CEP72_HUMAN
ID CEP72_HUMAN Reviewed; 647 AA.
AC Q9P209; B4DR26; Q9BV03; Q9BWM3; Q9NVR4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Centrosomal protein of 72 kDa;
DE Short=Cep72;
GN Name=CEP72; Synonyms=KIAA1519;
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 VARIANT ALA-509.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(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), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 93-647 (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Placenta;
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIZ.
RX PubMed=19536135; DOI=10.1038/emboj.2009.161;
RA Oshimori N., Li X., Ohsugi M., Yamamoto T.;
RT "Cep72 regulates the localization of key centrosomal proteins and proper
RT bipolar spindle formation.";
RL EMBO J. 28:2066-2076(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-382 AND SER-404, 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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDK5RAP2 AND PCM1.
RX PubMed=26297806; DOI=10.7554/elife.07519;
RA Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L.,
RA Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N.,
RA Walsh C.A., Reiter J.F.;
RT "Centriolar satellites assemble centrosomal microcephaly proteins to
RT recruit CDK2 and promote centriole duplication.";
RL Elife 4:0-0(2015).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in the recruitment of key centrosomal proteins to
CC the centrosome. Provides centrosomal microtubule-nucleation activity on
CC the gamma-tubulin ring complexes (gamma-TuRCs) and has critical roles
CC in forming a focused bipolar spindle, which is needed for proper
CC tension generation between sister chromatids. Required for localization
CC of KIZ, AKAP9 and gamma-tubulin ring complexes (gamma-TuRCs)
CC (PubMed:19536135). Involved in centriole duplication. Required for
CC CDK5RAP22, CEP152, WDR62 and CEP63 centrosomal localization and
CC promotes the centrosomal localization of CDK2 (PubMed:26297806).
CC {ECO:0000269|PubMed:19536135, ECO:0000269|PubMed:26297806}.
CC -!- SUBUNIT: Interacts with KIZ, PCM1 and CDK5RAP2.
CC {ECO:0000269|PubMed:19536135, ECO:0000269|PubMed:26297806}.
CC -!- INTERACTION:
CC Q9P209; O15265: ATXN7; NbExp=2; IntAct=EBI-739498, EBI-708350;
CC Q9P209; Q7Z7H3: CATIP; NbExp=5; IntAct=EBI-739498, EBI-10258233;
CC Q9P209; Q96SN8: CDK5RAP2; NbExp=3; IntAct=EBI-739498, EBI-308374;
CC Q9P209; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-739498, EBI-743375;
CC Q9P209; Q3B820: FAM161A; NbExp=3; IntAct=EBI-739498, EBI-719941;
CC Q9P209; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-739498, EBI-6658203;
CC Q9P209; P51114: FXR1; NbExp=2; IntAct=EBI-739498, EBI-713291;
CC Q9P209; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-739498, EBI-5916454;
CC Q9P209; Q14005-2: IL16; NbExp=3; IntAct=EBI-739498, EBI-17178971;
CC Q9P209; Q0VD86: INCA1; NbExp=3; IntAct=EBI-739498, EBI-6509505;
CC Q9P209; Q2M2Z5: KIZ; NbExp=3; IntAct=EBI-739498, EBI-2554344;
CC Q9P209; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-739498, EBI-739832;
CC Q9P209; Q9Y5B8: NME7; NbExp=12; IntAct=EBI-739498, EBI-744782;
CC Q9P209; Q96CV9: OPTN; NbExp=3; IntAct=EBI-739498, EBI-748974;
CC Q9P209; Q15154: PCM1; NbExp=7; IntAct=EBI-739498, EBI-741421;
CC Q9P209; Q9Y237: PIN4; NbExp=4; IntAct=EBI-739498, EBI-714599;
CC Q9P209; P25786: PSMA1; NbExp=5; IntAct=EBI-739498, EBI-359352;
CC Q9P209; Q6NXQ0: SFRS2; NbExp=3; IntAct=EBI-739498, EBI-10251550;
CC Q9P209; Q96R06: SPAG5; NbExp=2; IntAct=EBI-739498, EBI-413317;
CC Q9P209; Q86W54: SPATA24; NbExp=4; IntAct=EBI-739498, EBI-3916986;
CC Q9P209; Q96FJ0: STAMBPL1; NbExp=8; IntAct=EBI-739498, EBI-745021;
CC Q9P209; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-739498, EBI-16429014;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:19536135}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:26297806}. Note=Localizes to the centrosome and
CC centrosome-surrounding particles throughout the cell cycle. These
CC particles disappear after microtubules are depolymerized using
CC nocodazole, suggesting that CEP72-associating particles localize in a
CC microtubule- dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P209-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P209-2; Sequence=VSP_037835, VSP_037836;
CC -!- SIMILARITY: Belongs to the CEP72 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91685.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA96043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB040952; BAA96043.1; ALT_INIT; mRNA.
DR EMBL; AK001427; BAA91685.1; ALT_INIT; mRNA.
DR EMBL; AK299072; BAG61138.1; -; mRNA.
DR EMBL; BC000132; AAH00132.1; -; mRNA.
DR EMBL; BC001750; AAH01750.2; -; mRNA.
DR CCDS; CCDS34126.1; -. [Q9P209-1]
DR RefSeq; NP_060610.2; NM_018140.3. [Q9P209-1]
DR RefSeq; XP_011512365.1; XM_011514063.1. [Q9P209-1]
DR AlphaFoldDB; Q9P209; -.
DR SMR; Q9P209; -.
DR BioGRID; 120844; 144.
DR DIP; DIP-54272N; -.
DR IntAct; Q9P209; 103.
