CDK12_RAT
ID CDK12_RAT Reviewed; 1484 AA.
AC Q3MJK5; Q8R458;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cyclin-dependent kinase 12;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=Cdc2-related kinase, arginine/serine-rich;
DE Short=CrkRS;
DE AltName: Full=Cell division cycle 2-related protein kinase 7;
DE Short=CDC2-related protein kinase 7;
DE AltName: Full=Cell division protein kinase 12;
DE AltName: Full=Protein kinase for splicing component;
GN Name=Cdk12; Synonyms=Crk7, Crkrs, Pksc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CCNL1 AND
RP CCNL2, SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=16537916; DOI=10.1128/mcb.26.7.2736-2745.2006;
RA Chen H.-H., Wang Y.-C., Fann M.-J.;
RT "Identification and characterization of the CDK12/cyclin L1 complex
RT involved in alternative splicing regulation.";
RL Mol. Cell. Biol. 26:2736-2745(2006).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-324; SER-331;
RP SER-333; SER-382; SER-384; SER-422; SER-640; SER-677; SER-681 AND THR-889,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cyclin-dependent kinase that phosphorylates the C-terminal
CC domain (CTD) of the large subunit of RNA polymerase II (POLR2A),
CC thereby acting as a key regulator of transcription elongation.
CC Regulates the expression of genes involved in DNA repair and is
CC required for the maintenance of genomic stability. Preferentially
CC phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated
CC at 'Ser-7', but can also phosphorylate 'Ser-2'. Involved in regulation
CC of MAP kinase activity, possibly leading to affect the response to
CC estrogen inhibitors (By similarity). Required for RNA splicing,
CC possibly by phosphorylating SRSF1/SF2. {ECO:0000250,
CC ECO:0000269|PubMed:16537916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
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=2.7.11.22;
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=2.7.11.22;
CC -!- SUBUNIT: Interacts with CCNL1 and CCNL2. {ECO:0000269|PubMed:16537916}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537916}. Nucleus
CC speckle {ECO:0000269|PubMed:16537916}. Note=Colocalized with nuclear
CC speckles throughout interphase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CDK12(L);
CC IsoId=Q3MJK5-1; Sequence=Displayed;
CC Name=2; Synonyms=CDK12(S);
CC IsoId=Q3MJK5-2; Sequence=VSP_030288, VSP_030289;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic tissues such as brain,
CC spinal cord, heart, lung, liver, gut and limb. Levels are lower in
CC adult tissues. {ECO:0000269|PubMed:16537916}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 10.5 and 14.5 dpc.
CC {ECO:0000269|PubMed:16537916}.
CC -!- PTM: Phosphorylation at Thr-889 increases kinase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; AY072294; AAL69525.1; -; mRNA.
DR EMBL; AY962568; AAY41734.1; -; mRNA.
DR RefSeq; NP_001029039.1; NM_001033867.1. [Q3MJK5-1]
DR RefSeq; NP_620271.1; NM_138916.2. [Q3MJK5-2]
DR AlphaFoldDB; Q3MJK5; -.
DR SMR; Q3MJK5; -.
DR STRING; 10116.ENSRNOP00000008256; -.
DR iPTMnet; Q3MJK5; -.
DR PhosphoSitePlus; Q3MJK5; -.
DR jPOST; Q3MJK5; -.
DR PaxDb; Q3MJK5; -.
DR PRIDE; Q3MJK5; -.
DR GeneID; 192350; -.
DR KEGG; rno:192350; -.
DR UCSC; RGD:621111; rat. [Q3MJK5-1]
DR CTD; 51755; -.
DR RGD; 621111; Cdk12.
DR VEuPathDB; HostDB:ENSRNOG00000006000; -.
DR eggNOG; KOG0600; Eukaryota.
DR InParanoid; Q3MJK5; -.
DR OMA; STKHNRE; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q3MJK5; -.
DR TreeFam; TF101060; -.
DR Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR PRO; PR:Q3MJK5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000006000; Expressed in spleen and 18 other tissues.
DR ExpressionAtlas; Q3MJK5; baseline and differential.
DR Genevisible; Q3MJK5; RN.
DR GO; GO:0002944; C:cyclin K-CDK12 complex; ISO:RGD.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IDA:RGD.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:RGD.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043405; P:regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:RGD.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Isopeptide bond; Kinase;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Ubl conjugation.
