ARIP4_MOUSE
ID ARIP4_MOUSE Reviewed; 1466 AA.
AC Q99NG0; Q3UPJ1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Helicase ARIP4;
DE EC=3.6.4.12;
DE AltName: Full=Androgen receptor-interacting protein 4;
DE AltName: Full=RAD54-like protein 2;
DE AltName: Full=Steroid receptor-interacting SNF2 domain-containing protein-like;
GN Name=Rad54l2; Synonyms=Arip4, Srisnf2l;
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], FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING,
RP INTERACTION WITH AR, AND MUTAGENESIS OF LYS-310 AND 462-ASP-GLU-463.
RC STRAIN=Swiss Webster; TISSUE=Embryo;
RX PubMed=12058073; DOI=10.1091/mbc.01-10-0484.;
RA Rouleau N., Domans'kyi A., Reeben M., Moilanen A.-M., Havas K., Kang Z.,
RA Owen-Hughes T., Palvimo J.J., Jaenne O.A.;
RT "Novel ATPase of SNF2-like protein family interacts with androgen receptor
RT and modulates androgen-dependent transcription.";
RL Mol. Biol. Cell 13:2106-2119(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 33-1466.
RC STRAIN=C57BL/6J;
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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH DYRK1A.
RX PubMed=15199138; DOI=10.1128/mcb.24.13.5821-5834.2004;
RA Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.;
RT "Dyrk1A potentiates steroid hormone-induced transcription via the chromatin
RT remodeling factor Arip4.";
RL Mol. Cell. Biol. 24:5821-5834(2004).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, INTERACTION
RP WITH AR, SUMOYLATION, AND MUTAGENESIS OF LYS-361; LYS-573; LYS-664;
RP LYS-935; LYS-961 AND LYS-1013.
RX PubMed=16212558; DOI=10.1042/bj20050823;
RA Domanskyi A., Virtanen K.T., Palvimo J.J., Jaenne O.A.;
RT "Biochemical characterization of androgen receptor-interacting protein 4.";
RL Biochem. J. 393:789-795(2006).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17003240; DOI=10.1152/ajpendo.00287.2006;
RA Domanskyi A., Zhang F.-P., Nurmio M., Palvimo J.J., Toppari J.,
RA Jaenne O.A.;
RT "Expression and localization of androgen receptor-interacting protein-4 in
RT the testis.";
RL Am. J. Physiol. 292:E513-E522(2007).
RN [7]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17374848; DOI=10.1210/me.2007-0052;
RA Zhang F.-P., Domanskyi A., Palvimo J.J., Sariola H., Partanen J.,
RA Jaenne O.A.;
RT "An adenosine triphosphatase of the sucrose nonfermenting 2 family,
RT androgen receptor-interacting protein 4, is essential for mouse embryonic
RT development and cell proliferation.";
RL Mol. Endocrinol. 21:1430-1442(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1168 AND SER-1171, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Spleen, and Testis;
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: DNA helicase that modulates androgen receptor (AR)-dependent
CC transactivation in a promoter-dependent manner. Not able to remodel
CC mononucleosomes in vitro. Acts as an AR-coregulator in Sertoli cells.
CC {ECO:0000269|PubMed:12058073, ECO:0000269|PubMed:16212558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- ACTIVITY REGULATION: Enzyme activity is enhanced by dsDNA (double-
CC stranded DNA) and ssDNA (single-stranded DNA).
CC {ECO:0000269|PubMed:16212558}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 nM for DNA {ECO:0000269|PubMed:16212558};
CC KM=25 uM for ATP {ECO:0000269|PubMed:16212558};
CC -!- SUBUNIT: Interacts with AR via its N-terminus. Interacts with DYRK1A.
CC Binds DNA and mononucleosomes, but does not seem to form large
CC multiprotein complexes. {ECO:0000269|PubMed:12058073,
CC ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:16212558}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12058073,
CC ECO:0000269|PubMed:15199138}. Note=Localizes in speckle-like nuclear
CC compartments.
CC -!- TISSUE SPECIFICITY: Expressed at relatively low level, with highest
CC expression in testis, liver and kidney. In brain, it is expressed in
CC hippocampal and cerebellar neurons. In testis, it is present at high
CC level in Sertoli cell nuclei. Also present in Leydig cell (at protein
CC level). {ECO:0000269|PubMed:15199138, ECO:0000269|PubMed:17003240}.
