MPP9_HUMAN
ID MPP9_HUMAN Reviewed; 1031 AA.
AC Q99550; A0A0A0MTP3; A1L486; A6NEE2; B3KR87; Q9H976; U3KQ28;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 5.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=M-phase phosphoprotein 9;
GN Name=MPHOSPH9; Synonyms=MPP9;
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 SER-125.
RC TISSUE=Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 815-1031 (ISOFORM 2), SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION.
RC TISSUE=Lymphoblast;
RX PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
RA Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression cloning.";
RL Mol. Biol. Cell 7:1455-1469(1996).
RN [6]
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 [7]
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21399614; DOI=10.1038/emboj.2011.63;
RA Jakobsen L., Vanselow K., Skogs M., Toyoda Y., Lundberg E., Poser I.,
RA Falkenby L.G., Bennetzen M., Westendorf J., Nigg E.A., Uhlen M.,
RA Hyman A.A., Andersen J.S.;
RT "Novel asymmetrically localizing components of human centrosomes identified
RT by complementary proteomics methods.";
RL EMBO J. 30:1520-1535(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-842, AND IDENTIFICATION BY
RP 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCP110; CEP97 AND KIF24,
RP PHOSPHORYLATION AT SER-629 AND SER-636, UBIQUITINATION AT LYS-632, AND
RP MUTAGENESIS OF SER-629; LYS-632 AND SER-636.
RX PubMed=30375385; DOI=10.1038/s41467-018-06990-9;
RA Huang N., Zhang D., Li F., Chai P., Wang S., Teng J., Chen J.;
RT "M-Phase Phosphoprotein 9 regulates ciliogenesis by modulating CP110-CEP97
RT complex localization at the mother centriole.";
RL Nat. Commun. 9:4511-4511(2018).
CC -!- FUNCTION: Negatively regulates cilia formation by recruiting the CP110-
CC CEP97 complex (a negative regulator of ciliogenesis) at the distal end
CC of the mother centriole in ciliary cells (PubMed:30375385). At the
CC beginning of cilia formation, MPHOSPH9 undergoes TTBK2-mediated
CC phosphorylation and degradation via the ubiquitin-proteasome system and
CC removes itself and the CP110-CEP97 complex from the distal end of the
CC mother centriole, which subsequently promotes cilia formation
CC (PubMed:30375385). {ECO:0000269|PubMed:30375385}.
CC -!- SUBUNIT: Interacts with CCP110, CEP97 and KIF24.
CC {ECO:0000269|PubMed:30375385}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:21399614,
CC ECO:0000269|PubMed:30375385}. Golgi apparatus membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:30375385}. Note=Localizes to the distal and
CC proximal end of centriole pairs in duplicated centrosomes. In ciliated
CC cells, localizes to the distal and proximal end of daughter centriole
CC and proximal of the mother centriole but not in the distal end of the
CC mother centriole (PubMed:21399614). Recruited by KIF24 to the distal
CC end of mother centriole where it forms a ring-like structure
CC (PubMed:30375385). {ECO:0000269|PubMed:21399614,
CC ECO:0000269|PubMed:30375385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99550-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99550-2; Sequence=VSP_035838;
CC -!- PTM: TTBK2-mediated phosphorylation at Ser-629 and Ser-636, promotes
CC its ubiquitination at Lys-632 leading to proteasomal degradation, loss
CC of MPHOSPH9 facilitates the removal of the CP110-CEP97 complex from the
CC mother centrioles, promoting the initiation of ciliogenesis
CC (PubMed:30375385). Phosphorylated in M (mitotic) phase
CC (PubMed:8885239). {ECO:0000269|PubMed:30375385,
CC ECO:0000269|PubMed:8885239}.
CC -!- PTM: Ubiquitinated at Lys-632, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:30375385}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW98392.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK023016; BAB14359.1; -; mRNA.
DR EMBL; AK091181; BAG52299.1; -; mRNA.
