ID FGD6_HUMAN Reviewed; 1430 AA.
AC Q6ZV73; Q6ZR53; Q7Z2Z7; Q96D44; Q9NUR8; Q9P2I5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 6;
DE AltName: Full=Zinc finger FYVE domain-containing protein 24;
GN Name=FGD6; Synonyms=KIAA1362, ZFYVE24;
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 1).
RC TISSUE=Hippocampus, and Placenta;
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 MRNA] OF 966-1430 (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1206 (ISOFORM 1).
RC TISSUE=Endothelial cell;
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 669-1430 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515; SER-692; SER-721 AND
RP SER-1197, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-515; SER-554;
RP SER-692; SER-721 AND SER-1197, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May activate CDC42, a member of the Ras-like family of
CC Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a
CC role in regulating the actin cytoskeleton and cell shape (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZV73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZV73-2; Sequence=VSP_013091, VSP_013092;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92052.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA92600.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC87464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD98096.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK002045; BAA92052.1; ALT_INIT; mRNA.
DR EMBL; AK124904; BAC85990.1; -; mRNA.
DR EMBL; AK128492; BAC87464.1; ALT_INIT; mRNA.
DR EMBL; BC013319; AAH13319.2; -; mRNA.
DR EMBL; BX538322; CAD98096.1; ALT_SEQ; mRNA.
DR EMBL; AB037783; BAA92600.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31878.1; -. [Q6ZV73-1]
DR RefSeq; NP_060821.3; NM_018351.3. [Q6ZV73-1]
DR AlphaFoldDB; Q6ZV73; -.
DR SMR; Q6ZV73; -.
DR BioGRID; 120899; 44.
DR IntAct; Q6ZV73; 27.
DR MINT; Q6ZV73; -.
DR STRING; 9606.ENSP00000344446; -.
DR GlyGen; Q6ZV73; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZV73; -.
DR PhosphoSitePlus; Q6ZV73; -.
DR BioMuta; FGD6; -.
DR DMDM; 61213484; -.
DR EPD; Q6ZV73; -.
DR jPOST; Q6ZV73; -.
DR MassIVE; Q6ZV73; -.
DR MaxQB; Q6ZV73; -.
DR PaxDb; 9606-ENSP00000344446; -.
DR PeptideAtlas; Q6ZV73; -.
DR ProteomicsDB; 68397; -. [Q6ZV73-1]
DR ProteomicsDB; 68398; -. [Q6ZV73-2]
DR Antibodypedia; 1926; 117 antibodies from 17 providers.
DR DNASU; 55785; -.
DR Ensembl; ENST00000343958.9; ENSP00000344446.4; ENSG00000180263.14. [Q6ZV73-1]
DR Ensembl; ENST00000546711.5; ENSP00000450342.1; ENSG00000180263.14. [Q6ZV73-2]
DR GeneID; 55785; -.
DR KEGG; hsa:55785; -.
DR MANE-Select; ENST00000343958.9; ENSP00000344446.4; NM_018351.4; NP_060821.3.
DR UCSC; uc001tdp.4; human. [Q6ZV73-1]
DR AGR; HGNC:21740; -.
DR CTD; 55785; -.
DR DisGeNET; 55785; -.
DR GeneCards; FGD6; -.
DR HGNC; HGNC:21740; FGD6.
DR HPA; ENSG00000180263; Low tissue specificity.
DR MIM; 613520; gene.
DR neXtProt; NX_Q6ZV73; -.
DR OpenTargets; ENSG00000180263; -.
DR PharmGKB; PA134967436; -.
DR VEuPathDB; HostDB:ENSG00000180263; -.
DR eggNOG; KOG1729; Eukaryota.
DR GeneTree; ENSGT00940000156334; -.
DR HOGENOM; CLU_004959_0_0_1; -.
DR InParanoid; Q6ZV73; -.
DR OMA; YILPMSS; -.
DR OrthoDB; 5385125at2759; -.
DR PhylomeDB; Q6ZV73; -.
DR TreeFam; TF316247; -.
DR PathwayCommons; Q6ZV73; -.
DR SignaLink; Q6ZV73; -.
DR BioGRID-ORCS; 55785; 15 hits in 1159 CRISPR screens.
DR ChiTaRS; FGD6; human.
DR GenomeRNAi; 55785; -.
DR Pharos; Q6ZV73; Tbio.
DR PRO; PR:Q6ZV73; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6ZV73; Protein.
DR Bgee; ENSG00000180263; Expressed in buccal mucosa cell and 137 other cell types or tissues.
DR ExpressionAtlas; Q6ZV73; baseline and differential.
DR Genevisible; Q6ZV73; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR CDD; cd15743; FYVE_FGD6; 1.
DR CDD; cd15793; PH1_FGD6; 1.
