TTC3_MOUSE
ID TTC3_MOUSE Reviewed; 1979 AA.
AC O88196; Q05D15; Q3TMM9; Q3TPC8; Q3TPV5; Q3TQL0; Q3TSK0; Q3UFH5; Q5DTM5;
AC Q6PG61; Q8BPM4; Q8C2N6;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase TTC3;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P53804};
DE AltName: Full=RING-type E3 ubiquitin transferase TTC3 {ECO:0000305};
DE AltName: Full=TPR repeat protein D;
DE Short=Mtprd;
GN Name=Ttc3; Synonyms=Kiaa4119;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9603993; DOI=10.1093/oxfordjournals.jbchem.a022043;
RA Tsukahara F., Urakawa I., Hattori M., Hirai M., Ohba K., Yoshioka T.,
RA Sakaki Y., Muraki T.;
RT "Molecular characterization of the mouse mtprd gene, a homologue of human
RT TPRD: unique gene expression suggesting its critical role in the
RT pathophysiology of Down syndrome.";
RL J. Biochem. 123:1055-1063(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1194 AND 1423-1979 (ISOFORMS 4
RP AND 5), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1116-1874 (ISOFORM
RP 6).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpora quadrigemina, Eye, Heart, Lung, Pancreas, Spinal cord,
RC Thymus, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1178 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1181 (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N-3, and NMRI; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009; SER-1060 AND SER-1794,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which catalyzes the formation of
CC 'Lys-48'-polyubiquitin chains (By similarity). Mediates the
CC ubiquitination and subsequent degradation of phosphorylated Akt (AKT1,
CC AKT2 and AKT3) in the nucleus (By similarity). Acts as a terminal
CC regulator of Akt signaling after activation; its phosphorylation by
CC Akt, which is a prerequisite for ubiquitin ligase activity, suggests
CC the existence of a regulation mechanism required to control Akt levels
CC after activation (By similarity). Positively regulates TGFB1-induced
CC epithelial-mesenchymal transition and myofibroblast differentiation by
CC mediating the ubiquitination and subsequent degradation of SMURF2 (By
CC similarity). Regulates neuronal differentiation by regulating actin
CC remodeling and Golgi organization via a signaling cascade involving
CC RHOA, CIT and ROCK (By similarity). Inhibits cell proliferation (By
CC similarity). {ECO:0000250|UniProtKB:P53804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P53804};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P53804}.
CC -!- SUBUNIT: Interacts (when phosphorylated on Ser-378) with AKT1, AKT2 and
CC AKT3 (when phosphorylated) (By similarity). Interacts with CIT (By
CC similarity). Interacts with POLG (By similarity). Interacts with HSP70
CC (By similarity). Interacts with SMURF2 (By similarity).
CC {ECO:0000250|UniProtKB:P53804}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53804}. Cytoplasm
CC {ECO:0000250|UniProtKB:P53804}. Golgi apparatus
CC {ECO:0000250|UniProtKB:D3ZSP7}. Note=Nuclear localization may be
CC dependent on the proteolytic cleavage of full length protein in the
CC cytoplasm (By similarity). This cleavage may reveal an N-terminal
CC nuclear localization signal, allowing N-terminal fragments to enter the
CC nucleus (By similarity). {ECO:0000250|UniProtKB:P53804}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O88196-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88196-2; Sequence=VSP_038776;
CC Name=3;
CC IsoId=O88196-3; Sequence=VSP_038775;
CC Name=4;
CC IsoId=O88196-4; Sequence=VSP_038775, VSP_038776, VSP_038777;
CC Name=5;
CC IsoId=O88196-5; Sequence=VSP_038774;
CC Name=6;
CC IsoId=O88196-6; Sequence=VSP_038778;
CC -!- PTM: Phosphorylation on Ser-378 by Akt is required for ubiquitin ligase
CC activity. {ECO:0000250|UniProtKB:P53804}.
CC -!- PTM: Proteolytically cleaved into differently sized N- and C-terminal
CC fragments. {ECO:0000250|UniProtKB:P53804}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19173.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH57207.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC35513.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD90293.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE28586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB008516; BAA31563.1; -; mRNA.
DR EMBL; AK053765; BAC35513.1; ALT_INIT; mRNA.
DR EMBL; AK088273; BAC40250.1; -; mRNA.
DR EMBL; AK162004; BAE36675.1; -; mRNA.
DR EMBL; AK163496; BAE37372.1; -; mRNA.
DR EMBL; AK164106; BAE37630.1; -; mRNA.
DR EMBL; AK164492; BAE37809.1; -; mRNA.
