CRBG3_HUMAN
ID CRBG3_HUMAN Reviewed; 2970 AA.
AC Q68DQ2; B4DLE8; F6VHI2; Q4G0V8; Q7Z4R9; Q86VD0; Q8N262; Q8N7F1; Q8NDQ8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Very large A-kinase anchor protein;
DE Short=vlAKAP;
DE AltName: Full=Beta/gamma crystallin domain-containing protein 3;
GN Name=CRYBG3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2455-2970 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-1364 (ISOFORM VLAKAP), AND VARIANT HIS-2874.
RC TISSUE=Testis, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2238-2970 (ISOFORM 1), AND
RP VARIANT HIS-2874.
RC TISSUE=Lymph node, and Rectum tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2650-2970 (ISOFORM 1).
RC TISSUE=Skin;
RA Zan Q., Guo J.H., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2685-2970 (ISOFORM 1), AND
RP VARIANT HIS-2874.
RC TISSUE=Brain;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP IDENTIFICATION (ISOFORM VLAKAP), FUNCTION (ISOFORM VLAKAP), AND SUBUNIT
RP (ISOFORM VLAKAP).
RX PubMed=25097019; DOI=10.1021/bi500721a;
RA Burgers P.P., van der Heyden M.A., Kok B., Heck A.J., Scholten A.;
RT "A systematic evaluation of protein kinase A-A-Kinase anchoring protein
RT interaction motifs.";
RL Biochemistry 54:11-21(2015).
CC -!- FUNCTION: [Isoform vlAKAP]: Anchoring protein that mediates the
CC subcellular compartmentation of protein kinase A (PKA).
CC {ECO:0000269|PubMed:25097019}.
CC -!- SUBUNIT: Isoform vlAKAP binds to dimeric RII-alpha regulatory subunit
CC of PKA (PRKAR2A/PRKAR2B). {ECO:0000269|PubMed:25097019}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=vlAKAP;
CC IsoId=Q68DQ2-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q68DQ2-1; Sequence=VSP_057114;
CC Name=2;
CC IsoId=Q68DQ2-2; Sequence=VSP_057115, VSP_057116;
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36247.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP97687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03608.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH18168.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK091199; BAC03608.1; ALT_INIT; mRNA.
DR EMBL; AK098569; BAC05338.1; -; mRNA.
DR EMBL; AK296966; BAG59510.1; -; mRNA.
DR EMBL; AC110491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831927; CAD38587.1; -; mRNA.
DR EMBL; CR749313; CAH18168.1; ALT_FRAME; mRNA.
DR EMBL; AF451988; AAP97687.1; ALT_INIT; mRNA.
DR EMBL; BC036247; AAH36247.1; ALT_INIT; mRNA.
DR EMBL; BC050394; AAH50394.1; -; mRNA.
DR CCDS; CCDS43113.2; -. [Q68DQ2-3]
DR RefSeq; NP_705833.3; NM_153605.3. [Q68DQ2-3]
DR SMR; Q68DQ2; -.
DR BioGRID; 126284; 51.
DR IntAct; Q68DQ2; 16.
DR MINT; Q68DQ2; -.
DR STRING; 9606.ENSP00000374273; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR GlyGen; Q68DQ2; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q68DQ2; -.
DR PhosphoSitePlus; Q68DQ2; -.
DR BioMuta; CRYBG3; -.
DR DMDM; 172045724; -.
DR EPD; Q68DQ2; -.
DR jPOST; Q68DQ2; -.
DR MassIVE; Q68DQ2; -.
DR MaxQB; Q68DQ2; -.
DR PaxDb; Q68DQ2; -.
DR PeptideAtlas; Q68DQ2; -.
DR PRIDE; Q68DQ2; -.
DR ProteomicsDB; 4529; -.
DR ProteomicsDB; 66095; -. [Q68DQ2-3]
DR ProteomicsDB; 66096; -. [Q68DQ2-2]
DR Antibodypedia; 49902; 2 antibodies from 1 providers.
