyms=C9orf81;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-665 (ISOFORM 1).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-327, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP INVOLVEMENT IN CRDHL1, FUNCTION, INTERACTION WITH FAM161A, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27588451; DOI=10.1016/j.ajhg.2016.07.009;
RA Nikopoulos K., Farinelli P., Giangreco B., Tsika C., Royer-Bertrand B.,
RA Mbefo M.K., Bedoni N., Kjellstroem U., El Zaoui I., Di Gioia S.A.,
RA Balzano S., Cisarova K., Messina A., Decembrini S., Plainis S.,
RA Blazaki S.V., Khan M.I., Micheal S., Boldt K., Ueffing M., Moulin A.P.,
RA Cremers F.P., Roepman R., Arsenijevic Y., Tsilimbaris M.K., Andreasson S.,
RA Rivolta C.;
RT "Mutations in CEP78 cause cone-rod dystrophy and hearing loss associated
RT with primary-cilia defects.";
RL Am. J. Hum. Genet. 99:770-776(2016).
RN [9]
RP INVOLVEMENT IN CRDHL1, AND TISSUE SPECIFICITY.
RX PubMed=27588452; DOI=10.1016/j.ajhg.2016.07.010;
RA Namburi P., Ratnapriya R., Khateb S., Lazar C.H., Kinarty Y., Obolensky A.,
RA Erdinest I., Marks-Ohana D., Pras E., Ben-Yosef T., Newman H., Gross M.,
RA Swaroop A., Banin E., Sharon D.;
RT "Bi-allelic truncating mutations in CEP78, encoding centrosomal protein 78,
RT cause cone-rod degeneration with sensorineural hearing loss.";
RL Am. J. Hum. Genet. 99:777-784(2016).
RN [10]
RP FUNCTION, INTERACTION WITH PLK4, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=27246242; DOI=10.1242/jcs.184093;
RA Brunk K., Zhu M., Baerenz F., Kratz A.S., Haselmann-Weiss U., Antony C.,
RA Hoffmann I.;
RT "Cep78 is a new centriolar protein involved in Plk4-induced centriole
RT overduplication.";
RL J. Cell Sci. 129:2713-2718(2016).
RN [11]
RP INVOLVEMENT IN CRDHL1.
RX PubMed=27627988; DOI=10.1136/jmedgenet-2016-104166;
RA Fu Q., Xu M., Chen X., Sheng X., Yuan Z., Liu Y., Li H., Sun Z., Li H.,
RA Yang L., Wang K., Zhang F., Li Y., Zhao C., Sui R., Chen R.;
RT "CEP78 is mutated in a distinct type of Usher syndrome.";
RL J. Med. Genet. 54:190-195(2017).
CC -!- FUNCTION: May be required for efficient PLK4 centrosomal localization
CC and PLK4-induced overduplication of centrioles (PubMed:27246242). May
CC play a role in cilium biogenesis (PubMed:27588451).
CC {ECO:0000269|PubMed:27246242, ECO:0000269|PubMed:27588451}.
CC -!- SUBUNIT: Interacts with PLK4 (PubMed:27246242). Interacts with FAM161A
CC (PubMed:27588451). {ECO:0000269|PubMed:27246242,
CC ECO:0000269|PubMed:27588451}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:27246242}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:27588451}. Note=Mainly localizes at the
CC centriolar wall, but also found in the pericentriolar material
CC (PubMed:27246242). Expressed in photoreceptor inner segment
CC (PubMed:27588452). {ECO:0000269|PubMed:27246242,
CC ECO:0000269|PubMed:27588452}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5JTW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JTW2-2; Sequence=VSP_026321, VSP_026322, VSP_026323;
CC Name=3;
CC IsoId=Q5JTW2-3; Sequence=VSP_026322;
CC Name=4;
CC IsoId=Q5JTW2-5; Sequence=VSP_026321, VSP_026323;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:27588451,
CC PubMed:27588452). Expressed in different retinal cell types with higher
CC expression in cone compared to rod cells (at protein level)
CC (PubMed:27588452). {ECO:0000269|PubMed:27588451,
CC ECO:0000269|PubMed:27588452}.
CC -!- DEVELOPMENTAL STAGE: Expression is cell cycle-dependent, with low
CC levels in mitosis. The expression starts to increase during late G1
CC until the S/G2 transition (at protein level).