FT CHAIN 1..1484
FT /note="Cyclin-dependent kinase 12"
FT /id="PRO_0000314471"
FT DOMAIN 723..1016
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 855
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 729..737
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 752
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 810..815
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1036
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 73
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 688
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 889
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 1240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT MOD_RES 1242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14AX6"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT CROSSLNK 506
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV4"
FT VAR_SEQ 1250..1258
FT /note="ACPPHILPP -> GKQTGHESQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16537916"
FT /id="VSP_030288"
FT VAR_SEQ 1259..1484
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16537916"
FT /id="VSP_030289"
SQ SEQUENCE 1484 AA; 163790 MW; E3B346EA6A587D7B CRC64;
MPNSERHGGK KDGSGGASGT SQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA
ASLGTIIKPL VEYDDISSDS DTFSDDMAFK SDRRENDERR GTDRSDRLHR HRHHQHRRSR
DLLKTKQTEK EKNQEVSKSG SMKDRLSGSS KRSVEGNDDY GKAQLSKSSS KESRSSKMHK
EKTRKERELK SGHKDRSKSH RKRETPKSYK TVDSPKRRSR SPHRKWSDSS KQDDSPSGAS
YGQDYDLSPP RSHTSSNYDS YKKSPGSTSR RQSISPPYKE PSAYQSSTRS PSPYSRRQRS
VSPYSRRRSS SYERSGSYSG RSPSPYGRRR SSSPFLSKRS LSRSPISSRK SMKSRSRSPA
YSRHSSSHSK KKRSGSRSRH SSISPVRLPL NSSLGAELSR KKKERAAAAA AAKLDGKESK
GSPIILPKKE KFEVKESGLE SKKLPRGIKS EKSTPDTELV NVAHSNTEVK NCLDTGKVKL
DENLQKHPVK DLKAQGTKDT KPVALKEVIV TSKETETSEK EALPPLPTIT SPPPLPSTTP
PPQTPPLPPL PPLPAVPLQP PLPPPQPPFS QVPVSNTSTL PSSPHPRTST LSSQTNSQPL
VQVSMKTQLS VTAAIPHLKT STLPPLPLPP LLPGDDDMDS PKEMLPSKPA KKEKEQRTRH
LLTDLPLPPE LPGGDPSPPD SPEPKAITPP QQPYKKRPKI CCPRYGERRQ TESDWGKRCV
DKFDIIGIIG EGTYGQVYKA KDKDTGELVA LKKVRLDNEK EGFPITAIRE IKILRQLVHQ
SVVNMKEIVT DKQDALDFKK DKGAFYLVFE YMDHDLMGLL ESGLVHFSED HIKSFMKQLM
EGLDYCHKKN FLHRDIKCSN ILLNNSGQIK LADFGLARLY NSEESRPYTN KVITLWYRPP
ELLLGEERYT PAIDVWSCGC ILGELFTKKP IFQANLELAQ LELISRLCGS PCPAVWPDVI
KLPYFNTMKP KKQYRRRLRE EFSFIPSAAL DLLDHMLTLD PSKRCTAEQT LQSDFLKDVE
LSKMAPPDLP HWQDCHELWS KKRRRQRQSG IVIEEQPPSK ASRKETTSGT AAEPVKNSSP
APPQPAPVKA EPGPGDAVGL GDITQQLNQS ELAVLLNLLQ SQTDLSIPQM AQLLNIHSNP
EMQQQLEALN QSISALTEAS SQQQDSESIA PEESLKEVPS VSVVLPPAEQ TTPEASNTPA
DMQNMLAVLL SQLMKTQEPA GNLEENTSDK NSGPQGPRRT PTMPQEEAAA CPPHILPPEK
RPPEPPGPPP PPPPPPLVEG DLSSAPQELN PAVTAALLQL LSQPEAEPPG HLPHEHQALR
PMEYSTRSHP NRTYGNTDGP ETGFSATDTD ERSSGPALTE SLVQTLVKNR TFSGSVSHLG
ESNSYQGTGS VQFPGDQDLR FTRVPLALHS VVGQPFLKSE GNSNSVVHAE TKLQNYGELG
PGTTGANSSG TTLQWGGPAQ SFGKPYRGAA RVPPRGGRGR GVPY