DR DNASU; 131544; -.
DR Ensembl; ENST00000389622.7; ENSP00000374273.3; ENSG00000080200.10. [Q68DQ2-3]
DR GeneID; 131544; -.
DR KEGG; hsa:131544; -.
DR MANE-Select; ENST00000389622.7; ENSP00000374273.3; NM_153605.4; NP_705833.3.
DR UCSC; uc021xbn.3; human. [Q68DQ2-3]
DR CTD; 131544; -.
DR DisGeNET; 131544; -.
DR GeneCards; CRYBG3; -.
DR HGNC; HGNC:34427; CRYBG3.
DR HPA; ENSG00000080200; Low tissue specificity.
DR neXtProt; NX_Q68DQ2; -.
DR OpenTargets; ENSG00000080200; -.
DR PharmGKB; PA164718140; -.
DR VEuPathDB; HostDB:ENSG00000080200; -.
DR eggNOG; ENOG502QTHR; Eukaryota.
DR GeneTree; ENSGT00940000160816; -.
DR HOGENOM; CLU_000811_0_0_1; -.
DR InParanoid; Q68DQ2; -.
DR OMA; NSYVMPS; -.
DR OrthoDB; 89929at2759; -.
DR TreeFam; TF331078; -.
DR PathwayCommons; Q68DQ2; -.
DR SignaLink; Q68DQ2; -.
DR BioGRID-ORCS; 131544; 0 hits in 246 CRISPR screens.
DR ChiTaRS; CRYBG3; human.
DR GenomeRNAi; 131544; -.
DR Pharos; Q68DQ2; Tdark.
DR PRO; PR:Q68DQ2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q68DQ2; protein.
DR Bgee; ENSG00000080200; Expressed in gingival epithelium and 209 other tissues.
DR ExpressionAtlas; Q68DQ2; baseline and differential.
DR Genevisible; Q68DQ2; HS.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0051018; F:protein kinase A binding; IPI:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR CDD; cd00161; RICIN; 1.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR011024; G_crystallin-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00030; Crystall; 6.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR01367; BGCRYSTALLIN.
DR SMART; SM00458; RICIN; 1.
DR SMART; SM00247; XTALbg; 6.
DR SUPFAM; SSF49695; SSF49695; 3.
DR SUPFAM; SSF50370; SSF50370; 1.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 9.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lectin; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2970
FT /note="Very large A-kinase anchor protein"
FT /id="PRO_0000325758"
FT DOMAIN 2334..2383
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2429..2467
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2479..2523
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2524..2566
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2572..2613
FT /note="Beta/gamma crystallin 'Greek key' 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2614..2656
FT /note="Beta/gamma crystallin 'Greek key' 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2667..2703
FT /note="Beta/gamma crystallin 'Greek key' 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2704..2746