DR MINT; Q9P209; -.
DR STRING; 9606.ENSP00000264935; -.
DR iPTMnet; Q9P209; -.
DR PhosphoSitePlus; Q9P209; -.
DR BioMuta; CEP72; -.
DR DMDM; 62901504; -.
DR EPD; Q9P209; -.
DR jPOST; Q9P209; -.
DR MassIVE; Q9P209; -.
DR MaxQB; Q9P209; -.
DR PaxDb; Q9P209; -.
DR PeptideAtlas; Q9P209; -.
DR PRIDE; Q9P209; -.
DR ProteomicsDB; 83703; -. [Q9P209-1]
DR ProteomicsDB; 83704; -. [Q9P209-2]
DR Antibodypedia; 22247; 184 antibodies from 25 providers.
DR DNASU; 55722; -.
DR Ensembl; ENST00000264935.6; ENSP00000264935.5; ENSG00000112877.8. [Q9P209-1]
DR GeneID; 55722; -.
DR KEGG; hsa:55722; -.
DR MANE-Select; ENST00000264935.6; ENSP00000264935.5; NM_018140.4; NP_060610.2.
DR UCSC; uc003jbf.4; human. [Q9P209-1]
DR CTD; 55722; -.
DR DisGeNET; 55722; -.
DR GeneCards; CEP72; -.
DR HGNC; HGNC:25547; CEP72.
DR HPA; ENSG00000112877; Tissue enhanced (testis).
DR MIM; 616475; gene.
DR neXtProt; NX_Q9P209; -.
DR OpenTargets; ENSG00000112877; -.
DR Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA142672125; -.
DR VEuPathDB; HostDB:ENSG00000112877; -.
DR eggNOG; ENOG502QV2Y; Eukaryota.
DR GeneTree; ENSGT00530000063884; -.
DR HOGENOM; CLU_027497_0_0_1; -.
DR InParanoid; Q9P209; -.
DR OMA; KITHLGH; -.
DR OrthoDB; 881430at2759; -.
DR PhylomeDB; Q9P209; -.
DR TreeFam; TF338646; -.
DR PathwayCommons; Q9P209; -.
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; Q9P209; -.
DR BioGRID-ORCS; 55722; 9 hits in 1083 CRISPR screens.
DR ChiTaRS; CEP72; human.
DR GeneWiki; CEP72; -.
DR GenomeRNAi; 55722; -.
DR Pharos; Q9P209; Tbio.
DR PRO; PR:Q9P209; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9P209; protein.
DR Bgee; ENSG00000112877; Expressed in ventricular zone and 99 other tissues.
DR Genevisible; Q9P209; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0033566; P:gamma-tubulin complex localization; IMP:UniProtKB.
DR GO; GO:1904779; P:regulation of protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR040146; CEP72.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR23311:SF7; PTHR23311:SF7; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..647
FT /note="Centrosomal protein of 72 kDa"
FT /id="PRO_0000089499"
FT REPEAT 29..50
FT /note="LRR 1"
FT REPEAT 55..76
FT /note="LRR 2"
FT REPEAT 77..98
FT /note="LRR 3"
FT DOMAIN 111..150
FT /note="LRRCT"
FT REGION 152..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 476..620
FT /evidence="ECO:0000255"
FT COMPBIAS 231..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 172..193
FT /note="PHHPRAKCTEALAKQSLVMDAD -> IQTSVEPAVGTVPVWGLWEAGP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037835"
FT VAR_SEQ 194..647
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037836"
FT VARIANT 238
FT /note="P -> L (in dbSNP:rs869955)"
FT /id="VAR_050798"
FT VARIANT 412
FT /note="P -> T (in dbSNP:rs12522955)"
FT /id="VAR_050799"
FT VARIANT 509
FT /note="T -> A (in dbSNP:rs868649)"
FT /evidence="ECO:0000269|PubMed:10819331"
FT /id="VAR_050800"
FT CONFLICT 566
FT /note="G -> V (in Ref. 2; BAA91685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 71718 MW; 9F45C88511311460 CRC64;
MARAGPRLVL SEEAVRAKSG LGPHRDLAEL QSLSIPGTYQ EKITHLGHSL MSLTGLKSLD
LSRNSLVSLE GIQYLTALES LNLYYNCISS LAEVFRLHAL TELVDVDFRL NPVVKVEPDY
RLFVVHLLPK LQQLDDRPVR ASERKASRLH FASEDSLDSK ESVPASLKEG RPHHPRAKCT
EALAKQSLVM DADDEAVLNL IAECEWDLGR PPGSTSFSQK GREADSRGSQ ESRHLLSPQL
VQYQCGDSGK QGRETRRSSC RGCCLEKMPW SQLCGELPPL YGAEPEASRA PRPHTYFTPH
PDSMDTEDSA SSQKLDLSGE MVPGPLPAPG KCRKRRMPVG RFQTFSDQEG LGCPERTHGS
SVPKESLSRQ DSSESRNGRT LSQPEASETE EQRSRGVTDT REPSPGSHSA LPGKKTALQA
ALLETLLDLV DRSWGGCRSL HSNEAFLAQA RHILSSVEEF TAAQDSSAMV GEDVGSLALE
SKSLQSRLAE QQQQHAREMS EVTAELHHTH KELDDLRQHL DKSLEENSRL KSLLLSMKKE
VKSADTAATL NLQIAGLQTS VKRLCGEIVE LKQHLEHYDK IQELTQMLQE SHSSLVSTNE
HLLQELSQVR AQHRAEVEQM HWSYQELKKT MALFPHSSAS HGGCQAC
