KS6C1_MOUSE
ID KS6C1_MOUSE Reviewed; 1056 AA.
AC Q8BLK9; Q3UDY3; Q6PDY4; Q8BMQ5; Q8BX49;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ribosomal protein S6 kinase delta-1;
DE Short=S6K-delta-1;
DE EC=2.7.11.1;
DE AltName: Full=52 kDa ribosomal protein S6 kinase;
GN Name=Rps6kc1;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-1056 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, Ovary, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 436-1056 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Cerebellum;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-426 AND SER-599, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-426; SER-446;
RP SER-448; SER-493; SER-599; SER-602; SER-634; SER-661 AND SER-787, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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: May be involved in transmitting sphingosine-1 phosphate
CC (SPP)-mediated signaling into the cell. Plays a role in the recruitment
CC of PRDX3 to early endosomes. {ECO:0000250|UniProtKB:Q96S38}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with SPHK1 and phosphatidylinositol 3-phosphate.
CC Interacts (via PX domain) with PRDX3. {ECO:0000250|UniProtKB:Q96S38}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96S38}.
CC Membrane {ECO:0000250|UniProtKB:Q96S38}. Early endosome
CC {ECO:0000250|UniProtKB:Q96S38}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BLK9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLK9-2; Sequence=VSP_018043, VSP_018044, VSP_018050,
CC VSP_018051;
CC Name=3;
CC IsoId=Q8BLK9-3; Sequence=VSP_018046, VSP_018048, VSP_018049;
CC Name=4;
CC IsoId=Q8BLK9-4; Sequence=VSP_018045, VSP_018047;
CC -!- DOMAIN: The PX domain is essential for its localization to the early
CC endosomes. {ECO:0000250|UniProtKB:Q96S38}.
CC -!- DOMAIN: The first protein kinase domain appears to be a pseudokinase
CC domain as it does not contain the classical characteristics, such as
CC the ATP-binding motif, ATP-binding site and active site.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to a partial intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to a partial intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. S6 kinase subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33510.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK030313; BAC26894.1; -; mRNA.
DR EMBL; AK044809; BAC32101.1; -; mRNA.
DR EMBL; AK049003; BAC33510.1; ALT_INIT; mRNA.
DR EMBL; AK149858; BAE29128.1; -; mRNA.
DR EMBL; BC058403; AAH58403.1; -; mRNA.
DR RefSeq; NP_848890.3; NM_178775.4.
DR AlphaFoldDB; Q8BLK9; -.
DR SMR; Q8BLK9; -.
DR BioGRID; 235773; 1.
DR IntAct; Q8BLK9; 1.
DR MINT; Q8BLK9; -.
DR STRING; 10090.ENSMUSP00000061769; -.
DR iPTMnet; Q8BLK9; -.
DR PhosphoSitePlus; Q8BLK9; -.
DR jPOST; Q8BLK9; -.
DR MaxQB; Q8BLK9; -.
DR PaxDb; Q8BLK9; -.
DR PeptideAtlas; Q8BLK9; -.
DR PRIDE; Q8BLK9; -.
DR ProteomicsDB; 263471; -. [Q8BLK9-1]
DR ProteomicsDB; 263472; -. [Q8BLK9-2]
DR ProteomicsDB; 263473; -. [Q8BLK9-3]
DR ProteomicsDB; 263474; -. [Q8BLK9-4]
DR Antibodypedia; 34615; 169 antibodies from 27 providers.
DR DNASU; 320119; -.
DR Ensembl; ENSMUST00000159624; ENSMUSP00000125010; ENSMUSG00000089872. [Q8BLK9-4]
DR GeneID; 320119; -.
DR KEGG; mmu:320119; -.
DR UCSC; uc007ebg.1; mouse. [Q8BLK9-3]
DR UCSC; uc007ebh.2; mouse. [Q8BLK9-2]
DR CTD; 26750; -.
DR MGI; MGI:2443419; Rps6kc1.
DR VEuPathDB; HostDB:ENSMUSG00000089872; -.
DR eggNOG; KOG0603; Eukaryota.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00940000155656; -.
DR HOGENOM; CLU_055745_0_0_1; -.
DR InParanoid; Q8BLK9; -.
DR OrthoDB; 255297at2759; -.
DR PhylomeDB; Q8BLK9; -.
DR BioGRID-ORCS; 320119; 2 hits in 67 CRISPR screens.
DR ChiTaRS; Rps6kc1; mouse.
DR PRO; PR:Q8BLK9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BLK9; protein.