FT /note="Beta/gamma crystallin 'Greek key' 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2793..2834
FT /note="Beta/gamma crystallin 'Greek key' 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 2836..2968
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1322
FT /note="RII-binding helix"
FT /evidence="ECO:0000269|PubMed:25097019"
FT REGION 2095..2124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2139..2163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2086
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W49"
FT MOD_RES 2093
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W49"
FT MOD_RES 2094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W49"
FT MOD_RES 2100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W49"
FT MOD_RES 2104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W49"
FT VAR_SEQ 1..2742
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057115"
FT VAR_SEQ 1..1948
FT /note="Missing (in isoform 1)"
FT /id="VSP_057114"
FT VAR_SEQ 2743..2747
FT /note="KPIDY -> MNKKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057116"
FT VARIANT 2381
FT /note="R -> H (in dbSNP:rs11918990)"
FT /id="VAR_039906"
FT VARIANT 2709
FT /note="Y -> C (in dbSNP:rs17302349)"
FT /id="VAR_039907"
FT VARIANT 2874
FT /note="N -> H (in dbSNP:rs4857302)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_039908"
FT CONFLICT 2693
FT /note="S -> P (in Ref. 3; CAH18168)"
FT /evidence="ECO:0000305"
FT CONFLICT 2765
FT /note="R -> G (in Ref. 5; AAH36247)"
FT /evidence="ECO:0000305"
FT CONFLICT 2768..2771
FT /note="Missing (in Ref. 4; AAP97687)"
FT /evidence="ECO:0000305"
FT CONFLICT 2847
FT /note="Q -> R (in Ref. 5; AAH50394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2970 AA; 330633 MW; A0851F4BC1252D1E CRC64;
MSSGRRRGSA PWHSFSRFFA PRSPSRDKEE EEEERPGTSP PPAPGRSAAS VENEPMSTSQ
KKENVLSSEA VKIRQSEDKR NHAEKPVTLP VQEDPKKAYD LSSSTSDTKI GESDRQPKES
FFQFLGNLFN ISGKSSLGEA KQSSFKDDQD KTEKDLQNPS DHHEDGIKRE REIFSGSLRT
QTHPTEEQDS NSSELSDAFS LDTTQDSDQE TTNLLKQIDG KPEKPSVTYA TYRGPRHIGK
YLKQQTGLAT VNTLDRENES SDSSTNRHID PGSEIEAGVL PLLLSASTDS SMKGNLLEGP
LEDSDCSKTS FNKENSLTNN PELQNIASSN NLLNKNAWGS IERNRSSPSS VTNSSYDGES
DSQHHLSCEP VSQTNRNLVC SALLTGSNHR KVPCSPDFQR VTTTENTIKE NSTVMSNRTL
VQREELVEPQ GPAISDFSCS KSDGSDTTEQ ESTNLPSPNK SIRHEHLQLP ESECSDKQTI
DSSSKQAATH TNIIALQRHA VTDTEFVNEG KRLSAQDSQK NVAVREIRRE TESASAGESI
ASSHVKAPED KIESLPKDTD QYFETKAKKL DFRSHDKIPH IRMNKKDLAS LNYISESAVV
ASLGNENAPE LKFELNRSHI SETPLDSESP QQAEVSPDAK TSLSLDCKKL NFSISPPTFV