DR EMBL; AK165850; BAE38412.1; -; mRNA.
DR EMBL; AK148494; BAE28586.1; ALT_INIT; mRNA.
DR EMBL; AK220495; BAD90293.1; ALT_INIT; mRNA.
DR EMBL; BC019173; AAH19173.1; ALT_SEQ; mRNA.
DR EMBL; BC057207; AAH57207.1; ALT_SEQ; mRNA.
DR CCDS; CCDS37407.1; -. [O88196-1]
DR PIR; JW0059; JW0059.
DR AlphaFoldDB; O88196; -.
DR SMR; O88196; -.
DR IntAct; O88196; 4.
DR MINT; O88196; -.
DR STRING; 10090.ENSMUSP00000112801; -.
DR GlyConnect; 2272; 1 N-Linked glycan (1 site).
DR GlyGen; O88196; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; O88196; -.
DR PhosphoSitePlus; O88196; -.
DR EPD; O88196; -.
DR jPOST; O88196; -.
DR MaxQB; O88196; -.
DR PaxDb; O88196; -.
DR PeptideAtlas; O88196; -.
DR PRIDE; O88196; -.
DR ProteomicsDB; 300150; -. [O88196-1]
DR ProteomicsDB; 300151; -. [O88196-2]
DR ProteomicsDB; 300152; -. [O88196-3]
DR ProteomicsDB; 300153; -. [O88196-4]
DR ProteomicsDB; 300154; -. [O88196-5]
DR ProteomicsDB; 300155; -. [O88196-6]
DR UCSC; uc008aau.1; mouse. [O88196-2]
DR UCSC; uc008aaw.1; mouse. [O88196-3]
DR UCSC; uc008aax.1; mouse. [O88196-4]
DR UCSC; uc012aiu.1; mouse. [O88196-1]
DR MGI; MGI:1276539; Ttc3.
DR eggNOG; KOG0800; Eukaryota.
DR InParanoid; O88196; -.
DR PhylomeDB; O88196; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; Ttc3; mouse.
DR PRO; PR:O88196; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88196; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005773; C:vacuole; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0010771; P:negative regulation of cell morphogenesis involved in differentiation; IDA:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR043866; TTC3/DZIP3_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF19179; DUF5861; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Golgi apparatus; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1979
FT /note="E3 ubiquitin-protein ligase TTC3"
FT /id="PRO_0000392034"
FT REPEAT 231..264
FT /note="TPR 1"
FT REPEAT 266..298
FT /note="TPR 2"
FT REPEAT 536..572
FT /note="TPR 3"
FT REPEAT 576..609
FT /note="TPR 4"
FT ZN_FING 1931..1971
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..230
FT /note="Interaction with POLG"
FT /evidence="ECO:0000250|UniProtKB:P53804"
FT REGION 422..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53804"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..401
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038774"
FT VAR_SEQ 143..160
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_038775"
FT VAR_SEQ 1056
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_038776"
FT VAR_SEQ 1089..1110
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038777"
FT VAR_SEQ 1593
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038778"
FT CONFLICT 94
FT /note="L -> P (in Ref. 1; BAA31563)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="F -> S (in Ref. 1; BAC35513/BAE38412)"
FT /evidence="ECO:0000305"