CC -!- DEVELOPMENTAL STAGE: Mainly expressed in the neural tube and limb buds
CC during early embryonic development. Also present in testis: at the
CC onset of spermatogenesis, it is expressed in spermatogonia, pachytene,
CC and diplotene spermatocytes. In Sertoli cells it is expressed in a
CC stage-dependent manner, with high expression levels at stages II-VI and
CC VII-VIII. {ECO:0000269|PubMed:17003240, ECO:0000269|PubMed:17374848}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be important
CC for the association with nuclear receptors. {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:16212558}.
CC -!- DISRUPTION PHENOTYPE: Death by 11.5 dpc. At 9.5 dpc and 10.5 dpc,
CC almost all major tissues are proportionally smaller, and the neural
CC tube is shrunk in some embryos. Dramatically reduced cell proliferation
CC and increased apoptosis are observed in 9.5 dpc and 10.5 dpc embryos.
CC Embryonic fibroblasts stop to grow after 2 or 3 passages and exhibit
CC increased apoptosis and decreased DNA synthesis compared with wild-
CC type. {ECO:0000269|PubMed:17374848}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {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; AJ132389; CAC24703.1; -; mRNA.
DR EMBL; BC133714; AAI33715.1; -; mRNA.
DR EMBL; AK143506; BAE25404.1; -; mRNA.
DR RefSeq; NP_109655.2; NM_030730.2.
DR AlphaFoldDB; Q99NG0; -.
DR SMR; Q99NG0; -.
DR BioGRID; 219861; 1.
DR IntAct; Q99NG0; 1.
DR STRING; 10090.ENSMUSP00000045454; -.
DR iPTMnet; Q99NG0; -.
DR PhosphoSitePlus; Q99NG0; -.
DR EPD; Q99NG0; -.
DR jPOST; Q99NG0; -.
DR MaxQB; Q99NG0; -.
DR PaxDb; Q99NG0; -.
DR PRIDE; Q99NG0; -.
DR ProteomicsDB; 265099; -.
DR DNASU; 81000; -.
DR GeneID; 81000; -.
DR KEGG; mmu:81000; -.
DR CTD; 23132; -.
DR MGI; MGI:1933196; Rad54l2.
DR eggNOG; KOG1016; Eukaryota.
DR InParanoid; Q99NG0; -.
DR OrthoDB; 815681at2759; -.
DR PhylomeDB; Q99NG0; -.
DR BioGRID-ORCS; 81000; 14 hits in 74 CRISPR screens.
DR ChiTaRS; Rad54l2; mouse.
DR PRO; PR:Q99NG0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99NG0; protein.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0019901; F:protein kinase binding; IPI:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR CDD; cd18069; DEXHc_ARIP4; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR044573; ARIP4_DEXHc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45797; PTHR45797; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1466
FT /note="Helicase ARIP4"
FT /id="PRO_0000315782"
FT DOMAIN 291..511
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 727..895
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 462..465
FT /note="DEAH box"
FT MOTIF 550..554
FT /note="LXXLL motif 1"
FT MOTIF 1328..1332
FT /note="LXXLL motif 2"
FT COMPBIAS 9..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 681
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 758
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 900
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 1013
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT CROSSLNK 1017
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B4"
FT MUTAGEN 310
FT /note="K->A: Abolishes ATP-binding."
FT /evidence="ECO:0000269|PubMed:12058073"
FT MUTAGEN 361
FT /note="K->E: Decreased sumoylation; when associated with E-
FT 573; E-664; E-935; E-961 and E-1013."
FT /evidence="ECO:0000269|PubMed:16212558"
FT MUTAGEN 462..463
FT /note="DE->AA: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:12058073"
FT MUTAGEN 573
FT /note="K->E: Decreased sumoylation; when associated with E-
FT 361; E-664; E-935; E-961 and E-1013."
FT /evidence="ECO:0000269|PubMed:16212558"
FT MUTAGEN 664
FT /note="K->E: Decreased sumoylation; when associated with E-
FT 361; E-573; E-935; E-961 and E-1013."
FT /evidence="ECO:0000269|PubMed:16212558"
FT MUTAGEN 935
FT /note="K->E: Decreased sumoylation; when associated with E-
FT 361; E-573; E-664; E-961 and E-1013."