DR CDD; cd13237; PH2_FGD5_FGD6; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR037743; FGD6_N_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF12; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 6; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton;
KW Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1430
FT /note="FYVE, RhoGEF and PH domain-containing protein 6"
FT /id="PRO_0000080952"
FT DOMAIN 871..1060
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1089..1183
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1333..1429
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1222..1281
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..843
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZL1"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1370..1374
FT /note="DVAAL -> VRSEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013091"
FT VAR_SEQ 1375..1430
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013092"
FT VARIANT 257
FT /note="Q -> R (in dbSNP:rs10507047)"
FT /id="VAR_024286"
FT VARIANT 1393
FT /note="E -> K (in dbSNP:rs3794255)"
FT /id="VAR_051985"
FT CONFLICT 832
FT /note="S -> P (in Ref. 3; CAD98096)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="S -> F (in Ref. 3; CAD98096)"
FT /evidence="ECO:0000305"
FT CONFLICT 949
FT /note="Q -> H (in Ref. 1; BAC85990)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="Y -> D (in Ref. 2; AAH13319)"
FT /evidence="ECO:0000305"
FT CONFLICT 992
FT /note="A -> T (in Ref. 2; AAH13319)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="R -> C (in Ref. 4; BAA92600)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="I -> V (in Ref. 2; AAH13319)"
FT /evidence="ECO:0000305"
FT CONFLICT 1115
FT /note="A -> V (in Ref. 3; CAD98096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1430 AA; 160816 MW; 705D1D4DFB50D8FF CRC64;
MTSAAEIKKP PVAPKPKFVV ANNKPAPPPI APKPDIVISS VPQSTKKMKP AIAPKPKVLK
TSPVREIGQS PSRKIMLNLE GHKQELAEST DNFNCKYEGN QSNDYISPMC SCSSECIHKL
GHRENLCVKQ LVLEPLEMNE NLENSKIDET LTIKTRSKCD LYGEKAKNQG GVVLKASVLE
EELKDALIHQ MPPFISAQKH RPTDSPEMNG GCNSNGQFRI EFADLSPSPS SFEKVPDHHS
CHLQLPSDEC EHFETCQDDS EKSNNCFQSS ELEALENGKR STLISSDGVS KKSEVKDLGP
LEIHLVPYTP KFPTPKPRKT RTARLLRQKC VDTPSESTEE PGNSDSSSSC LTENSLKINK
ISVLHQNVLC KQEQVDKMKL GNKSELNMES NSDAQDLVNS QKAMCNETTS FEKMAPSFDK
DSNLSSDSTT VDGSSMSLAV DEGTGFIRCT VSMSLPKQLK LTCNEHLQSG RNLGVSAPQM
QKESVIKEEN SLRIVPKKPQ RHSLPATGVL KKAASEELLE KSSYPSSEEK SSEKSLERNH
LQHLCAQNRG VSSSFDMPKR ASEKPVWKLP HPILPFSGNP EFLKSVTVSS NSEPSTALTK
PRAKSLSAMD VEKCTKPCKD STKKNSFKKL LSMKLSICFM KSDFQKFWSK SSQLGDTTTG
HLSSGEQKGI ESDWQGLLVG EEKRSKPIKA YSTENYSLES QKKRKKSRGQ TSAANGLRAE
SLDDQMLSRE SSSQAPYKSV TSLCAPEYEN IRHYEEIPEY ENLPFIMAIR KTQELEWQNS
SSMEDADANV YEVEEPYEAP DGQLQLGPRH QHSSSGASQE EQNDLGLGDL PSDEEEIINS
SDEDDVSSES SKGEPDPLED KQDEDNGMKS KVHHIAKEIM SSEKVFVDVL KLLHIDFRDA
VAHASRQLGK PVIEDRILNQ ILYYLPQLYE LNRDLLKELE ERMLHWTEQQ RIADIFVKKG
PYLKMYSTYI KEFDKNIALL DEQCKKNPGF AAVVREFEMS PRCANLALKH YLLKPVQRIP
QYRLLLTDYL KNLIEDAGDY RDTQDALAVV IEVANHANDT MKQGDNFQKL MQIQYSLNGH
HEIVQPGRVF LKEGILMKLS RKVMQPRMFF LFNDALLYTT PVQSGMYKLN NMLSLAGMKV
RKPTQEAYQN ELKIESVERS FILSASSATE RDEWLEAISR AIEEYAKKRI TFCPSRSLDE
ADSENKEEVS PLGSKAPIWI PDTRATMCMI CTSEFTLTWR RHHCRACGKI VCQACSSNKY
GLDYLKNQPA RVCEHCFQEL QKLDHQHSPR IGSPGNHKSP SSALSSVLHS IPSGRKQKKI
PAALKEVSAN TEDSSMSGYL YRSKGNKKPW KHFWFVIKNK VLYTYAASED VAALESQPLL
GFTVIQVKDE NSESKVFQLL HKNMLFYVFK AEDAHSAQKW IEAFQEGTIL
//