FT CONFLICT 1164
FT /note="I -> F (in Ref. 1; BAE37809)"
FT /evidence="ECO:0000305"
FT CONFLICT 1177
FT /note="L -> P (in Ref. 1; BAC40250)"
FT /evidence="ECO:0000305"
FT CONFLICT 1522
FT /note="N -> S (in Ref. 1; BAE36675)"
FT /evidence="ECO:0000305"
FT CONFLICT 1571
FT /note="S -> P (in Ref. 1; BAE36675/BAE37630/BAE37809)"
FT /evidence="ECO:0000305"
FT CONFLICT 1603
FT /note="A -> V (in Ref. 1; BAE36675/BAE37630/BAE37809)"
FT /evidence="ECO:0000305"
FT CONFLICT 1822
FT /note="N -> S (in Ref. 1; BAE36675)"
FT /evidence="ECO:0000305"
FT CONFLICT 1847
FT /note="V -> F (in Ref. 1; BAE36675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1979 AA; 223931 MW; 63A93E3CA1CECF00 CRC64;
MDDFAEGGLS LADDILLEDY PYEDDCICTP DFTTDDYVRV TQLYYEGVGM QYKDYAQSEK
NLEYDICNIW CSKPLSILQD YCDAIKLYIF WPLLFQHQHS SIISRLHPCV EAIRSRAAEI
SLKKLQHLEL MEDIVDLAKK VANDSFLIEG LLKIGYKIEN KILAMEDALN WIKYTGDVTI
LPKLGSVDNC WPMLSIFFTE YKYHITRVVT ENCNLLEEFR RHSCMQCVKQ GELMKMRGNE
EFSKEKFEIA VIYYTRAIEY RPENHLLYGN RALCFLRMGQ FRNALSDGKR AIVLKNTWPK
GHYRYCDALC MLGEYDWALQ ANIKAQKLCK NDPEGIKDLI QQHVKLQKQI EDLQGRTSNK
NPIKAFYESR AYIPRNSSAP AFRTSLNFVE TERGFRKTKY KMANGGDQNQ KVADEALKGD
DCDCHPEFLP PPSQPPRHKG KQKSRNNESE KPSFNSEVSL QVDLKSILEK QFSKSSRAAH
QDFANIMKML RSLIQDGYTA LLEQRCRSAA QAFTELLNGL DPQKIKQLNL AMINYVLVVY
GLAVSLLGIG RPEELSEAEN QFKRIIEHYP NEGLDCLAYC GIGKVYLKKN RFLEALNHFE
KAKTLISRLP GILTWPTSNV IIEESKPEKV KVMLEKFVEE CKFPPVPDAV CCYQKCRGYS
KIQIYLTDPD FKGFIRISCC QYCKVEFHMN CWKKLKTTTF NDKIDKDFLQ GICLTPDCEG
IISKIIIYSS GGQVKCEFEH KVIKEKVPSR PVLKQKCSSL EKLRLKEDKK LKRKIQKQEA
KKLAQERMEE DLRESNPPKN EEPEETSDSA QRCQFLDDRI LQCIKQNADK IKSVVLNTST
LLKELLSWKV LSTEDYTTCF SSKNFVHEAV DYVIGHLIQE KNRVKTRIFL HVLSELKELD
PKLAPWIQRL NSFGLDAIGP FFTRYGASLK ELDFHVVTVL WDEKYGHKLG SIEGKQLDYF
FEPASAMEAR CLIWLLEEHR DKFPALHSAL DEFFDIMDSR CTVLRKQDSD EMPFGCIKVK
NKGKKKKPKD SKPMLVGSGA ASVAPSSEAV TPEDHSRRNS DSAGPFAVPD HLRQDVEEFE
ALYDQHSSEY VVRNKKLWDI NPKQKCSTLY DYFSQLLEEH GPLDMSDRMF SEEYEFFPEE
TRQILEKAGG LKSFLLGCPR FVVIDNCIAL KKVASRLKKK RKKKNMKAKV EDISKTGEYL
RVKLPLNPTA REFQPDVKSE ALSEDVKSIP GPADSSTLAA EDLKAQLDSD SSSGSASEDS
RLEVASPDSP TPLCEDASPS PTPAPEEAKP TYWAQSHLVT GFCTYLPFQG FGITQRPAYI
NMVPSLSQFT SIYTPLANIS SEYPMQRSMP VVPSFVASNR ADENAAAYFE SPNLNTEHDS
GDHMASETQI LEDTLGVCVR SQGSAADADP ALSEPEGNSE HSGSSDSLWE ASLENVSGTT
DAPAAPSVAI QVSRSMVHQE VNTEPYEPFE TQQGDLSQKE KECHLLREQL KVACENCEQI
ELRSSQEIKD LEEKLQRHTE ENKISKTELD WFLQDLDREI KKWQQEKKEI QERLKALKKK
IKKVINTSEM SAQKNDGFDK ECEPHPDQSL GFSSALTDEK TKAEESVRKG KELYEESHQR
AVAAEVSVLE NWKEREVCKL QGVASQSEAY LKSLKLMSSD SATYPDVEYD ILSWESFLST
VREEIESKKS QFEEHIKAIK NGSRLSDLSS VQLSEVSFPG CSTIHPQFLS ESSGHEDPGL
VACVDSMTGA VLNDPYMDSA SGCPEEVPEL SLGSPTHQPE VTQQLELKGA SQVSPSEQSP
EADEKLSGQA TRSSQSPKKP SNSIIEHLSV IFPCYTSTEL AGFIKKVRNK TKNSFSGLTI
EEIVEKVTEH IVDEQKKKKP NPGKDKKTSE AHSAASVAKS SQSPPLAAAG PSARTKGQKK
DDVPAPDGNS CEICHEIFKS KNMRVLKCGH KFHKGCFKQW LKGQSTCPTC GSSDLLSEE