CC {ECO:0000269|PubMed:27246242}.
CC -!- DISEASE: Cone-rod dystrophy and hearing loss 1 (CRDHL1) [MIM:617236]:
CC An autosomal recessive disease defined by the association of
CC progressive cone-rod dystrophy with sensorineural hearing loss. Cone-
CC rod dystrophy is characterized by retinal pigment deposits visible on
CC fundus examination, predominantly in the macular region, and initial
CC loss of cone photoreceptors followed by rod degeneration. This leads to
CC decreased visual acuity and sensitivity in the central visual field,
CC followed by loss of peripheral vision. Severe loss of vision occurs
CC earlier than in retinitis pigmentosa, due to cone photoreceptors
CC degenerating at a higher rate than rod photoreceptors.
CC {ECO:0000269|PubMed:27588451, ECO:0000269|PubMed:27588452,
CC ECO:0000269|PubMed:27627988}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CEP78 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH91515.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH91515.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
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DR EMBL; AL353705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091515; AAH91515.1; ALT_SEQ; mRNA.
DR EMBL; BC128058; AAI28059.1; -; mRNA.
DR EMBL; AK022705; BAB14190.1; -; mRNA.
DR CCDS; CCDS47984.1; -. [Q5JTW2-2]
DR CCDS; CCDS47985.1; -. [Q5JTW2-5]
DR CCDS; CCDS83376.1; -. [Q5JTW2-3]
DR CCDS; CCDS83377.1; -. [Q5JTW2-1]
DR RefSeq; NP_001092272.1; NM_001098802.1. [Q5JTW2-2]
DR RefSeq; NP_001317620.1; NM_001330691.1. [Q5JTW2-3]
DR RefSeq; NP_001317622.1; NM_001330693.1. [Q5JTW2-1]
DR RefSeq; NP_001317623.1; NM_001330694.1.
DR RefSeq; NP_115547.1; NM_032171.1. [Q5JTW2-5]
DR AlphaFoldDB; Q5JTW2; -.
DR SMR; Q5JTW2; -.
DR BioGRID; 123903; 94.
DR IntAct; Q5JTW2; 27.
DR MINT; Q5JTW2; -.
DR STRING; 9606.ENSP00000365782; -.
DR GlyGen; Q5JTW2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5JTW2; -.
DR MetOSite; Q5JTW2; -.
DR PhosphoSitePlus; Q5JTW2; -.
DR BioMuta; CEP78; -.
DR DMDM; 74742229; -.
DR EPD; Q5JTW2; -.
DR jPOST; Q5JTW2; -.
DR MassIVE; Q5JTW2; -.
DR MaxQB; Q5JTW2; -.
DR PaxDb; Q5JTW2; -.
DR PeptideAtlas; Q5JTW2; -.
DR PRIDE; Q5JTW2; -.
DR ProteomicsDB; 20620; -.
DR ProteomicsDB; 63235; -. [Q5JTW2-1]
DR ProteomicsDB; 63236; -. [Q5JTW2-2]
DR ProteomicsDB; 63237; -. [Q5JTW2-3]
DR Antibodypedia; 27392; 88 antibodies from 21 providers.
DR DNASU; 84131; -.
DR Ensembl; ENST00000376597.9; ENSP00000365782.4; ENSG00000148019.14. [Q5JTW2-2]
DR Ensembl; ENST00000415759.6; ENSP00000399286.2; ENSG00000148019.14. [Q5JTW2-5]
DR Ensembl; ENST00000424347.6; ENSP00000411284.2; ENSG00000148019.14. [Q5JTW2-1]
DR Ensembl; ENST00000642669.1; ENSP00000495681.1; ENSG00000148019.14. [Q5JTW2-5]
DR Ensembl; ENST00000643273.2; ENSP00000496423.2; ENSG00000148019.14. [Q5JTW2-3]
DR GeneID; 84131; -.
DR KEGG; hsa:84131; -.
DR MANE-Select; ENST00000643273.2; ENSP00000496423.2; NM_001330691.3; NP_001317620.1. [Q5JTW2-3]
DR UCSC; uc004akx.3; human. [Q5JTW2-1]
DR CTD; 84131; -.
DR DisGeNET; 84131; -.
DR GeneCards; CEP78; -.
DR HGNC; HGNC:25740; CEP78.