DR EMBL; AC073857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98392.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471054; EAW98394.1; -; Genomic_DNA.
DR EMBL; BC130440; AAI30441.1; -; mRNA.
DR EMBL; X98258; CAA66911.1; -; mRNA.
DR RefSeq; NP_073619.3; NM_022782.3. [Q99550-1]
DR RefSeq; XP_016874162.1; XM_017018673.1. [Q99550-1]
DR RefSeq; XP_016874168.1; XM_017018679.1.
DR RefSeq; XP_016874169.1; XM_017018680.1.
DR AlphaFoldDB; Q99550; -.
DR BioGRID; 115493; 87.
DR IntAct; Q99550; 34.
DR MINT; Q99550; -.
DR STRING; 9606.ENSP00000475489; -.
DR iPTMnet; Q99550; -.
DR PhosphoSitePlus; Q99550; -.
DR BioMuta; MPHOSPH9; -.
DR DMDM; 215274134; -.
DR EPD; Q99550; -.
DR jPOST; Q99550; -.
DR MassIVE; Q99550; -.
DR PaxDb; Q99550; -.
DR PeptideAtlas; Q99550; -.
DR PRIDE; Q99550; -.
DR ProteomicsDB; 78323; -. [Q99550-1]
DR ProteomicsDB; 78324; -. [Q99550-2]
DR Antibodypedia; 31757; 175 antibodies from 24 providers.
DR DNASU; 10198; -.
DR Ensembl; ENST00000606320.6; ENSP00000475489.1; ENSG00000051825.15.
DR GeneID; 10198; -.
DR KEGG; hsa:10198; -.
DR UCSC; uc001uel.5; human. [Q99550-1]
DR UCSC; uc058uri.1; human.
DR CTD; 10198; -.
DR DisGeNET; 10198; -.
DR GeneCards; MPHOSPH9; -.
DR HGNC; HGNC:7215; MPHOSPH9.
DR HPA; ENSG00000051825; Low tissue specificity.
DR MIM; 605501; gene.
DR neXtProt; NX_Q99550; -.
DR PharmGKB; PA30921; -.
DR VEuPathDB; HostDB:ENSG00000051825; -.
DR eggNOG; KOG4713; Eukaryota.
DR HOGENOM; CLU_008784_0_0_1; -.
DR InParanoid; Q99550; -.
DR OMA; NKQMPDQ; -.
DR OrthoDB; 572984at2759; -.
DR PhylomeDB; Q99550; -.
DR TreeFam; TF336168; -.
DR PathwayCommons; Q99550; -.
DR SignaLink; Q99550; -.
DR SIGNOR; Q99550; -.
DR BioGRID-ORCS; 10198; 4 hits in 946 CRISPR screens.
DR ChiTaRS; MPHOSPH9; human.
DR GenomeRNAi; 10198; -.
DR Pharos; Q99550; Tbio.
DR PRO; PR:Q99550; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q99550; protein.
DR Bgee; ENSG00000051825; Expressed in ventricular zone and 154 other tissues.
DR ExpressionAtlas; Q99550; baseline and differential.
DR Genevisible; Q99550; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR InterPro; IPR026636; MPHOSPH9.
