CE295_HUMAN
ID CE295_HUMAN Reviewed; 2601 AA.
AC Q9C0D2; C9J5H9; C9JQY8; Q8N7L4; Q8N919; Q8N9B0; Q96LT8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Centrosomal protein of 295 kDa {ECO:0000305};
GN Name=CEP295 {ECO:0000312|HGNC:HGNC:29366};
GN Synonyms=KIAA1731 {ECO:0000312|HGNC:HGNC:29366};
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 1), AND VARIANTS GLN-208
RP AND GLU-499.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-2566 (ISOFORM 4), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 2152-2601 (ISOFORM 3).
RC TISSUE=Cerebellum, Chondrocyte, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND POSSIBLE FUNCTION.
RX PubMed=20844083; DOI=10.1091/mbc.e10-03-0246;
RA Knorz V.J., Spalluto C., Lessard M., Purvis T.L., Adigun F.F., Collin G.B.,
RA Hanley N.A., Wilson D.I., Hearn T.;
RT "Centriolar association of ALMS1 and likely centrosomal functions of the
RT ALMS motif-containing proteins C10orf90 and KIAA1731.";
RL Mol. Biol. Cell 21:3617-3629(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-654; SER-938;
RP SER-1637 AND THR-2473, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25131205; DOI=10.1016/j.celrep.2014.07.022;
RA Izquierdo D., Wang W.J., Uryu K., Tsou M.F.;
RT "Stabilization of cartwheel-less centrioles for duplication requires
RT CEP295-mediated centriole-to-centrosome conversion.";
RL Cell Rep. 8:957-965(2014).
RN [8]
RP FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=27185865; DOI=10.1242/jcs.186338;
RA Chang C.W., Hsu W.B., Tsai J.J., Tang C.J., Tang T.K.;
RT "CEP295 interacts with microtubules and is required for centriole
RT elongation.";
RL J. Cell Sci. 129:2501-2513(2016).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32060285; DOI=10.1038/s41467-020-14767-2;
RA Atorino E.S., Hata S., Funaya C., Neuner A., Schiebel E.;
RT "CEP44 ensures the formation of bona fide centriole wall, a requirement for
RT the centriole-to-centrosome conversion.";
RL Nat. Commun. 11:903-903(2020).
CC -!- FUNCTION: Centriole-enriched microtubule-binding protein involved in
CC centriole biogenesis (PubMed:20844083, PubMed:25131205,
CC PubMed:27185865). Essential for the generation of the distal portion of
CC new-born centrioles in a CENPJ- and CEP120-mediated elongation
CC dependent manner during the cell cycle S/G2 phase after formation of
CC the initiating cartwheel structure (PubMed:27185865). Required for the
CC recruitment of centriolar proteins, such as POC1B, POC5 and CEP135,
CC into the distal portion of centrioles (PubMed:27185865). Also required
CC for centriole-to-centrosome conversion during mitotic progression, but
CC is dispensable for cartwheel removal or centriole disengagement
CC (PubMed:25131205). Binds to and stabilizes centriolar microtubule
CC (PubMed:27185865). {ECO:0000269|PubMed:20844083,
CC ECO:0000269|PubMed:25131205, ECO:0000269|PubMed:27185865,
CC ECO:0000269|PubMed:32060285}.
CC -!- SUBUNIT: Interacts (via ALMS motif) with microtubules; this interaction
CC is direct. {ECO:0000269|PubMed:27185865}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:25131205,
CC ECO:0000269|PubMed:27185865, ECO:0000269|PubMed:32060285}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:20844083, ECO:0000269|PubMed:27185865}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:27185865}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:27185865}. Note=Associates with both
CC of the converted centrioles during G1 but becomes more enriched at the
CC newly formed daughter (or unconverted) centrioles during S, G2, and
CC early M phases (PubMed:25131205, PubMed:32060285). In early S phase,
CC localized at the procentriolar microtubule wall and enriched at the
CC proximal ends of the centrioles in CENPJ- and CEP135-dependent manner
CC (PubMed:27185865). Colocalizes with SASS6 and CEP250 proteins
CC (PubMed:25131205). Colocalizes with CEP135 and CEP192 at the
CC centrosomes (PubMed:27185865). Associates with interphase microtubules
CC and mitotic spindles (PubMed:27185865). Colocalizes with centriolar
CC acetylated tubulin (PubMed:25131205). {ECO:0000269|PubMed:25131205,
CC ECO:0000269|PubMed:27185865, ECO:0000269|PubMed:32060285}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9C0D2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0D2-2; Sequence=VSP_032289, VSP_032290;
CC Name=3;
CC IsoId=Q9C0D2-3; Sequence=VSP_032291;
CC Name=4;
CC IsoId=Q9C0D2-4; Sequence=VSP_032288, VSP_032291;
CC -!- DOMAIN: The N-terminal and the ALMS motif-containing C-terminal regions
CC are essential for CEP295-mediated centriole elongation.