FT /evidence="ECO:0000269|PubMed:16212558"
FT MUTAGEN 961
FT /note="K->E: Decreased sumoylation; when associated with E-
FT 361; E-573; E-664; E-935 and E-1013."
FT /evidence="ECO:0000269|PubMed:16212558"
FT MUTAGEN 1013
FT /note="K->E: Decreased sumoylation; when associated with E-
FT 361; E-573; E-664; E-935 and E-961."
FT /evidence="ECO:0000269|PubMed:16212558"
FT CONFLICT 1197
FT /note="I -> V (in Ref. 3; BAE25404)"
FT /evidence="ECO:0000305"
FT CONFLICT 1267
FT /note="I -> V (in Ref. 3; BAE25404)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1466 AA; 162540 MW; D5945AD802B03D12 CRC64;
MSDESASGSD PDLDPDVELE DEEEEEEEEE VAVEEHDRDD EEGLLDDTSL EGMCGTEHAQ
LGEDGQRPPR CTSTTSSQSE PSEQLRHQGK ILASEDPKKK RAQKPSHMRR NIRKLLREDQ
LEPVTKAAQQ EELERRKRLE QQRKEYAAPI PTVPLEFLPE EIVLRASDGP QLPPRVLAQE
VICLDSSSGS EDEKSSRDEV IELSSGEEDT LHIVDSSESV SEEDEEEEKG GTHVNDALNQ
HDALGRVLVN LNHPPEEENV FLAPQLARAV KPHQIGGIRF LYDNLVESLE RFKTSSGFGC
ILAHSMGLGK TLQVISFIDV LFRHTPAKTV LAIVPVNTLQ NWLAEFNMWL PAPEALPADS
KPEEVQPRFF KVHILNDEHK TVASRAKVTA DWVSEGGVLL MGYEMYRLLT LKKSLATSRP
KKTKKRSHPV IIDLDEEDRQ QEFRREFEKA LCRPGPDVVI CDEGHRIKNC QASTSQALKN
IRSRRRVVLT GYPLQNNLIE YWCMVDFVRP DFLGTRQEFS NMFERPILNG QCIDSTPQDV
RLMRYRSHVL HSLLEGFVQR RGHTVLKIHL PAKEENVILV RLSQIQRDLY TQFMDRFRDC
GTSGWLGLNP LKAFCVCCKI WNHPDVLYEA LQKENLANEQ DLDVEELGSA GTSARCPPHG
TKVKGEDSAL PSSMGEATNS KFLQGVGFNP FQERGNNIVT YEWAKELLTN YQTGVLENSP
KMVLLFHLIE ESVKLGDKIL VFSQSLSTLA LIEEFLGKRD MPCLPGAEGQ GTQKWVRNVS
YFRLDGSTPA FERERLINQF NDPSNLTTWL FLLSTRAGCL GVNLIGANRV VVFDASWNPC
HDAQAVCRVY RYGQKKPCHI YRLVADYTLE KKIYDRQISK QGMSDRVVDD LNPMLNFTRK
EVENLLHFVE KEPAPQTSLD IKGIKESVLQ LACLKYPHLI TKEPFEHESL LLNRKDHKLT
KAEKKAAKKS YEEDKRTSVP YTRPSYAQYY PASDQSLTSI PAFSQRNWQP TLKGDEKPVA
SVRPVQSTPI PMMPRHVPLS GGVSSASSTN TSMNFPINYL QRAGVLVQKV VTTTDIVIPG
LNSSTDVQAR INAGESIHII RGTKGTYIRT SDGRIFAVRA TGKPKAPEDG RMAASGSQGP
SLASTSNGRH SASSPKAPDP EGLARPVSPD SPEIISELQQ YADVAAARES RQSSPSISAA
LPGPPGQLMD NSTIPGTALG TEPCLGGHCL NSSLLVTGQP SGGRHPVLDL RGHKRKLATP
SVTQESIRRR SRKGHLPAPV QPYEHGYPVS GGFAMPPVSL NHNLTTPFTS QAGENSLFMG
SNPSYYQLSN LLADARLVFP VTTDPLVPAG PVSSSSTATS VTASNPSFML NPSVPGMLPS
YSLPFSQPLL SEPRMFAPFP SPGLPSNLSR GVSVYPGYMS PHAGYPAGGL LRSQVPPFDS
HEVAEVGFSS NDDEDKDDDV IEVTGK
