AKA12_RAT
ID AKA12_RAT Reviewed; 1687 AA.
AC Q5QD51; Q5QD49; Q5QD50; Q9Z1F7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=A-kinase anchor protein 12;
DE Short=AKAP-12;
GN Name=Akap12;
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] (ISOFORM 1), AND PHOSPHORYLATION.
RX PubMed=8626441; DOI=10.1074/jbc.271.11.6417;
RA Chapline C., Mousseau B., Ramsay K., Duddy S., Li Y., Kiley S.C., Jaken S.;
RT "Identification of a major protein kinase C-binding protein and substrate
RT in rat embryo fibroblasts. Decreased expression in transformed cells.";
RL J. Biol. Chem. 271:6417-6422(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=15496411; DOI=10.1074/jbc.m408828200;
RA Streb J.W., Kitchen C.M., Gelman I.H., Miano J.M.;
RT "Multiple promoters direct expression of three AKAP12 isoforms with
RT distinct subcellular and tissue distribution profiles.";
RL J. Biol. Chem. 279:56014-56023(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15923193; DOI=10.1074/jbc.m414017200;
RA Streb J.W., Miano J.M.;
RT "Cross-species sequence analysis reveals multiple charged residue-rich
RT domains that regulate nuclear/cytoplasmic partitioning and membrane
RT localization of a kinase anchoring protein 12 (SSeCKS/Gravin).";
RL J. Biol. Chem. 280:28007-28014(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-245; SER-268;
RP SER-271; SER-274; SER-304; THR-331; SER-335; SER-350; SER-469; SER-491;
RP SER-507; SER-509; SER-541; SER-544; SER-585; SER-599; SER-614; THR-629;
RP SER-631; SER-635; SER-638; SER-683; SER-736; SER-770; SER-771; SER-1059;
RP SER-1348; SER-1352; SER-1354 AND SER-1571, AND IDENTIFICATION BY MASS
RP 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: Anchoring protein that mediates the subcellular
CC compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to dimeric RII-alpha regulatory subunit of PKC.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Membrane
CC {ECO:0000250|UniProtKB:Q02952}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q02952}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q5QD51-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q5QD51-2; Sequence=VSP_028137, VSP_028138;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q5QD51-3; Sequence=VSP_028136;
CC -!- PTM: Phosphorylated by PKC (in vitro). {ECO:0000269|PubMed:8626441}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD03788.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U41453; AAD03788.1; ALT_FRAME; mRNA.
DR EMBL; AY695056; AAV84358.1; -; mRNA.
DR EMBL; AY695057; AAV84359.1; -; mRNA.
DR EMBL; AY695058; AAV84360.1; -; mRNA.
DR RefSeq; NP_001028825.1; NM_001033653.1. [Q5QD51-2]
DR RefSeq; NP_476444.2; NM_057103.2. [Q5QD51-1]
DR RefSeq; XP_006227910.1; XM_006227848.3. [Q5QD51-3]
DR AlphaFoldDB; Q5QD51; -.
DR SMR; Q5QD51; -.
DR BioGRID; 249703; 2.
DR IntAct; Q5QD51; 1.
DR MINT; Q5QD51; -.
DR STRING; 10116.ENSRNOP00000057494; -.
DR iPTMnet; Q5QD51; -.
DR PhosphoSitePlus; Q5QD51; -.
DR jPOST; Q5QD51; -.
DR PaxDb; Q5QD51; -.
DR PRIDE; Q5QD51; -.
DR Ensembl; ENSRNOT00000060767; ENSRNOP00000057494; ENSRNOG00000019549. [Q5QD51-1]
DR Ensembl; ENSRNOT00000083702; ENSRNOP00000070062; ENSRNOG00000019549. [Q5QD51-2]
DR Ensembl; ENSRNOT00000099245; ENSRNOP00000087138; ENSRNOG00000019549. [Q5QD51-3]
DR GeneID; 83425; -.
DR KEGG; rno:83425; -.
DR UCSC; RGD:70988; rat. [Q5QD51-1]
DR CTD; 9590; -.
DR RGD; 70988; Akap12.
DR eggNOG; ENOG502RDV6; Eukaryota.
DR GeneTree; ENSGT00730000111244; -.
DR HOGENOM; CLU_002691_0_0_1; -.
DR InParanoid; Q5QD51; -.
DR OMA; AWEPVEL; -.
DR OrthoDB; 158752at2759; -.
DR PhylomeDB; Q5QD51; -.
DR TreeFam; TF105411; -.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q5QD51; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019549; Expressed in testis and 19 other tissues.
DR Genevisible; Q5QD51; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0008179; F:adenylate cyclase binding; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051018; F:protein kinase A binding; IEA:InterPro.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0035733; P:hepatic stellate cell activation; IEP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0061870; P:positive regulation of hepatic stellate cell migration; IMP:RGD.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:1900143; P:positive regulation of oligodendrocyte apoptotic process; IMP:RGD.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:InterPro.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:RGD.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IEA:InterPro.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR InterPro; IPR028540; AKAP12.
DR InterPro; IPR001573; AKAP_WSK.
DR PANTHER; PTHR23209; PTHR23209; 1.
DR Pfam; PF03832; WSK; 3.