CC {ECO:0000269|PubMed:27185865}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21822.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB21822.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB71582.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04638.1; Type=Erroneous initiation; Note=Truncated N-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; AB051518; BAB21822.2; ALT_SEQ; mRNA.
DR EMBL; AK057804; BAB71582.1; ALT_INIT; mRNA.
DR EMBL; AK095218; BAC04502.1; -; mRNA.
DR EMBL; AK095859; BAC04638.1; ALT_INIT; mRNA.
DR EMBL; AK098232; BAC05264.1; -; mRNA.
DR EMBL; AP001273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44708.1; -. [Q9C0D2-1]
DR RefSeq; NP_203753.1; NM_033395.1. [Q9C0D2-1]
DR AlphaFoldDB; Q9C0D2; -.
DR BioGRID; 124543; 65.
DR IntAct; Q9C0D2; 27.
DR STRING; 9606.ENSP00000316681; -.
DR CarbonylDB; Q9C0D2; -.
DR GlyGen; Q9C0D2; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q9C0D2; -.
DR PhosphoSitePlus; Q9C0D2; -.
DR BioMuta; CEP295; -.
DR DMDM; 296439480; -.
DR EPD; Q9C0D2; -.
DR jPOST; Q9C0D2; -.
DR MassIVE; Q9C0D2; -.
DR MaxQB; Q9C0D2; -.
DR PaxDb; Q9C0D2; -.
DR PeptideAtlas; Q9C0D2; -.
DR PRIDE; Q9C0D2; -.
DR ProteomicsDB; 80007; -. [Q9C0D2-1]
DR ProteomicsDB; 80008; -. [Q9C0D2-2]
DR ProteomicsDB; 80009; -. [Q9C0D2-3]
DR ProteomicsDB; 80010; -. [Q9C0D2-4]
DR Antibodypedia; 50774; 21 antibodies from 7 providers.
DR Ensembl; ENST00000325212.11; ENSP00000316681.6; ENSG00000166004.15. [Q9C0D2-1]
DR Ensembl; ENST00000531700.5; ENSP00000437323.1; ENSG00000166004.15. [Q9C0D2-2]
DR GeneID; 85459; -.
DR KEGG; hsa:85459; -.
DR MANE-Select; ENST00000325212.11; ENSP00000316681.6; NM_033395.2; NP_203753.1.
DR UCSC; uc001pdu.1; human. [Q9C0D2-1]
DR CTD; 85459; -.
DR GeneCards; CEP295; -.
DR HGNC; HGNC:29366; CEP295.
DR HPA; ENSG00000166004; Low tissue specificity.
DR MIM; 617728; gene.
DR neXtProt; NX_Q9C0D2; -.
DR OpenTargets; ENSG00000166004; -.
DR PharmGKB; PA142671597; -.
DR VEuPathDB; HostDB:ENSG00000166004; -.
DR eggNOG; ENOG502QSZR; Eukaryota.
DR GeneTree; ENSGT00940000153123; -.
DR HOGENOM; CLU_001093_0_0_1; -.
DR InParanoid; Q9C0D2; -.
DR OMA; FVNREMD; -.
DR OrthoDB; 97863at2759; -.
DR PhylomeDB; Q9C0D2; -.
DR TreeFam; TF331536; -.
DR PathwayCommons; Q9C0D2; -.
DR SignaLink; Q9C0D2; -.
DR BioGRID-ORCS; 85459; 80 hits in 1080 CRISPR screens.
DR ChiTaRS; CEP295; human.
DR GenomeRNAi; 85459; -.
DR Pharos; Q9C0D2; Tbio.
DR PRO; PR:Q9C0D2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9C0D2; protein.
DR Bgee; ENSG00000166004; Expressed in oocyte and 184 other tissues.
DR ExpressionAtlas; Q9C0D2; baseline and differential.
DR Genevisible; Q9C0D2; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IDA:UniProtKB.
DR GO; GO:1903724; P:positive regulation of centriole elongation; IMP:UniProtKB.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IDA:UniProtKB.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; IMP:UniProtKB.
DR GO; GO:1901985; P:positive regulation of protein acetylation; IMP:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; IBA:GO_Central.
DR InterPro; IPR029299; ALMS_motif.
DR InterPro; IPR029560; CEP295.
DR PANTHER; PTHR21553:SF25; PTHR21553:SF25; 1.