DR PANTHER; PTHR14926; PTHR14926; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1031
FT /note="M-phase phosphoprotein 9"
FT /id="PRO_0000096557"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..648
FT /note="Required for its centrosomal localization"
FT /evidence="ECO:0000269|PubMed:30375385"
FT REGION 299..348
FT /note="Interaction with CEP97"
FT /evidence="ECO:0000269|PubMed:30375385"
FT REGION 321..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..879
FT /note="Interaction with KIF24"
FT /evidence="ECO:0000269|PubMed:30375385"
FT REGION 711..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..652
FT /evidence="ECO:0000255"
FT COILED 957..1022
FT /evidence="ECO:0000255"
FT COMPBIAS 153..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 629
FT /note="Phosphoserine; by TTBK2"
FT /evidence="ECO:0000269|PubMed:30375385"
FT MOD_RES 636
FT /note="Phosphoserine; by TTBK2"
FT /evidence="ECO:0000269|PubMed:30375385"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 632
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:30375385"
FT VAR_SEQ 999..1031
FT /note="EALEDRLERINRELGSVRMTLKKFHVLRTSANL -> TPQICEESSHKCAFA
FT GHYVPCHLYDYRFQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8885239"
FT /id="VSP_035838"
FT VARIANT 125
FT /note="G -> S (in dbSNP:rs36121382)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_047643"
FT VARIANT 926
FT /note="A -> D (in dbSNP:rs1260318)"
FT /id="VAR_047644"
FT MUTAGEN 629
FT /note="S->A: Loss of phosphorylation and localization at
FT distal ends of the mother centriole. Significant decrease
FT in ubiquitination; when associated with A-636."
FT /evidence="ECO:0000269|PubMed:30375385"
FT MUTAGEN 632
FT /note="K->A: Decreased ubiquitination and increased protein
FT stability."
FT /evidence="ECO:0000269|PubMed:30375385"
FT MUTAGEN 636
FT /note="S->A: Reduced phosphorylation. Significant decrease
FT in ubiquitination; when associated with A-629."
FT /evidence="ECO:0000269|PubMed:30375385"
FT CONFLICT 795
FT /note="K -> E (in Ref. 1; BAB14359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1031 AA; 116134 MW; 974A6471D286FDB1 CRC64;
MGFFSLSSER NESVIHYPES TEPEIQQEMS TSQPDCNVDS CSVSSGYGTF CISELNLYKS
KDPKEFMEHI DVPKGQYVAP AVPAESLVDG VKNENFYIQT PEECHVSLKE DVSISPGEFE
HNFLGENKVS EVYSGKTNSN AITSWAQKLK QNQPKRAHVE DGGSRSKQGN EQSKKTPIEK
SDFAAATHPR AFYLSKPDET PNAWMSDSGT GLTYWKLEEK DMHHSLPETL EKTFISLSST
DVSPNQSNTS NEMKLPSLKD IYYKKQRENK QLPERNLTSA SNPNHPPEVL TLDPTLHMKP
KQQISGIQPH GLPNALDDRI SFSPDSVLEP SMSSPSDIDS FSQASNVTSQ LPGFPKYPSH
TKASPVDSWK NQTFQNESRT SSTFPSVYTI TSNDISVNTV DEENTVMVAS ASVSQSQLPG
TANSVPECIS LTSLEDPVIL SKIRQNLKEK HARHIADLRA YYESEINSLK QKLEAKEISG
VEDWKITNQI LVDRCGQLDS ALHEATSRVR TLENKNNLLE IEVNDLRERF SAASSASKIL
QERIEEMRTS SKEKDNTIIR LKSRLQDLEE AFENAYKLSD DKEAQLKQEN KMFQDLLGEY
ESLGKEHRRV KDALNTTENK LLDAYTQISD LKRMISKLEA QVKQVEHENM LSLRHNSRIH
VRPSRANTLA TSDVSRRKWL IPGAEYSIFT GQPLDTQDSN VDNQLEETCS LGHRSPLEKD
SSPGSSSTSL LIKKQRETSD TPIMRALKEL DEGKIFKNWG TQTEKEDTSN INPRQTETSV
NASRSPEKCA QQRQKRLNSA SQRSSSLPPS NRKSSTPTKR EIMLTPVTVA YSPKRSPKEN
LSPGFSHLLS KNESSPIRFD ILLDDLDTVP VSTLQRTNPR KQLQFLPLDD SEEKTYSEKA
TDNHVNHSSC PEPVPNGVKK VSVRTAWEKN KSVSYEQCKP VSVTPQGNDF EYTAKIRTLA
ETERFFDELT KEKDQIEAAL SRMPSPGGRI TLQTRLNQEA LEDRLERINR ELGSVRMTLK
KFHVLRTSAN L