DR Bgee; ENSMUSG00000089872; Expressed in dentate gyrus of hippocampal formation granule cell and 236 other tissues.
DR ExpressionAtlas; Q8BLK9; baseline and differential.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd07287; PX_RPK118_like; 1.
DR CDD; cd05576; STKc_RPK118_like; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042132; PX_S6K-delta-1.
DR InterPro; IPR035053; STK_RPK118-like.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Endosome; Kinase;
KW Lipid-binding; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1056
FT /note="Ribosomal protein S6 kinase delta-1"
FT /id="PRO_0000233128"
FT DOMAIN 8..132
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 276..304
FT /note="MIT"
FT DOMAIN 343..444
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 789..1046
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 204..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 919
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 795..803
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 823
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S38"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S38"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S38"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S38"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S38"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S38"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S38"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 36..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018043"
FT VAR_SEQ 89..158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018044"
FT VAR_SEQ 279..336
FT /note="ESSPTRREAVKRRTAEYLMRAESICSLRAAPQLHTGPQPPGSLSSRPPWSLR
FT SPAEEL -> KVRQCHHWLESLGSLQKSERNLEKPSHTRAQQDIASPLVTKITKSHHLI
FT ICRSVHSSK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018045"
FT VAR_SEQ 317..347
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018046"
FT VAR_SEQ 337..1056
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018047"
FT VAR_SEQ 932..947
FT /note="HIQLTYFSRWSEVEDS -> QELSQMHFFLFAVASN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018048"
FT VAR_SEQ 948..1056
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018049"
FT VAR_SEQ 961
FT /note="E -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018050"
FT VAR_SEQ 962..1056
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018051"
FT CONFLICT 855..857
FT /note="GSE -> DSD (in Ref. 2; AAH58403)"
FT /evidence="ECO:0000305"
FT CONFLICT 855
FT /note="G -> D (in Ref. 1; BAC33510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1056 AA; 115712 MW; 315E6BB9926E4F42 CRC64;
MTSPWGHSAD LARFYTVTEP QRHPRGYTVY KVTARVVSRR NPEDVQEIIV WRRYSDFKKL
HRELWQIHRN AFRHSELFPP FAKGTVFGRF DKTVIEERRQ CAEDLLQFSA NIPALYNSRQ
LQDFFKGGVI SDGSELIGPA EAYPDSPANA FPECGTEGFS SDSDLLSLTV DADSLAEVDD
GMASRQGSPS RTFGLSLSTD SSAVGAVASD SEPSRVEDRE SRSLFPSSLK PRLGRRDYLE
KAGELIKLAL KKEEEDDYEA ASDFYRKGVD LLLEGVQGES SPTRREAVKR RTAEYLMRAE
SICSLRAAPQ LHTGPQPPGS LSSRPPWSLR SPAEELKAFR VLGVIDKVLL VMDTRTEQTF
ILKGLRKSSE CSRNRKTIIP RCVPNMVCLH TYIISEESVF LVLQRAEGGK LWSYISKFLN
RSSQESLDIK EGRPSMPPRV CLQQPSASPQ GGSSFESRGS DTGSMLKALP LKTSLTPSSQ
DDSNQEDDGQ PSSPKWLDSG SSSEDECTAG YLTLCNEYGQ EKMDLVSLSE ESVMQPEGDK
ADTQAVSSPA SLATGSVSPS THLRVFSGGE DLEAVSSPPT SESLSRSKNS PMEFFRIDSK
DSTSELLGLD FGEKLHSLKP EPLKALFTLE DGDSPSQSLD PGESKRESEA QDSVSRGSDD
SVPVISFKEA AAEAISGAEE GRPDLLVNLP GELQPTKEAS AMDPKFSQAS AGRLDSKLLE
APDVLCLRLS SEQCHGLGPE GPEELSDPTE FCPGGVIPEH DAQADPGVLF EAAVDHRSSP
DQFLFSSLRS ESDRLGQVEV VVTAQALQES LFHISSPCSG ANKEHSAYAD TATSEEVLLF
TEPTKEEANS LFQRGSEAQE RGVGAGEADK EIHQIFEDLD KRLAASSRFF IPEGCIQRWA
AEMVVALDAL HREGIVCRDL NPNNILLNDG GHIQLTYFSR WSEVEDSCDS DAVARMYCAP
EVGAVTEETE ACDWWSLGAV LFELLTGKTL VECHPAGINT HTTLNMPGCV SEEARSLIQQ
LLQFNPMERL GAGVAGVEDI KSHPFFTPVD WAELTR