DR HPA; ENSG00000148019; Low tissue specificity.
DR MalaCards; CEP78; -.
DR MIM; 617110; gene.
DR MIM; 617236; phenotype.
DR neXtProt; NX_Q5JTW2; -.
DR OpenTargets; ENSG00000148019; -.
DR Orphanet; 231183; Usher syndrome type 3.
DR PharmGKB; PA134937066; -.
DR VEuPathDB; HostDB:ENSG00000148019; -.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00390000013287; -.
DR HOGENOM; CLU_021273_0_0_1; -.
DR InParanoid; Q5JTW2; -.
DR OMA; MTLKLCK; -.
DR OrthoDB; 982225at2759; -.
DR PhylomeDB; Q5JTW2; -.
DR TreeFam; TF328928; -.
DR PathwayCommons; Q5JTW2; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q5JTW2; -.
DR BioGRID-ORCS; 84131; 11 hits in 1082 CRISPR screens.
DR ChiTaRS; CEP78; human.
DR GeneWiki; CEP78; -.
DR GenomeRNAi; 84131; -.
DR Pharos; Q5JTW2; Tbio.
DR PRO; PR:Q5JTW2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5JTW2; protein.
DR Bgee; ENSG00000148019; Expressed in secondary oocyte and 163 other tissues.
DR ExpressionAtlas; Q5JTW2; baseline and differential.
DR Genevisible; Q5JTW2; HS.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0044782; P:cilium organization; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR026212; Cep78.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13516; LRR_6; 2.
DR PRINTS; PR02062; CENTROSOME78.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cone-rod dystrophy; Cytoplasm;
KW Cytoskeleton; Deafness; Phosphoprotein; Reference proteome.
FT CHAIN 1..689
FT /note="Centrosomal protein of 78 kDa"
FT /id="PRO_0000291952"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..505
FT /evidence="ECO:0000255"
FT COMPBIAS 574..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 356
FT /note="I -> IV (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026321"
FT VAR_SEQ 599
FT /note="Q -> QVSICMQSAYNEGTLMK (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026322"
FT VAR_SEQ 687..689
FT /note="ESH -> GEYTKKHSDKQHPGKDLHS (in isoform 2 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026323"
FT CONFLICT 49
FT /note="R -> G (in Ref. 2; AAI28059)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="K -> R (in Ref. 2; AAI28059)"
FT /evidence="ECO:0000305"
FT CONFLICT 236..237
FT /note="CN -> GY (in Ref. 3; BAB14190)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="K -> R (in Ref. 3; BAB14190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 689 AA; 76396 MW; 5FEEE6542F8E4F5F CRC64;
MIDSVKLRRD SAADFFSHYE YLCALQNSVP LPAVRACLRE GVLDFNADRL RGVDWAPLLS
TLKINKDLPL VSIKSFFQPW LGDTGSDMNK FCRSRVPAIR YKDVTFQLCK ALKGCLSISS
VLKNLELNGL ILRERDLTIL AKGLNKSASL VHLSLANCPI GDGGLEIICQ GIKSSITLKT
VNFTGCNLTW QGADHMAKIL KYQTMRRHEE TWAESLRYRR PDLDCMAGLR RITLNCNTLI
GDLGACAFAD SLSEDLWLRA LDLQQCGLTN EGAKALLEAL ETNTTLVVLD IRKNPLIDHS
MMKAVIKKVL QNGRSAKSEY QWITSPSVKE PSKTAKQKRR TIILGSGHKG KATIRIGLAT
KKPVSSGRKH SLGKEYYAPA PLPPGVSGFL PWRTAERAKR HRGFPLIKTR DICNQLQQPG
FPVTVTVESP SSSEVEEVDD SSESVHEVPE KTSIEQEALQ EKLEECLKQL KEERVIRLKV
DKRVSELEHE NAQLRNINFS LSEALHAQSL TNMILDDEGV LGSIENSFQK FHAFLDLLKD
AGLGQLATMA GIDQSDFQLL GHPQMTSTVS NPPKEEKKAL EDEKPEPKQN ALGQMQNIQF
QKITGDARIP LPLDSFPVPV STPEGLGTSS NNLGVPATEQ RQESFEGFIA RMCSPSPDAT
SGTGSQRKEE ELSRNSRSSS EKKTKTESH