DR PROSITE; PS51893; AKAP_CAM_BD; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT CHAIN 2..1687
FT /note="A-kinase anchor protein 12"
FT /id="PRO_0000304942"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..544
FT /note="Involved in PKC-binding"
FT /evidence="ECO:0000250"
FT REGION 298..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1511
FT /note="RII-binding"
FT /evidence="ECO:0000250"
FT REGION 1522..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1599..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 594..614
FT /note="AKAP CaM-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT MOTIF 743..763
FT /note="AKAP CaM-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT MOTIF 784..804
FT /note="AKAP CaM-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 353
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 629
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 871
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT MOD_RES 1571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1637
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT CROSSLNK 1030
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q02952"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15496411"
FT /id="VSP_028136"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15496411"
FT /id="VSP_028137"
FT VAR_SEQ 81..88
FT /note="EEEVVDED -> MLGTITIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15496411"
FT /id="VSP_028138"
FT CONFLICT 60
FT /note="T -> S (in Ref. 1; AAD03788)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="S -> N (in Ref. 1; AAD03788)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="S -> N (in Ref. 1; AAD03788)"
FT /evidence="ECO:0000305"
FT CONFLICT 1006
FT /note="G -> S (in Ref. 1; AAD03788)"
FT /evidence="ECO:0000305"
FT CONFLICT 1219
FT /note="A -> T (in Ref. 1; AAD03788)"
FT /evidence="ECO:0000305"
FT CONFLICT 1651
FT /note="A -> R (in Ref. 1; AAD03788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1687 AA; 181110 MW; AC02148E9BD2DB0C CRC64;
MGAGSSTEQR SPEQPAGSDT PSELVLSGHG PAAEASGAAG DPADADPATK LPQKNGQLST
VNGVAEQGDV HVQEENQEGQ EEEVVDEDVG QRESEDVREK DRVEEMAANS TAVEDITKDG
QEETSEIIEQ IPASESNVEE MVQPAESQAN DVGFKKVFKF VGFKFTVKKD KNEKSDTVQL
LTVKKDEGEG AEASVGAGDH QEPSVETAVG ESASKESELK QSTEKQEGTL KQEQSSTEIP
LQAESDQAAE EEAKDEGEEK QEKEPTKSPE SPSSPVSSET TSSFKKFFTH GWAGWRKKTS
FKKSKEDDLE TAEKRKEQEA EKVDEEEKEK TEPASEEQEP AEDTDQARLS ADYEKVELPL
EDQVGDLEAS SEEKCAPLAT EVFDEKMEAH QEVVAEVHVS TVEKTEEEQG GGGEAEGGVV
VEGTGESLPP EKLAEPQEVP QEAEPAEELM KSREMCVSGG DHTQLTDLSP EEKTLPKHPE
GIVSEVEMLS SQERIKVQGS PLKKLFSSSG LKKLSGKKQK GKRGGGGDEE PGEYQHIHTE
SPESADEQKG ESSASSPEEP EETTCLEKGP LEAPQDGEAE EGTTSDGEKK REGITPWASF
KKMVTPKKRV RRPSESDKEE ELEKVKSATL SSTDSTVSEM QDEVKTVGEE QKPEEPKRRV
DTSVSWEALI CVGSSKKRAR KASSSDDEGG PRTLGGDSHR AEEASKDKEA GTDAVPASTQ
EQDQAQGSSS PEPAGSPSEG EGVSTWESFK RLVTPRKKSK SKLEEKAEDS SVEQLSTEIE
PSREESWVSI KKFIPGRRKK RADGKQEQAT VEDSGPVEIN EDDPDVPAVV PLSEYDAVER
EKMEAQGNAE LPQLLGAVYV SEELSKTLVH TVSVAVIDGT RAVTSVEERS PSWISASVTE
PLEHTAGEAM PPVEEVTEKD IIAEETPVLT QTLPEGKDAH DDMVTSEVDF TSEAVTATET
SEALRTEEVT EASGAEETTD MVSAVSQLTD SPDTTEEATP VQEVEGGVLD TEEEERQTQA
ILQAVADKVK EESQVPATQT VQRTGSKALE KVEEVEEDSE VLASEKEKDV MPKGPVQEAG
AEHLAQGSET GQATPESLEV PEVTADVDHV ATCQVIKLQQ LMEQAVAPES SETLTDSETN
GSTPLADSDT ADGTQQDETI DSQDSKATAA VRQSQVTEEE AATAQKEEPS TLPNNVPAQE
EHGEEPGRDV LEPTQQELAA AAVPVLAKTE VGQEGEVDWL DGEKVKEEQE VFVHSGPNSQ
KAADVTYDSE VMGVAGCQEK ESTEVQSLSL EEGEMETDVE KEKRETKPEQ VSEEGEQETA
APEHEGTYGK PVLTLDMPSS ERGKALGSLG GSPSLPDQDK AGCIEVQVQS LDTTVTQTAE
AVEKVIETVV ISETGESPEC VGAHLLPAEK SSATGGHWTL QHAEDTVPLG PESQAESIPI
IVTPAPESTL HPDLQGEISA SQRERSEEED KPDAGPDADG KESTAIEKVL KAEPEILELE
SKSNKIVLNV IQTAVDQFAR TETAPETHAY DSQTQVPAMQ ADSQGAQQML DKNESCQDET
PSAAAQRGLA SPDRSGGMGS ASEMLAALAV ESAGVKVSIE KLPPQPKDQK EHAADGPQLQ
SLAQAEASAS GNLTKESPDT NGPKLTEEGD APKVEVQEEE MSTKSVKENK AQAEEDLQEP
KGDLAES