SGVGMLSKLD IPDLMNEGSP VPIETGNVNI VGISYQPRKC KEENVKNHVE AAGRKSPPPS
FCLEYTSAIF EFKEVLSNSE KCQVLPGSEA SGPHLTGLEL LSFDSGNLSK DCSSILSQDP
NRVELVSSNT KANMSIIEKS DSLSLEAKTA NIVSKAEIDG QNNVLVESHS GRGKTISLSK
VSLSKVEPRN ISQDKMSSFP LKITHVPEKP ILSELTFLEV EQGKRFQSIN HNEIGEKCSD
AGLKENCQAE LSPAASKYED KPEPEVDALG SPPALLKSNI SWILPPIHDE KISRQMAQNC
EAHTCVFHQS LDICGTKKIS GHSEMAELSL TNISPKFQET GSMKVNSPFL DSDSSLEKNS
SASEDSSFLK VPSVLKLEKK SSSYRKKENI HFLNGGIDSV SSSSSYPEEV SMIVNSHKPQ
NNLDSIQVTK DLTHEGTSVT NLLYPTTSYL EFETSVSIGT EVTPFQEHFG IYTGKISIDF
PTAAQFDNLV EAETGAVAGP AASVNSSGQQ CSEASAEHIE ARRRAHDQLL DLKSSLLKKA
DTLIGEIFNS VREELKFKHT VSTCQEHIAI EGIMNLGTLK EDISEKNPSE VTLTEIQQTE
GLEEQGMENM SEVKEKPCVS PTVGEKNLLV DPNSMNVSCL LEDKARELVN EIIYVAQEKL
RNDTFEDTED TWDSELQANT SKILNSDSVK PHDVVREFLV SEQPVNQSTQ ISENKVLNEF
FSLSNLASGT ESIKGGEIVL YQKSLFSGNG SGLSDSINLQ ESDTVLLAED MSHKRLDDRV
KTHLFRSEDC NETMEIENVD NNKTETEDRR TLVLNFKWPP LVNDDIHAPG TSKSSLSDSL
VCISEKNLPG HSKNTPLAMS DVGKVHKKDN EINIGKIELI PSMLETGKTN KKDAELNILK
YEAVPPMIEM GRIHKMDAEL NVTKTEPKAN VFKMGEVYQM DAESCIEKTE GSAVILGMEK
AYKMKDTEGD IGKIEVIPMM PEVKNIHQKD AEGDIVKTEM TPVTVDMENI YQTHAEGDIG
KTGTIALSEV ENIHQKGGEG ISEKAEVIPV TLAMENTYQK DAEGDIGKAE VMPVRLEMEN
TYPKDTERDG GKTEVMPLAL EVVNTYQKNA KGFTGNTEGS VLKMEATYRK TAEEVIKNTE
IVPCVLKVKE AHETAPAPLE MEKACKRDVK ETIGATVSTP SVIEMEKISP EDRGENIGKH
KVLPAVVDIE KIHGTGLELT TKQGEAMLPA FESKTPQEYA EGSVEETKEE PTEIKEGLIA
HENRLPTYFR GYESPTLSKD YEGYPAPAMP DFQPGDTTVR LDKRMSLTAI YDKRRETDYS
DKGYNLAFVS QDEQENSSFT ILYEEPLQEE DKYASAEARQ TQSVLFHDTS ADSMPVLACE
RSESRTDLVH HFEKGTKLGE TFDSDSSEMF LSVEAKRYKI YPLALSPIYE DDSSQEDILS
SEVSPGHHGP RKSRDSENQS SSVLSLLQSV SERLKMNFDE DDREAADEEE EEEEAAVLHK
GDLRAGSGER VTFQLPDPSI TFYPDDQESV GISKNSYVMP NEPTTSNLQV GLWPEKTSFL
QKSDLTSKLH SSLKSAYHQY LQTSQSHSSE KGARFGGIFQ EPVSKYFRVQ DSPGRLSPFI
ENVDKQTLRC NPRPGKMVIY DLHESTYKQE VYCNIPDATS WSFPNGVLIK VVRGCWILYE
KPHFRGQKCV LEEGEKVLNR DWILQNRRHP QRNFILGSLK RVLKDCSIPE IELFPQSDPA
CCPVYIQRAV PNLEELNISK SVSFTVKSGV WLAYPDINFK GQATVLEEDH GLFEISTAEM
KSLHPLQMGG LKVEMPMNLK VIIYEKPHFH GQAKEFSEHI DSVPNFLKNN GDFHRIGSIR
VIGGVWVAYE KEHFKGQQFL LEEGDFEDSN ACGALSSPIL SFRYLQANFI ESSVTLFESD
LESGKFIDIT NQEISDLEEI GFGSKTRSIH VKSGVWVAYQ QKFFCGEQYI LEKGKYKCFF
DWGGSNNIIM SIRPIQLEPL GINEPPHLLK AFSKPGFQGE CIDFTEETSD LTSLMPCSFK
VLRGCWLLYY QEDMFVNHCV LEEGLYADLT SCGCPASKVK SLKPIDYVFE EPSISLFALE
HCEGRELHLE EAVNSVLNKD LHFYTQSVWV KSGLWIAYEG SNFLGRQILL RPNEIPNWTA
FSRWKTIGSL RPMKQPAVYI RIKNRAQGEY LTVTGSLADT RATSVCISPY SGKNTQIWYY
CRGLFKSKAS DTCLDVIGGR DTPGAKVALW TEHGQFRQKW RLNKNGTISS YLSDQLVLDV
KGGNYCDKTH VIVNQPLEGE ETQKWDIEIL