DR Pfam; PF15309; ALMS_motif; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2601
FT /note="Centrosomal protein of 295 kDa"
FT /id="PRO_0000324595"
FT REGION 1..560
FT /note="Necessary for centriole targeting and microtubule
FT association"
FT /evidence="ECO:0000269|PubMed:27185865"
FT REGION 1008..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1979..2004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2085..2117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2478..2601
FT /note="ALMS motif"
FT COILED 207..273
FT /evidence="ECO:0000255"
FT COILED 500..552
FT /evidence="ECO:0000255"
FT COILED 1053..1082
FT /evidence="ECO:0000255"
FT COILED 1498..1544
FT /evidence="ECO:0000255"
FT COILED 1728..1758
FT /evidence="ECO:0000255"
FT COILED 2556..2581
FT /evidence="ECO:0000255"
FT COMPBIAS 1558..1579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1795..1831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..2000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2088..2117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2473
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1988
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032288"
FT VAR_SEQ 1..1772
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032289"
FT VAR_SEQ 1818..1865
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032290"
FT VAR_SEQ 2466
FT /note="T -> TA (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032291"
FT VARIANT 80
FT /note="Q -> K (in dbSNP:rs7128850)"
FT /id="VAR_059337"
FT VARIANT 208
FT /note="R -> Q (in dbSNP:rs10831088)"
FT /evidence="ECO:0000269|PubMed:11214970"
FT /id="VAR_059338"
FT VARIANT 499
FT /note="A -> E (in dbSNP:rs4753495)"
FT /evidence="ECO:0000269|PubMed:11214970"
FT /id="VAR_059339"
FT VARIANT 1026
FT /note="E -> K (in dbSNP:rs3802771)"
FT /id="VAR_059340"
FT VARIANT 1270
FT /note="A -> G (in dbSNP:rs2298707)"
FT /id="VAR_059341"
FT VARIANT 1441
FT /note="G -> E (in dbSNP:rs3802773)"
FT /id="VAR_059342"
FT VARIANT 1459
FT /note="L -> R (in dbSNP:rs3802774)"
FT /id="VAR_059343"
FT CONFLICT 511
FT /note="Q -> H (in Ref. 1; BAB21822)"
FT /evidence="ECO:0000305"
FT CONFLICT 1888
FT /note="F -> L (in Ref. 3; BAC04502)"
FT /evidence="ECO:0000305"
FT CONFLICT 2026
FT /note="V -> L (in Ref. 3; BAC05264)"
FT /evidence="ECO:0000305"
FT CONFLICT 2081
FT /note="P -> S (in Ref. 3; BAC05264)"
FT /evidence="ECO:0000305"
FT CONFLICT 2278
FT /note="S -> G (in Ref. 3; BAC05264)"
FT /evidence="ECO:0000305"
FT CONFLICT 2294
FT /note="Q -> R (in Ref. 3; BAC05264)"
FT /evidence="ECO:0000305"
FT CONFLICT 2437
FT /note="E -> V (in Ref. 3; BAB71582/BAC04502/BAC04638/
FT BAC05264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2601 AA; 295176 MW; F18F9B2EE1DAADC7 CRC64;
MKRKVVNTHK LRLSPNEEAF ILKEDYERRR KLRLLQVREQ ERDIALQIRE DIKQRRNQQF
TRLAEELRAE WEESQTQKIQ NLEKLYLASL RSMGEGHRQA KENEPDLDAL AQRAAERKRK
ADLRHKEALK VQKNQKEILL KQKTWHIKAR KEALLVEKER SAKITSLPPP PPTLFENIEV
KRISAVKTNS STYHHLHTFV NRETDTKRPD ARLAAEEEAK RLEELQKQAA QERMERFEKA
HVRGFQAMKK IHLAQNQEKL MKELKQLQQE DLARRRQTVA QMPPQLVELP YKRSEMKEDW
QRELEFAFED MYNADRKVKG NLILHLEPEP LPTVTNQIQD EELDLSMEQE NLGAAEDLPV
TEAEICSSET DVPLVMKTQQ IPSKVLFKKL LNKIRSQKSL WTIKSMSEDE SEMITTVSEI
ESKAPTVESG TIASKERTLS SGQEQVVESD TLTIESGPLA SEDKPLSCGT NSGKEQEINE
TLPITTVAQS SVLLHPQEAA ARIRMSARQK QIMEIEEQKQ KQLELLEQIE QQKLRLETDC
FRAQLEEEKR KKTQPTGVGI APASCPVISD EDSHRQMIRN YQHQLLQQNR LHRQSVETAR
KQLLEYQTML KGRCPSVSAP SLITDSVISV PSWKSERPTA ISEHWDQGQR LKLSPNKYQP
IQPIQTSKLE QDHFQVARQN HFPQRQVETT ETLRASDILT NQALESQEHL RQFSQTETQQ
RDYKLVPKDS ETLSRALSHD RQLISQDARK ISETFGATTF QSLESQQLFS ENSENISYHL
TEPSSFVPLV PQHSFSSLPV KVESGKIQEP FSAMSKSTVS TSHSIISQMH DRPLLPSENI
TAQQGNMKAL QEQLDLQKKV LQATQEAQEQ LLLCKQKEVE QQTGLSVFLP LVTPDSSALL
PSAKADLGRI QESSPTKNNI AVSSDHHVIS QLQDKRLSLS QPILSQQNNF KFLQEQLNIQ
KDSLQARREA QEVLYVHKQS ELDRRVCSEQ AEPSFPFQVA QHTFTSLPSA DTKSGKIQEQ
HSSKSEKGLV SCQSDIPISQ DGSLSFLQQF LPLHDSLKLL QEQLTKQRDT LQARHEAQVE
LLLHRQRDLG DSKSGLVSSS SSPVVVQHSV ASQASAKAEP RRIQELYLSE KENVGPSCHL
IIPTFQDKSL SFPQHSLAQQ ENLTILQEQS QIQRVILGAK EGTQEFVHTE SELEKRISSE
QTGTSSSLSQ VDESERFQEC ISIKSDSTIP LSHPKIPRCQ ERLLRVSQHM LPLQDNLEEH
QAWLDTEKEA FHFSQKTQEN TSSEQTGSSS FIPQLVQLSF TSLASAESGT ILEPLFTESE
SKIFSSHLQI PQLQDRLLRI SQLIQPQQDN LKALQEQLAT QREAIILARQ EAREELLLHQ
SEWEGRISPE QVDTSSLPLV PQHSFASLPL NESERNQEPC SINSDNIVSS GHSEIPTLPD
GLLGLSHLVL PQQDNLIALE EHLHAQTDFL PSIEKTQKEL VLSKPCKFEE KVSSEHFIQS
HHGDLQALQQ QLDTQKKAIR SIQEVQEELL LQRLSELEKR VSSEQVCSSS FVSQVPVADS
ERTQKSFPTK SNDTLPSSHR EIPRLQDRLL SLSKPILPQQ DNMTAQLDAQ REVMYSYEKP
QEELSLNKQR KLNKSESAEH TIPSLFLPKE TEHSFIPLPF AEAKPKSTCE LYSSQNEHAA
PPSNPVIPGF QDRLLSFSQS VLTQQDNLGL QKQLDLQREV LHYSQKAQEK LLVQRQTALQ
QQIQKHEETL KDFFKDSQIS KPTVENDLKT QKMGQLRDWF PNTQDLAGND QENIRHADRN
NSDDNHLASE DTSAKQSGEH LEKDLGRRSS KPPVAKVKCG LDLNQHELSA IQEVESPAIG
RTSILGKPGI YEDRDPLRVS ISREQSFFGS PLAHDPFSCL QLVGQENVCG DDYDEAVKLK
ESVVENHAVL SYAVEEEHAY LGPTVKPDDK AKTLSYEPLS SATVSTGSLL SYENTDLSLT
DPESFSEHMD DSKQESTTSK EEETNIISSI VPSTQDIYQR QNSSDVHKSL LPAVDETTCG
HTHFQQMIDK YINEANLIPE KTDLQELEHI FPNLHHQLFK PLEPHPDFDL SSSSSGISPD
NRDFYQRSDS SSESHCATGL SKSTVYFTAL RRTSMHSSLN TSPNQQPDTN LAHVGAHSFA
TENIIGGSEQ CFEQLQPEYS SQEESQHADL PSIFSIEARD SSQGMKNQNY PSEEHTEILQ
NKKKIVHFQL SIGNLSSVYS SSDEANVFDQ LNVQHSTPCG SNSSECSTKH QLESRKESMG
FEELSKRGVV TMLQSQGLIE DNKNETCRVL DINPQVEETD SRLCVRTVEM GTSIQAPYSL
TTQNEKYFEN SAETDIPKIT KKLSQLGESE LFASSGSFSL QSSIPVWETE TGHGIMEEPE
LTLISTTDTS IAEMDFANLT LEEKSENEAK CFFQVSEFLP LVSATEASDY PAVSELSIEK
PRTASTETPR RLTPVPGSLQ EAFIKRKKSF MERSHQRQKE IRNKIHVSEN SQIKTVKEKP
SISSSVSRLK GVNKVRASFP EDRKTTQALR HQRGLRLYNQ LAEVKQQKEE KTKQEAYAQN
RARAKEFHKK TLEKLRAKNT C
